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Cerebral Amyloid Angiopathy, App-Related OMIM

A number sign (#) is used with this entry because cerebral amyloid angiopathy (CAA) can be caused by mutation in the gene encoding the amyloid precursor protein (APP; 104760). Mutations in the APP gene can also cause autosomal dominant Alzheimer disease-1 (AD1; 104300), which shows overlapping clinical and neuropathologic features. ... Revesz et al. (2003) reviewed the pathology and genetics of APP-related CAA and discussed the different neuropathologic consequences of different APP mutations. ... In 4 affected members of an Italian family with cerebral amyloid angiopathy, Obici et al. (2005) identified a mutation in the APP gene (104760.0019). In 2 brothers from an extensive Iowa kindred with progressive dementia and cerebroarterial amyloidosis, Grabowski et al. (2001) identified a heterozygous mutation in the APP gene (N694D; 104760.0016). ... Human APP mRNA was detected in neurons and neuronal processes, but not in vessel walls. ... Herzig et al. (2006) extended their earlier studies by developing several murine models of APP-related CAA and APP-related parenchymal amyloid deposition.

APP, APOE, PAOX, SMOX, DELEC1, TSHZ1, SCRN1, BHLHE40, TGFBR2, TGFB1, PSEN1, SERPINF2, SERPINF1, NOTCH3, SMAD2, LAMC2, CST3, CSF2, CRP, LINC01672

Abeta Amyloidosis, Iowa Type Orphanet

This subtype is due to a mutation in the APP gene (21q21.2), encoding the beta-amyloid precursor protein.
Abeta Amyloidosis, Dutch Type Orphanet

Etiology HCHWA-D is due to a mutation in the APP gene on chromosome 21q21.2, encoding the beta-amyloid precursor protein. ... Genetic testing reveals a mutation in the APP gene. Differential diagnosis Differential diagnoses include other conditions that could cause intracerebral hemorrhage such as coagulopathies, vasculitis (see these terms), CNS neoplasms, cerebral vascular malformations, ischemic stroke and antecedent trauma.
Hereditary Cerebral Amyloid Angiopathy MedlinePlus

The Dutch type is the most common, with over 200 affected individuals reported in the scientific literature. Causes Mutations in the APP gene are the most common cause of hereditary cerebral amyloid angiopathy. APP gene mutations cause the Dutch, Italian, Arctic, Iowa, Flemish, and Piedmont types of this condition. ... Familial British and Danish dementia are caused by mutations in the ITM2B gene. The APP gene provides instructions for making a protein called amyloid precursor protein. ... Additionally, the ITM2B protein may be involved in processing the amyloid precursor protein. Mutations in the APP , CST3 , or ITM2B gene lead to the production of proteins that are less stable than normal and that tend to cluster together (aggregate). ... Learn more about the genes associated with Hereditary cerebral amyloid angiopathy APP CST3 ITM2B Inheritance Pattern Hereditary cerebral amyloid angiopathy caused by mutations in the APP , CST3 , or ITM2B gene is inherited in an autosomal dominant pattern , which means one copy of the altered gene in each cell is sufficient to cause the disorder.
Abetal34v Amyloidosis Orphanet

This subtype is due to a mutation in the APP gene (21q21.2), encoding the beta-amyloid precursor protein.
Abetaa21g Amyloidosis Orphanet

This subtype is due to a mutation in the APP gene (21q21.2), encoding the beta-amyloid precursor protein.
Abeta Amyloidosis, Arctic Type Orphanet

This subtype is due to a mutation in the APP gene (21q21.2), encoding the beta-amyloid precursor protein.
Abeta Amyloidosis, Italian Type Orphanet

This subtype is due to a mutation in the APP gene (21q21.2), encoding the beta-amyloid precursor protein.

Familial Amyloid Cardiomyopathy Wikipedia

Marked axis deviation, bundle branch block , and AV block are common, as is atrial fibrillation . ... Med. 363, 1464-1470. v t e Amyloidosis Common amyloid forming proteins AA ATTR Aβ2M AL Aβ / APP AIAPP ACal APro AANF ACys ABri Systemic amyloidosis AL amyloidosis AA amyloidosis Aβ2M/Haemodialysis-associated AGel/Finnish type AA/Familial Mediterranean fever ATTR/Transthyretin-related hereditary Organ-limited amyloidosis Heart AANF/Isolated atrial Brain Familial amyloid neuropathy ACys+ABri/Cerebral amyloid angiopathy Aβ/Alzheimer's disease Kidney AApoA1+AFib+ALys/Familial renal Skin Primary cutaneous amyloidosis Amyloid purpura Endocrine Thyroid ACal/Medullary thyroid cancer Pituitary APro/Prolactinoma Pancreas AIAPP/Insulinoma AIAPP/Diabetes mellitus type 2

TTR, ALB

Inclusion Body Myositis OMIM

The authors discussed the abnormalities of APP processing, the role of abnormal intracellular protein folding, oxidative stress, and the potential role of cholesterol in the pathogenic cascade of IBM. ... Accumulation of the amyloid-beta peptide, which is derived from proteolysis of the larger beta-APP, seems to be an early pathologic event in both Alzheimer disease and IBM; in the latter, it occurs predominantly intracellularly within affected myofibers. To elucidate the possible role of beta-APP mismetabolism in the pathogenesis of IBM, Sugarman et al. (2002) selectively targeted beta-APP overexpression to skeletal muscle in transgenic mice, using the muscle creatine kinase promoter. They reported that older (more than 10 months) transgenic mice exhibited intracellular immunoreactivity to beta-APP and its proteolytic derivatives in skeletal muscle. In this transgenic model, selective overexpression of beta-APP led to the development of a subset of other histopathologic and clinical features characteristic of IBM, including centric nuclei, inflammation, and deficiencies in motor performance.

GNE, NT5C1A, APP, TARDBP, HLA-DRB1, SQSTM1, APOE, KHDRBS1, NUP62, DCTN4, GTF2H1, SDC1, CDR3, GSN, MAPT, TRBV20OR9-2, HLA-C, PLAAT4, FYCO1, MSTN, TNFRSF12A, NFAT5, CCR2, UBB, MALAT1, VCP, RBM45, AOC3, DCD, UCN2, DNAJB6, OPTN, KLRG1, MAP1LC3A, LILRB1, KDELR1, ICOSLG, SYNM, ROBO3, DDX58, CHMP1B, PABPC1, TIMP1, RRM2B, TWNK, FOXP3, KRT20, TTR, ACTB, THBS1, CST3, HLA-DQA1, HK1, H1-0, NR3C1, EPHB2, EMD, DES, CD47, TGFB1, CD38, CD36, CD34, MS4A1, CAPN3, BCL2, AOC2, HLA-DRB3, HMGB1, IFN1@, IFNG, TRIM21, AGER, MOK, PTPRC, PSME1, PSMB10, MAPK1, POLG, PMP22, MMP9, MMP1, MLF1, LMNA, IL6, IL1B, LOC102723996

Inclusion Body Myositis Orphanet

Inclusion body myositis (IBM) is a slowly progressive degenerative inflammatory disorder of skeletal muscles characterized by late onset weakness of specific muscles and distinctive histopathological features. Epidemiology IBM has a highly variable prevalence according to geographic, ethnic and age criteria. Prevalence in the general population ranges from 1:1,000,000 to 1:14,000 but a three-fold increase is observed when considering only a population over 50 years. Underdiagnosis may be an explanation for the high ethno-geographic variation. Male-to-female ratio is 2:1 on average (0.5 to 6.5:1). Clinical description IBM onset is over 50 years but may also occur earlier, in the 5th decade.
Inclusion Body Myositis Wikipedia

Inflammatory muscle disease in older adults This article needs additional citations for verification . Please help improve this article by adding citations to reliable sources . Unsourced material may be challenged and removed. Find sources: "Inclusion body myositis" – news · newspapers · books · scholar · JSTOR ( September 2009 ) ( Learn how and when to remove this template message ) Inclusion body myositis Other names sIBM Specialty Rheumatology Inclusion body myositis ( IBM ) ( / m aɪ oʊ ˈ s aɪ t ɪ s / ) (sometimes called sporadic inclusion body myositis , sIBM ) is the most common inflammatory muscle disease in older adults. [1] The disease is characterized by slowly progressive weakness and wasting of both proximal muscles (closest to the body's midline) and distal muscles (the limbs), most apparent in the finger flexors and knee extensors . [2] IBM is often confused with an entirely different class of diseases, called hereditary inclusion body myopathies (hIBM). [3] [4] The "M" in hIBM is an abbreviation for "myopathy" while the "M" in IBM is an abbreviation for "myositis". These diseases should not be confused with each other. In IBM, two processes appear to occur in the muscles in parallel, one autoimmune and the other degenerative. Inflammation is evident from the invasion of muscle fibers by immune cells .
Idiopathic Inflammatory Myopathy MedlinePlus

Idiopathic inflammatory myopathy is a group of disorders characterized by inflammation of the muscles used for movement (skeletal muscles). Idiopathic inflammatory myopathy usually appears in adults between ages 40 and 60 or in children between ages 5 and 15, though it can occur at any age. The primary symptom of idiopathic inflammatory myopathy is muscle weakness, which develops gradually over a period of weeks to months or even years. Other symptoms include joint pain and general tiredness (fatigue). There are several forms of idiopathic inflammatory myopathy, including polymyositis, dermatomyositis, and sporadic inclusion body myositis. Polymyositis and dermatomyositis involve weakness of the muscles closest to the center of the body (proximal muscles), such as the muscles of the hips and thighs, upper arms, and neck.
Inclusion Body Myositis GARD

Inclusion body myositis (IBM) is a progressive muscle disorder characterized by muscle inflammation, weakness, and atrophy (wasting). It is a type of inflammatory myopathy . IBM develops in adulthood, usually after age 50. The symptoms and rate of progression vary from person to person. The most common symptoms include progressive weakness of the legs, arms, fingers, and wrists. Some people also have weakness of the facial muscles (especially muscles controlling eye closure), or difficulty swallowing (dysphagia). Muscle cramping and pain are uncommon, but have been reported in some people.

Angioedema Induced By Ace Inhibitors, Susceptibility To OMIM

Clinical Features Blais et al. (1999) and Adam et al. (2002) reported significantly lower plasma aminopeptidase P (APP) activities in patients with a history of AEACEI. ... Measured genotype analysis strongly suggested that the linkage signal for APP activity at this locus was accounted for predominantly by the SNP association. ... There was a significant association between the -2399A allele and decreased serum APP activity in both men and women, but the APP activity was lower in men regardless of genotype. ... This haplotype was associated with decreased plasma APP activity and decreased luciferase gene expression compared to other haplotypes of these SNPs. Cilia La Corte et al. (2011) concluded that the ATG haplotype of XPNPEP2 is functional and contributes to the development of ACEi-angioedema through a reduction in APP activity.

SERPING1, KNG1, ACE, AGT

Acquired Angioedema GARD

Acquired angioedema (AAE) is a rare disorder that causes recurrent episodes of swelling (edema) of the face or body, lasting several days. People with AAE may have swelling of the face, lips, tongue, limbs, or genitals. People with AAE can have edema of the lining of the digestive tract, which can cause abdominal pain and nausea, as well as edema of the upper airway, which can be life-threatening. Swelling episodes may have various triggers, such as mild trauma (such as dental work), viral illness, cold exposure, pregnancy, certain foods, or emotional stress. The frequency of episodes is unpredictable and can vary widely. There are two forms of AAE.
Acquired Angioedema Orphanet

A rare disease characterized by the occurrence of transitory and recurrent subcutaneous and/or submucosal edemas resulting in swelling and/or abdominal pain due to an acquired C1 inhibitor (C1-INH) deficiency. Epidemiology Prevalence is unknown. Clinical description Onset most commonly occurs after 50 years of age. Patients present with white, circumscribed nonpruritic edemas that remain for a period of 48 to 72 hours and recur with variable frequency. The edemas may involve the digestive tract resulting in a clinical picture similar to that seen in intestinal occlusion syndrome, sometimes associated with ascites and hypovolemic shock. Laryngeal edema can be life-threatening with a risk of death of 25% in the absence of appropriate treatment.
Acquired C1 Esterase Inhibitor Deficiency Wikipedia

Acquired C1 esterase inhibitor deficiency Other names Acquired angioedema Specialty Hematology Acquired C1 esterase inhibitor deficiency presents with symptoms indistinguishable from hereditary angioedema , but generally with onset after the fourth decade of life. [1] : 153 C4 levels are low and C3 levels are normal. [2] See also [ edit ] Hereditary Angioedema Wheal response Urticaria Skin lesion List of cutaneous conditions References [ edit ] ^ James, William; Berger, Timothy; Elston, Dirk (2005). Andrews' Diseases of the Skin: Clinical Dermatology . (10th ed.). Saunders. ISBN 0-7216-2921-0 . ^ Markovic SN, Inwards DJ, Frigas EA, Phyliky RP (January 2000). "Acquired C1 esterase inhibitor deficiency". Ann. Intern. Med . 132 (2): 144–50. doi : 10.7326/0003-4819-132-2-200001180-00009 . PMID 10644276 . External links [ edit ] Classification D ICD - 10 : D84.1 ( ILDS D84.112) MeSH : C538173 External resources eMedicine : article/104888 v t e Lymphoid and complement disorders causing immunodeficiency Primary Antibody / humoral ( B ) Hypogammaglobulinemia X-linked agammaglobulinemia Transient hypogammaglobulinemia of infancy Dysgammaglobulinemia IgA deficiency IgG deficiency IgM deficiency Hyper IgM syndrome ( 1 2 3 4 5 ) Wiskott–Aldrich syndrome Hyper-IgE syndrome Other Common variable immunodeficiency ICF syndrome T cell deficiency ( T ) thymic hypoplasia : hypoparathyroid ( Di George's syndrome ) euparathyroid ( Nezelof syndrome Ataxia–telangiectasia ) peripheral: Purine nucleoside phosphorylase deficiency Hyper IgM syndrome ( 1 ) Severe combined (B+T) x-linked: X-SCID autosomal: Adenosine deaminase deficiency Omenn syndrome ZAP70 deficiency Bare lymphocyte syndrome Acquired HIV/AIDS Leukopenia : Lymphocytopenia Idiopathic CD4+ lymphocytopenia Complement deficiency C1-inhibitor ( Angioedema / Hereditary angioedema ) Complement 2 deficiency / Complement 4 deficiency MBL deficiency Properdin deficiency Complement 3 deficiency Terminal complement pathway deficiency Paroxysmal nocturnal hemoglobinuria Complement receptor deficiency This cutaneous condition article is a stub .

Alzheimer Disease 18 OMIM

Q170H and R181G mutant mice showed significant attenuation of APP processing compared to wildtype, with a decrease in APP-CTF-alpha levels and an increase in sAPP-beta levels, indicating that the mutations attenuated Adam10 alpha-secretase activity on APP. Crossing these Adam10 mutant mice with the Tg2576 AD mouse model showed that the Adam10 mutations increased amyloidogenic APP processing, as manifest by a shift from the alpha-secretase to the amyloidogenic beta-secretase pathway. ... Collectively, these findings suggested that diminished alpha-secretase activity of ADAM10 on APP resulting from mutations in the ADAM10 prodomain can cause AD-related pathology.

ADAM10, PSEN2

Early-Onset Alzheimer's Disease Wikipedia

This loss of brain volume affects ones ability to live and function properly, ultimately being fatal. [5] Beta-amyloid is a small piece of a larger protein called the amyloid precursor protein (APP). Once APP is activated, it is cut into smaller sections of other proteins. ... Alpha-secretase cleavage of APP, which precludes the production of Aβ, is the most common processing event for APP. 21 allelic mutations have been discovered in the APP gene. These guarantee onset of early-onset familial Alzheimer disease and all occur in the region of the APP gene that encodes the Aβ domain. ... "A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N-terminus of beta-amyloid". ... PMID 16817891 . ^ Chow VW, Mattson MP, Wong PC, Gleichmann M (March 2010). "An overview of APP processing enzymes and products" .

Alzheimer Disease OMIM

See also APP-related cerebral amyloid angiopathy (CAA; 605714), which shows overlapping clinical and neuropathologic features. ... Genetic analysis identified a mutation in the APP gene (V717I; 104760.0002). Farlow et al. (1994) reviewed the clinical characteristics of the disorder in the AD family reported by Murrell et al. (1991) in which affected members had a mutation in the APP gene (V717F; 104760.0003). ... Rovelet-Lecrux et al. (2006) estimated that in their whole cohort of 65 ADEOAD families, the frequency of the APP locus duplication was roughly 8% (5 of 65), which corresponds to half of the contribution of APP missense mutations to ADEOAD. ... Revesz et al. (2003) reviewed the pathology and genetics of APP-related CAA and discussed the different neuropathologic consequences of different APP mutations. ... Further studies indicated that suppression of PPARGC1A in hyperglycemia resulted in activation of the FOXO3A (602681) transcription factor, which inhibits nonamyloidogenic secretase processing of APP and promotes amyloidogenic processing of APP.

TOMM40, TREM2, ABCA7, APP, APOE, PSEN2, PSEN1, MAPT, SORL1, PRNP, CASP3, BACE1, GSK3B, NCSTN, IDE, IL1B, HFE, A2M, ACE, DHCR24, BIN1, ESR1, ADAM10, ADAMTS1, PGRMC1, VEGFA, ARC, CYP46A1, SLC30A4, VSNL1, PICALM, HMOX1, HLA-DRB5, IGF1R, IGF1, INPP5D, IGF2, MPO, NPY, NOS3, PLAU, PLCG2, PPARG, RELN, MTHFR, PYY, NECTIN2, SLC2A4, IGF2R, SOD2, MAOB, TF, LEP, TFAM, INSR, INS, TNF, TPI1, EPHA1, F2, ENO1, CR1, CASS4, ATP5F1A, CLU, CHRNB2, CHRNA7, MIR766, CD33, IQCK, EIF2S1, MIR505, APOC1, CALM1, MIR100, MIR146A, BDNF, BCL2, MIR375, MIR296, BCHE, MIR708, TPP1, SLC30A6, SNAR-I, DPYSL2, ACHE, CD2AP, GAPDHS, PCDH11X, CYP2D6, MIR4467, CRH, MIR3622B, BAX, AMFR, ABI3, CST3, MS4A4A, WWOX, BRCA2, FANCD2, TFF1, TAS2R64P, CTNNB1, SUCLA2, SNCA, CTSD, RNR2, NEFL, TAS2R62P, SOD1, ITPR3, ITPR2, ITPR1, FLAD1, PSENEN, TP53, CDK5R1, EIF2AK3, UBQLN1, ALG3, PIK3CG, PIK3CA, PIK3CD, SERPINA3, PIK3CB, DOCK3, APLP1, OGDH, CREB1, NOTCH1, CASP6, NGF, CCND1, FOS, DLX4, DLG4, DDIT3, RABGEF1, PEBP1, PYCARD, DAPK2, KCNIP3, CTSB, CSF2, CRMP1, CTSG, EHMT2, ENO2, ERBB4, TMED10, TERF2IP, PTK2B, FCN2, PTGES3, FGF2, ACKR1, DNM1L, SDC3, G6PD, GCHFR, ITM2B, CREBBP, MAP3K8, TRPM7, ADI1, MTCO2P12, UPK3B, ACTB, AKT1, AKT2, ANXA1, APBB1, DNLZ, STS, MIR34A, BRCA1, MIR137, C5AR1, DDR1, CAMK4, TMED10P1, MPEG1, C9orf72, ESCO1, CDCA5, PRRT2, MAP1LC3B, CAT, EHMT1, CNR2, SPPL2B, RAB9A, NRXN3, GFAP, SYNJ1, SERPINB5, CD99, MME, MNAT1, CCL2, RRAS, RPS27, RPS21, RAP1A, PYCR1, COX2, PTS, PTGS2, MTHFD1, MMUT, NCAM1, NFIA, NFIB, MAPK8, MAPK3, PRKCB, PRKCA, PPBP, MED1, NFIC, PPARA, NFIX, PKD1, NOTCH3, NRGN, MEOX2, MEF2A, SPRR2A, TTC3, GRIN2A, DENR, GRIN2B, RAB7A, LRP8, HPRT1, HSP90AA1, VIM, IDUA, UTRN, SUMO1, UBE2I, TTK, TPT1, SULT1E1, IL1A, IL6, IL12A, TSPAN6, TIE1, TGFB1, TG, KNG1, LAMC2, LGALS3, TERT, TERC, STIM1, H3P17

Alzheimer Disease 13 OMIM

For a general phenotypic description and a discussion of genetic heterogeneity of Alzheimer disease, see 104300. Mapping Liu et al. (2007) conducted a genome screen of 103 patients with late-onset AD who were ascertained as part of the Genetic Research in Isolated Populations (GRIP) program that was conducted in an isolated population from the southwestern area of the Netherlands. Genealogic information resulted in an extremely large and complex pedigree of 4,645 members. The pedigree was split into 35 subpedigrees to reduce the computational burden of linkage analysis. The strongest evidence for linkage, hlod = 5.20 at marker D1S498, was obtained at chromosome 1q21 (AD13).
Early-Onset Autosomal Dominant Alzheimer Disease GARD

There are three subtypes of early-onset familial AD which are each associated with changes (mutations) in unique genes: (1) Alzheimer disease, type 1 is caused by mutations in the APP gene (2) Alzheimer disease, type 3 is caused by mutations in the PSEN1 gene (3) Alzheimer disease, type 4 is caused by mutations in the PSEN2 gene.
Alzheimer Disease 11 OMIM

For a general phenotypic description and a discussion of genetic heterogeneity of Alzheimer disease (AD), see 104300. Mapping By genomewide linkage analysis of 466 families with late-onset AD, including 730 affected sib pairs, Pericak-Vance et al. (2000) identified a candidate disease locus on chromosome 9p22.1 (nonparametric maximum lod score of 2.97 at marker D9S741). Analysis of a subset of 199 families in which there was at least 1 autopsy-confirmed AD case yielded a higher lod score of 4.31 at the same marker. Scott et al. (2003) reexamined 437 white AD families included in the original report by Pericak-Vance et al. (2000) by considering age of onset as a covariate. Ordered-subsets analysis included continuous covariates in linkage analysis by rank ordering families by a covariate and summing lod scores.
Alzheimer Disease 6 OMIM

In HEK293 cells with an AD-associated APP mutation (104760.0008), overexpression of SORCS1 resulted in a significant decrease in amyloid-beta-40 and -beta-42 secretion, whereas suppression of SORCS1 in HEK293 cells increased beta-amyloid-40 levels. The findings indicated that SORCS1 can influence APP processing, and Reitz et al. (2011) suggested that variation in the SORCS1 gene may be associated with risk of LOAD. ... The findings indicated a role for calcium signaling in APP (104760) processing and suggested that variations in the CALHM1 gene may influence susceptibility to late-onset AD.
Alzheimer Disease 5 OMIM

For a phenotypic description and a discussion of genetic heterogeneity of Alzheimer disease (AD), see 104300. Mapping In a late-onset form of familial Alzheimer disease (AD), Pericak-Vance et al. (1997) identified linkage to a locus on chromosome 12. From a series of multiplex families affected with late-onset AD (at least 60 years) ascertained during the previous 14 years and for which DNA had been obtained, Pericak-Vance et al. (1997) selected a subset of 16 families (with 52 AD patients) to use for a genomewide screen. A second subset of 38 families (with 89 AD patients) was used for a follow-up analysis. Linkage analysis was performed using both genetic model-dependent (lod score) and model-independent methods.
Alzheimer Disease, Familial Early-Onset, With Coexisting Amyloid And Prion Pathology OMIM

Clinical Features Leuba et al. (2000) described a Swiss family whose members presented with standard clinical and neuropathologic features of Alzheimer disease (104300) and, in particular, severe neurofibrillary tangle degeneration present in the hippocampus and in several cortical areas, together with a large number of beta-amyloid deposits and senile plaques. The brain pathology of 5 deceased members of this family, from 2 generations, represented a coexisting beta-amyloid and prion protein (PrP; 176640) pathology. Frequent beta-amyloid-positive senile plaques were observed, together with senile plaques stained by the monoclonal antibody against PrP(106-126). In all 5 cases, the cerebral cortex showed spongiform changes, mainly in the superficial layers, with some degree of gliosis. Successive sections showed that both beta-amyloid- and PrP-positive senile plaques were deposited in all layers of the frontal and temporal cortex.
Alzheimer Disease 8 OMIM

Within this candidate region, 1 gene of particular interest was that encoding cystatin-3 (CST3; 604312), because it is known to be an amyloidogenic protein and is codeposited with the amyloid-beta precursor protein (APP; 104760) in amyloid plaques in the brain of AD patients. Using a covariate-based linkage method, Olson et al. (2001) showed that the APP region on chromosome 21q21 is strongly linked to AD-affected sib pairs of the oldest current age (i.e., age either at last exam or at death) who lacked E4 alleles at the apolipoprotein E (APOE; 107741) locus. ... Two-locus analysis provided evidence of strong epistasis between 20p and the APP region, limited to the oldest age group and to those lacking E4 alleles at the APOE locus.
Alzheimer Disease 2 OMIM

Onset was early in 4 other families tested; 2 had chromosome 21 APP (104760) mutations and 2 showed linkage to chromosome 14, thus representing AD1 (104300) and AD3 (607822), respectively.
Early-Onset Autosomal Dominant Alzheimer Disease Orphanet

Etiology EOAD is the consequence of either PSEN1 mutations (69%), APP mutations (13%), or APP duplication (7,5%), and exceptionally of PSEN2 mutations (2%).
Alzheimer Disease 4 OMIM

A number sign (#) is used with this entry because Alzheimer disease-4 (AD4) is caused by heterozygous mutation in the presenilin-2 gene (PSEN2; 600759) on chromosome 1q42. For a phenotypic description and a discussion of genetic heterogeneity of Alzheimer disease, see 104300. Clinical Features Bird et al. (1988) described 5 German kindreds with an autosomal dominant early-onset form of Alzheimer disease. All families were descendants of a group of immigrants, known as the Volga Germans, who came to the United States between 1870 and 1920. Their ancestors had moved from Germany to the southern Volga region of Russia in the 1760s.
Familial Alzheimer Disease GARD

There are three subtypes of early-onset familial AD which are each associated with changes (mutations) in unique genes: (1) Alzheimer disease, type 1 is caused by mutations in the APP gene (2) Alzheimer disease, type 3 is caused by mutations in the PSEN1 gene (3) Alzheimer disease, type 4 is caused by mutations in the PSEN2 gene.
Alzheimer Disease 15 OMIM

For a general phenotypic description and a discussion of genetic heterogeneity of Alzheimer disease, see 104300. Mapping Liu et al. (2007) conducted a genome screen of 103 patients with late-onset AD who were ascertained as part of the Genetic Research in Isolated Populations (GRIP) program that was conducted in an isolated population from the southwestern area of the Netherlands. Genealogic information resulted in an extremely large and complex pedigree of 4,645 members. The pedigree was split into 35 subpedigrees to reduce the computational burden of linkage analysis. They found significant evidence of linkage of AD to 3q22-q24 (AD15), in a region of 18 cM from D3S3514 to D3S3626 that reached a maximum hlod of 4.44 at marker D3S1579.
Alzheimer Disease 14 OMIM

For a general phenotypic description and a discussion of genetic heterogeneity of Alzheimer disease, see 104300. Mapping In a genome screen of individuals from an isolated population from the southwestern area of the Netherlands, ascertained as part of the Genetic Research in Isolated Populations (GRIP) program, Liu et al. (2007) found the strongest evidence of linkage for chromosome 1q21 (AD13; 611152). Approximately 30 cM upstream of this locus, at 1q25, another peak (AD14) was found (hlod = 4.0 at marker D1S218). Liu et al. (2007) noted that these 2 loci were in a linkage region spanning 1q21-q31 identified by Zubenko et al. (1998), Hiltunen et al. (2001), Myers et al. (2002), and Blacker et al. (2003). Haplotype analysis showed that the 2 linkage peaks on chromosome 1q21 and 1q25 are explained by different haplotypes, of 15 cM and 21 cM, respectively, segregating in different families.
Alzheimer Disease 12 OMIM

For a phenotypic description and a discussion of genetic heterogeneity of Alzheimer disease (AD), see 104300. Mapping Giedraitis et al. (2006) conducted a genome scan with 369 microsatellite markers in 12 extended families collected in Sweden. Age at disease onset ranged from 53 to 78 years, but in 10 of the families there was at least 1 member with age at onset of less than 65 years. Mutations in known early-onset Alzheimer disease susceptibility genes were excluded. All persons were genotyped for APOE (107741), but no clear linkage with the E4 allele was observed.
Alzheimer Disease 3 OMIM

In 2 Belgian families with early-onset autosomal dominant AD, Van Broeckhoven et al. (1987) excluded linkage to the APP locus on chromosome 21q. One pedigree contained 36 patients in 6 generations, and the second had 22 patients spanning 5 generations.
Alzheimer Disease 10 OMIM

For a phenotypic description and a discussion of genetic heterogeneity of Alzheimer disease (AD), see 104300. Mapping In an extended multiplex family, ascertained in a population-based study of early-onset AD in the northern Netherlands, Rademakers et al. (2005) obtained conclusive evidence of linkage of AD with a candidate region of 19.7 cM at 7q36. They identified a shared haplotype at 7q36 between the index family and 3 of 6 multiplex AD-affected families from the same geographic region, which was indicative of a founder effect and defined a priority region of 9.3 cM. Mutation analysis of coding exons of 29 candidate genes identified only an exonic silent mutation in the PAXIP1 gene (608254), 38030G-C in the exon 10 genomic sequence, which affected codon 626. It remained to be determined whether PAXIP1 has a functional role in the expression of AD in the index family or whether another mutation at this locus explained the observed linkage and sharing.
Alzheimer Disease 7 OMIM

For a phenotypic description and a discussion of genetic heterogeneity of Alzheimer disease (AD), see 104300. Mapping In a systematic survey of the human genome in patients with AD, Zubenko et al. (1998) identified D10S1423, located at 10p13, as a candidate susceptibility locus. The allelic associations in this survey were observed in independent samples of autopsied AD cases and controls from geographically disparate sites (Boston and Pittsburgh). Majores et al. (2000) replicated these findings by identifying an association of the D10S1423 234-bp allele with AD in an ethnically homogeneous group of 397 German AD cases and controls. Zubenko et al. (2001) described a prospective, longitudinal, double-blind assessment of the age-specific risk of AD encountered by 325 asymptomatic first-degree relatives of AD probands who carried the D10S1423 234-bp allele, the APOE E4 allele (107741), or both, after 11.5 years of systematic follow-up.

Atrioventricular Block Wikipedia

The signal travels from the SA node to the ventricles through the atrioventricular node (AV node). In an AV block, this electrical signal is either delayed or completely blocked. ... The electrical signal then travels to the AV node located on the lower portion of the interatrial septum . ... An ECG is used to differentiate between the different types of AV block. However, one important consideration when diagnosing AV blocks from ECGs is the possibility of pseudo- AV blocks which are due to concealed junctional extrasystoles. ... In a second-degree AV block, the impairment results in a failure to conduct an impulse, which causes a skipped beat. [9] Mobitz I [ edit ] Mobitz I is characterized by a progressive, yet, reversible block of the AV node. ... On ECG, there is no relationship between P waves and QRS complexes, meaning the P waves and QRS complexes are not in a 1:1 ratio. Third-degree AV block is the most severe of the AV blocks.

LMNA, GNAI2, SCN5A, KCNH2, DES, KCNQ1, PRKAG2, TRPM4, TTN, ACADVL, MTM1, KCNJ5, MMP2, AGXT, SCN4B, MYBPC3, TTR, BVES, SYNE2, SYNE1, TMEM43, KCNJ2, MMP14, CACNA2D1, GLA, GPX4, FHL1, EMD, SLC25A20, NKX2-5, CALR, TDP2, ARSD, TBX5, TRIM21, ARFGEF1, GJC1, TOPORS, ITGAM, SDS, PKD2L1, CACNA1C, SMUG1, RHOA, APRT, ARID2, HCN4, TBX6, CALCR, TBX3, SSB, SLC6A8, SCN10A, CAV1, PKD2, PITX2, CUX1, FLT4, MFAP1, GATA4, KRT5, GNB2, MIR19B1

Heart Block Wikipedia

Blockages are therefore classified based on where the blockage occurs - namely the SA node (" Sinoatrial block "), AV node (" AV block " or AVB ), and at or below the bundle of His ("Intra-Hisian" or "Infra-Hisian block" respectively). ... Therefore, most of the important heart blocks are AV nodal blocks and infra-Hisian blocks. ... Sinus rhythm (rate = 100/min) with 3:2 and 2:1 Type II AV block; right bundle branch block Sinus tachycardia with complete AV block and resulting junctional escape Following the path of the electrical signals, the places where conduction can be blocked give rise to different kinds of heart blocks: Location Name Within the sinoatrial node (SA node or Sinus node), where the heart's signals originate Sinoatrial nodal blocks (often abbreviated "SA nodal block" or "SA block", sometimes written "Sinuatrial block") Within the atrioventricular node (AV node) Atrioventricular block (often abbreviated "AV nodal block", "AV block" or AVB). ... In an SA block, the electrical impulse is delayed or blocked on the way to the atria, thus delaying atrial depolarization. By contrast, an AV block occurs in the AV node and delays ventricular depolarization. ... In SA node suppression, on the other hand, the SA node doesn't generate an electrical impulse because it is reset by the electrical impulse that enters the SA node. AV nodal blocks [ edit ] There are three basic types of AV nodal block : First-degree AV block Second-degree AV block Type I second-degree AV block (Mobitz I), also known as a Wenckebach block [5] Type 2 second-degree AV block (Mobitz II) - due to a block in or below the bundle of His [5] Third-degree AV block (complete heart block) Infra-Hisian block [ edit ] Infra-Hisian block is that of the distal conduction system.

CACNA1D, KCNJ5, LMNA, SCN10A

Ataxia With Vitamin E Deficiency GARD

Ataxia with vitamin E deficiency (AVED) is a progressive disease affecting motor control and movement. Symptoms of AVED include slurred speech (dysarthria), difficulty coordinating movements ( ataxia ), numbness in the hands and feet (peripheral neuropathy), and progressive leg weakness. ... Symptoms typically begin during childhood or adolescence and worsen with age, resulting in the need for a wheelchair by early adulthood. AVED is caused by a mutation to the TTPA gene. ... Vitamin E is important because it protects the cells of the neurological system (neurons) from dangerous molecules called free radicals. AVED is inherited in an autosomal recessive manner. Treatment for AVED includes vitamin E supplements, which will prevent AVED from developing if given before symptoms begin and may reverse some neurological symptoms if begun after AVED develops.

TTPA, APOB, APOA1, FXN, SH3BP4, ZFP36, SETX, APTX, COQ8A, COPRS, RRS1, AFP, TNF, NOS3, MTHFR, IL6, GNB3, SRR

Familial Isolated Vitamin E Deficiency Wikipedia

Familial isolated vitamin e deficiency Other names Ataxia With Vitamin E Deficiency Familial isolated vitamin e deficiency has an autosomal recessive pattern of inheritance . Specialty Neurology Familial Isolated Vitamin E Deficiency is a rare autosomal recessive neurodegenerative disease . [1] [2] [3] [4] Symptoms are similar to those of Friedreich ataxia . Contents 1 Cause 2 Diagnosis 3 Treatment 4 See also 5 References 6 External links Cause [ edit ] Familial Isolated Vitamin E Deficiency is caused by mutations in the gene for a- tocopherol transfer protein. [5] Diagnosis [ edit ] This section is empty. You can help by adding to it . ( July 2017 ) Treatment [ edit ] This section is empty. You can help by adding to it . ( July 2017 ) See also [ edit ] Vitamin E deficiency TTPA References [ edit ] ^ "Ataxia with vitamin E deficiency" . www.orpha.net .
Ataxia With Vitamin E Deficiency MedlinePlus

Ataxia with vitamin E deficiency is a disorder that impairs the body's ability to use vitamin E obtained from the diet. Vitamin E is an antioxidant, which means that it protects cells in the body from the damaging effects of unstable molecules called free radicals. A shortage (deficiency) of vitamin E can lead to neurological problems, such as difficulty coordinating movements (ataxia) and speech (dysarthria), loss of reflexes in the legs (lower limb areflexia), and a loss of sensation in the extremities (peripheral neuropathy). Some people with this condition have developed an eye disorder called retinitis pigmentosa that causes vision loss. Most people who have ataxia with vitamin E deficiency start to experience problems with movement between the ages of 5 and 15 years.
Vitamin E, Familial Isolated Deficiency Of OMIM

A number sign (#) is used with this entry because of evidence that ataxia with vitamin E deficiency (AVED) is caused by homozygous or compound heterozygous mutation in the TTPA gene (600415) on chromosome 8q12. ... Doerflinger et al. (1995) performed linkage studies in 6 new and 2 previously described families and demonstrated genetic homogeneity despite significant clinical variability. They refined the AVED position to a 1-cM interval on 8q. ... Doerflinger et al. (1995) also constructed a YAC contig over this interval to facilitate the search for the AVED gene. Molecular Genetics The tocopherol-binding protein is also known as alpha-tocopherol transfer protein and TTP1. ... Seven patients who also had low vitamin E levels were all homozygous for the common 744delA mutation in the TTPA gene (600415.0001), consistent with a diagnosis of AVED. Two patients with normal vitamin E levels were homozygous for a mutation in the FXN gene (606829.0001), consistent with a diagnosis of FRDA (229300).
Ataxia With Vitamin E Deficiency Orphanet

Epidemiology Global prevalence is not known but population-based studies have been performed and prevalence can be extrapolated at approximately 1/300,000. AVED is the second most frequently inherited cerebellar ataxia in North Africa. As vitamin E deficiency might bring protection against malaria (see this term), it could explain a higher prevalence of AVED in Plasmodium infested areas. Clinical description AVED presents generally between ages 5 and 20 years with variable phenotype and severity. ... On the contrary, in early-onset cases, the course is more severe, with an increased risk of cardiomyopathy. Overall, the clinical picture of AVED is close to that of Friedreich's ataxia (see this term). Etiology AVED is caused by mutations in the tocopherol (alpha) transfer protein gene ( TTPA ; 8q13). ... It remains unknown whether in families of index cases vitamin E preventive treatment can be administered in presymptomatic individuals to prevent development of AVED. Prognosis Even if treated, patients frequently have a poor prognosis and become wheelchair bound within 8 and 20 years of age.
Ataxia With Vitamin E Deficiency GeneReviews

Ataxia with vitamin E deficiency (AVED) generally manifests in late childhood or early teens between ages five and 15 years. ... Note: No electrophysiologic findings are specific to or diagnostic of AVED; even a severe neuropathy does not exclude AVED. ... Nomenclature AVED was first called "Friedreich ataxia phenotype with selective vitamin E deficiency" [Ben Hamida et al 1993]. ... The age of onset is similar in ataxia with vitamin E deficiency (AVED) and FRDA; however, only in AVED are plasma vitamin E concentrations low [Benomar et al 2002]. ... High serum concentration of phytanic acid differentiates Refsum disease from AVED. Inheritance is autosomal recessive.

First-Degree Atrioventricular Block Wikipedia

First-degree AV block Other names First degree heart block, PR prolongation An ECG showing a first degree AV block of greater than 300 ms Specialty Cardiology Symptoms Asymptomatic Complications Progression to second or third degree AV block Causes Fibrosis in AV node, medication, vagal tone , electrolyte disturbances Diagnostic method Electrocardiogram Treatment Avoidance of AV-nodal-blocking medication First-degree atrioventricular block (AV block) is a disease of the electrical conduction system of the heart in which electrical impulses conduct from the cardiac atria to the ventricles through the atrioventricular node (AV node) more slowly than normal. First degree AV block does not generally cause any symptoms, but may progress to more severe forms of heart block such as second - and third-degree atrioventricular block . ... The medications that most commonly cause first-degree heart block are those that increase the refractory time of the AV node, thereby slowing AV conduction. ... Diagnosis [ edit ] In normal individuals, the AV node slows the conduction of electrical impulse through the heart. ... In first-degree heart block, the diseased AV node conducts the electrical activity more slowly.

CACNA1C, CACNA2D1, TRPM4, RANGRF, KCNE5, GPD1L, AKAP9, ABCC9, HCN4, KCNE3, SLMAP, TBX5, SCN10A, SCN5A, SCN2B, SCN1B, PKP2, KCNJ8, KCND3, GJA5, GJA1, DMPK, CALM2, CACNB2, SCN3B, EHD1

Alzheimer's Disease Wikipedia

The hypothesis holds that an amyloid-related mechanism that prunes neuronal connections in the brain in the fast-growth phase of early life may be triggered by ageing-related processes in later life to cause the neuronal withering of Alzheimer's disease. [64] N-APP, a fragment of APP from the peptide's N-terminus , is adjacent to beta-amyloid and is cleaved from APP by one of the same enzymes. N-APP triggers the self-destruct pathway by binding to a neuronal receptor called death receptor 6 (DR6, also known as TNFRSF21 ). [64] DR6 is highly expressed in the human brain regions most affected by Alzheimer's, so it is possible that the N-APP/DR6 pathway might be hijacked in the ageing brain to cause damage. ... Osaka mutation A Japanese pedigree of familial Alzheimer's disease was found to be associated with a deletion mutation of codon 693 of APP. [65] This mutation and its association with Alzheimer's disease was first reported in 2008. [66] This mutation is known as the Osaka mutation. ... A β is a fragment from the larger amyloid precursor protein (APP). APP is a transmembrane protein that penetrates through the neuron's membrane. APP is critical to neuron growth, survival, and post-injury repair. [103] [104] In Alzheimer's disease, gamma secretase and beta secretase act together in a proteolytic process which causes APP to be divided into smaller fragments. [105] One of these fragments gives rise to fibrils of amyloid beta, which then form clumps that deposit outside neurons in dense formations known as senile plaques . [98] [106] AD is also considered a tauopathy due to abnormal aggregation of the tau protein .

APP, ACE, TREM2, ADAM10, APOE, PSEN1, GSK3B, HFE, MAPT, PLAU, NPY, BCL2, CASP3, BDNF, IDE, INSR, IL1B, LEP, BACE1, IGF2, IGF1R, ATP5F1A, INS, BAX, CR1, A2M, ABCA7, TOMM40, CD2AP, BIN1, EPHA1, CLU, PICALM, NOS3, PSEN2, APOC1, MPO, SORL1, VSNL1, INPP5D, NECTIN2, MS4A4A, PCDH11X, CASS4, BCHE, MIR146A, CYP46A1, DHCR24, CHRNA7, NCSTN, VEGFA, DPYSL2, PRNP, ESR1, PPARG, RELN, HMOX1, ACHE, CST3, MAOB, TNF, MTHFR, IGF1, CD33, TFAM, IL6, CYP2D6, CRH, SOD2, UNC5C, PLCG2, TF, ABI3, WWOX, SLC30A6, CHRNB2, ARC, PGRMC1, F2, CALM1, EIF2S1, HLA-DRB5, ENO1, TPI1, IGF2R, SLC30A4, MIR296, SLC2A4, MIR100, IQCK, MIR375, AMFR, SNAR-I, ADAMTS1, MAPK14, PIN1, PYY, PTGS2, S100B, PPARGC1A, NOS2, NGFR, NGF, NFE2L2, SOD1, SYP, CDK5, NGB, MIR505, GAPDHS, MME, MAP2, CTNNB1, TPP1, LRP1, IRS1, CHAT, GAPDH, MIR4467, MIR3622B, AGER, MIR766, MIR708, CAV1, NTRK2, PTGS1, APLP2, ADAM17, MFN2, DNM1, HSF1, GSR, IL33, CCR5, HSPD1, HSPB1, CIB1, CASP8, IKBKB, SERPINF1, ATP7A, MT2A, ADAM9, INS-IGF2, BCL2L2, CASP9, GAB2, PTK2B, PLCB1, ABCA1, GRN, CASP12, SQSTM1, FERMT2, HLA-DRB1, NFIC, CSF1R, APOB, MARK4, HSPG2, MS4A6A, CELF1, VCP, SYNJ1, ZCWPW1, MS4A4E, APH1B, APOC2, F13A1, EXOC3L2, PLXNA4, ADAMTS4, AKAP9, MADD, DST, PILRA, FRMD4A, LAMP1, SLC24A4, GLIS3, SPON1, CADPS2, IL34, COL18A1, TRIP4, SPI1, TGFB2, BCL3, MTHFD1L, AICDA, IL6R, DCHS2, MEGF10, SLC16A7, EPHX2, NDUFAF6, DSG2, OSBPL6, CELF2, UBE2L3, SPPL2A, MAPK7, CDH13, LAMA1, SGK1, SUCLG2, LUZP2, PTPRG, ST6GAL1, AP2A2, RBFOX1, SORCS3, TSPOAP1-AS1, TLN2, ZAP70, ALDH1A2, TCF7L2, FMN2, OTOF, EXOC4, HSD17B10, DNM1L, ALOX5, GULOP, HTR2A, AHCYL1, SDR42E2, HTR6, GTF2H1, GRM5, IAPP, AHSA1, STAG3, ALB, FARP1, TSHZ1, HRES1, AGFG2, DCAF7, SIGMAR1, BCKDK, RTN3, TPPP, HSPA4, HCLS1, HSP90AA1, G3BP1, PGAM5P1, BACE1-AS, KHDRBS1, ALDH2, CFH, HCRT, GPC6, ABCA8, GLP1R, NR3C1, TNRC6A, IL19, PARVB, DDX25, BZW2, FCN2, FGF10, GOLIM4, LINC00476, HPGDS, FANCD2, PDE7B, SIGLEC7, TSPAN16, TRPC4AP, POLDIP2, CNTNAP2, RNF19A, BACE2, UBQLN1, ITSN2, GRIN2B, ZGLP1, BCAS3, EPDR1, TMED9, ENO2, CYCS, ANXA1, EPHB2, EPO, RAPGEF6, APH1A, LARS1, EYA4, SNX9, ESR2, WAC, SLC8A1-AS1, DCTN4, RMDN1, QPCT, MTOR, SGK3, FBXL7, SZT2, GIP, ACSL6, WWC1, CLEC16A, KAZN, LINC01672, PRRC2C, COLGALT2, PLD3, HECW1, ZNF292, MYO16, DKK1, SIRT2, ACOT7, PSIP1, CLASRP, LINC00271, SIRT3, SIRT1, GFAP, NUP62, FYN, CBLC, INHCAP, TRIM51CP, GABPA, GABRA2, GABRG3, DAPK2, SMUG1, GAP43, GATA1, GCG, GCHFR, TARDBP, NCS1, GDNF, HDAC6, RAB3D, MVP, OGG1, LINC02268, LINC02325, SOAT1, ACTG2, ACTG1, SNCG, SNCA, SNCB, SNAP25, NOS1, ACTB, MEF2C-AS1, SLC6A4, NPC1, SLC6A3, GEMIN7-AS1, SLC1A2, LINC01508, LINC01725, NEFL, COX2, TNFRSF1B, STAG3L5P, TLR4, TLR2, MSH2, THY1, MT3, TH, SST, STAG3L5P-PVRIG2P-PILRB, TGFB1, TFF1, RNR2, LINC02653, LINC01712, TCF3, NRGN, CX3CL1, ELMO1, CCL2, PIK3CG, ABCA2, PLA2G1B, EIF2AK2, SERPINA3, PLG, MAPK8, MAPK1, PRKCB, PRKCA, PRKAB1, PRKAA2, PRKAA1, PMS2P1, POLD1, PTPA, PON1, PIK3CD, PIK3CB, PIK3CA, MOK, UPK3B, SORT1, ROS1, SERPINE1, REST, REN, RELB, RAC1, LINC01965, PVR, PVALB, PTPRA, LINC00972, ABCB1, LINC02008, MTCO2P12, TP53, OVCH1-AS1, MOBP, MNAT1, SLC4A8, AGT, INSIG1, AZIN1-AS1, EIF3E, FHL5, IRF2, GSTO1, ITM2B, GRAP2, LIPG, ADIPOQ, KL, MSC, LRAT, AP4M1, CCRL2, IL18, IL17A, IL12A, ST18, IFNG, ARL17B, AKT1, AIF1, KRBOX1, IGFALS, HDAC9, PHF14, IL10, IL1A, ALOX12-AS1, MICAL2, IL2RB, IL4, CLOCK, CXCL8, KCNN2, MPZL1, HERC2, VDR, TFEB, MAOA, COX10-AS1, ZNF232, YWHAZ, VLDLR, PARP1, UTRN, BCAM, UCHL1, UBB, TYROBP, AFF1, TTR, TRPM1, MMP9, AIMP2, LTBP2, KNG1, CRADD, CACNA1G, LAMC2, RPSA, CDK5R1, SUCLA2, LCN2, LDLR, BECN1, LPL, PDE5A, ABCB11, APOC4-APOC2, KHSRP, DENR, AGPS, LPA, CDKAL1, PPARA, MEIKIN, COL4A4, CRK, CEACAM22P, SCIMP, CREB1, CR1L, ZNF862, SH2D4B, CP, PNPLA7, SIMC1, GGACT, COMT, COL12A1, FAM181A, BRCA2, PPP1R37, GPR141, TENM3-AS1, CNR2, L3MBTL4, UBXN11, ACKR2, TMEM132C, CASTOR3, CLPTM1, STRADA, FNIP1, CDCA5, NLRP3, APOA1, CRMP1, KAT8, CSMD1, CLMN, PINK1, CYP8B1, AHNAK, MIR132, MIR107, CUX1, POTEM, PPP1R3B, FAS, SAP30L, ANKRD55, CTSD, CTSB, GEMIN7, EHMT1, LINC01184, CTNNA2, LINC01185, TMC5, THSD4, CCDC134, SP6, LINC01567, PDCD1LG2, SETD7, APOD, BHMG1, CSF2, HYI, BLOC1S3, TSPO, CHRNA4, CHRNA2, TAS2R62P, C3orf67, C9orf72, CCDC83, CCDC89, KDM1B, CD14, TGM6, ATXN7L1, RSPO4, ADGRF2, STH, TAS2R64P, CALHM1, RUNX1T1, PPP1R42, ALPK2, PCSK9, CAT, ANKRD31, CASP6, NKAIN3, TRIQK, CALB1, STEAP1B, CASP1, EPHA1-AS1, CAPN1, APOC4, FAM181A-AS1, NKPD1, SPRED2, CD36, SCARB1, PLPP4, MED12L, ARAP2, CHN2, CHI3L1, ACTBL2, C10orf71, MCIDAS, LRRK2, AKR1C4, ANO4, AGBL1, CEACAM20, ZNF813, RMDN3, CETP, CDR1, LINC00343, TCAM1P, APOC1P1, IGSF23, RMDN2, CDK1, SLC25A48, NKAIN2, FSIP1, CD68, BMPER, C3, CD40, CYP19A1, CRP, NIT2, ANO3, DLG4, ARHGAP20, RCAN1, WDR41, NDUFA12, STK32B, EDEM2, DSCAML1, RNF165, SH3RF1, DYRK1A, MIR29A, SYBU, AQP4, APBB1, DLX5, DBN1, PALM2AKAP2, CEACAM19, DPP4, IL6-AS1, ARVCF, CDC42SE2, DMXL1, TULP4, DAPK1, PMS2CL, POTEKP, MIR34A, VAT1L, OLR1, HDAC2, LRP8, GSN, CCL11, S100A9, COL25A1, POTEF, KLK6, BLMH, HSD17B7, P2RX7, COX8A, ABCB6, PRRT2, IL2, SORCS1, NR1I2, MAPK3, ITGAM, CASR, ATP7B, VDAC1, EGR1, PDE4A, RAB5A, SUMO1, NRG1, OXER1, NTRK1, TFCP2, ANK1, CSNK1D, DLST, APLP1, BLVRA, NFIB, IL1RN, HTT, ACAT1, PLA2G4A, NFIX, NLRP1, GPRC6A, HMGCR, PPID, LPAR3, FZD4, REG1A, MRGPRX1, LRP2, DBH, PSENEN, VPS35, ESCO1, HSD11B1, VN1R17P, SOX2, AGTR1, XBP1, MIR155, MRGPRX4, MRGPRX3, GAL, GPR151, IL13, PAEP, OGDH, GPR166P, STAT3, SET, NFIA, PLB1, AR, LGR6, DHRS11, ABCG2, C4A, KCNIP3, HSD17B13, ABCG1, TTBK1, NOTCH1, EIF2AK3, SLCO6A1, CHMP2B, RBM45, CD44, RIPK1, APBA1, GSTK1, ADNP, ICAM1, BRCA1, APCS, TNFRSF1A, NFKB1, CNTF, MMP3, KLC1, LBP, CTNNA3, SGSM3, FGF2, C4B, HIF1A, CREBBP, SERPINA1, TMEM106B, GRIA1, GRIA2, ECE1, C4B_2, GSAP, OGA, TFRC, PLA2G6, ST3GAL4, PAWR, MFAP1, KAT5, GSTM1, APRT, COX1, HP, NTF3, MIR206, FPR2, CDC42, FUS, MARK1, FGF1, PREP, C5AR1, PON2, MIR29C, CALB2, PDIK1L, SYK, S100A1, CH25H, SREBF2, COX5A, GRIN2A, VCAM1, TMED10, GSTP1, KLK8, PHF1, CXCL10, MEFV, SP1, GJA1, IGFBP3, SLC17A7, CYP3A4, FOXO3, HMGA1, SLC11A2, XPR1, MARK2, PPIF, CRHR1, SHANK3, MYC, CD40LG, CPOX, FKBP5, ANPEP, CAST, C1D, FKBP4, HSPA1A, FLT1, MIF, PLA2G2A, CX3CR1, CSF3, IFNB1, KALRN, PLTP, STXBP3, DDR1, PWAR1, PRDX2, TP63, VIM, IL23A, F2RL3, MMP14, MEF2C, TREM1, TMED10P1, NAT2, MIR342, SAMD9, RAB7A, PGR-AS1, TRPM2, EGFR, ADRB2, CLDN5, ETS2, SYT1, TIMP1, NME8, ELANE, F2R, CD59, EPHA4, CBS, MSMB, APLN, MMP2, MYCL, CALML5, SYN1, XRCC1, TGM2, EEF2, PLA2G7, ELAVL2, EDN1, TMEM97, HMGB1, MIR455, HTRA1, BPIFA2, SLC52A2, NQO1, TUBA1B, FOS, CRYAB, SLC2A1, GPR3, LGMN, SLC2A3, RIDA, FN1, ABCA4, HSPA1B, PECAM1, PTEN, HSPA8, HLA-A, PTPN1, HAMP, TXNIP, GRM2, P4HB, LIN28A, PSPH, GSTT1, CCN2, DECR1, CPLX1, BCYRN1, NES, POU5F1P4, MIR21, GRK5, POU5F1, NTSR1, MIR212, PRKN, LINC02210-CRHR1, HSPA5, DLD, DAB1, HTRA2, POU5F1P3, MIR137, DNAH8, MAPK10, GH1, SERPING1, ADAMTS2, EEF2K, GSTO2, ROCK2, NEDD9, SPTBN1, NTN1, CEBPD, GDF2, CEBPB, PWAR4, SYNM, IGFBP2, GLUL, ABCC9, ATM, PSPN, PTPRC, MIR29B1, RANBP9, NDRG2, CNR1, RTN4R, PTBP1, AQP1, PDK1, MIR106B, PDE4D, ARNTL, PRDX1, ADM, RENBP, POMC, PTPN4, MS, PDGFRB, P2RY2, MIR142, PDE9A, SSTR4, KLK3, BCL2A1, C2, SRPK2, NFATC2, ADCYAP1, LRRTM3, PLD1, NUBP1, MIR424, ATF4, BSG, MIR29B2, PPY, BMP4, TBP, SLC18A3, POLB, NOTCH3, SLC18A2, NPTX2, MTR, SI, MIR222, SH3GL2, ND2, NR4A2, SELENOP, CXCL12, CCL5, ATXN1, CALM3, ITGAX, IFNA13, DISC1, OPTN, HTR1F, HTR4, WNT3A, COL11A2, C20orf181, IFNA1, KEAP1, HDAC4, KLK4, SEMA6A, LRRC4, CRTC1, IL9, DAO, ALOX15, AGTR2, IDO1, SLC25A27, ABCG4, CD55, APOA4, MCOLN1, REM1, ATCAY, EBPL, HSPB2, HSPA9, PLK2, GAD1, NANOG, DCX, COASY, UBE2K, DDIT3, TREML2, APBB2, MAP1LC3B, SRRM2, GZMB, FXN, HNRNPA1, HPSE, RAB10, CIP2A, FOLH1, STIM2, DIO2, MMP24, CEBPZ, GBA, CDR2, ITPR3, CDKN2A, MELTF, SLC30A3, ADRA2B, FTO, FNDC5, GGA3, XPNPEP1, VGF, NR1H2, UGCG, MFGE8, MGAT3, CXCR4, TLR9, APOC3, GPT, ELK3, NEAT1, ADORA2A, MMEL1, TRPC6, EIF4E, CAMK2A, MS4A6E, SRR, HSPA14, IRS2, MGAM, C1orf52, HDAC3, PABPC4, ACKR3, LGALS3, FAM20C, WNK1, DRD4, CYP2C9, MBTPS1, DRD1, LRP6, GRK2, CYP2B6, OGT, LIPA, AD11, GORASP1, PTGDS, SPEN, MIR200B, NPTXR, DNMBP, MIR200A, NCOA6, MIR181C, RBP4, RELA, OPN1LW, EFHD2, MIR188, TPH1, HNRNPA1P10, CTNNBL1, SLC40A1, PNO1, CHCHD2, SDF4, RETN, GOLM1, PPP3R1, PYCARD, PAG1, CCR2, DDIT4, RCBTB1, SBNO1, PPARD, CD274, PCBP4, ACE2, PROS1, PRND, PPP1R15A, CIZ1, MIR26B, TPSG1, GGA1, CFAP97, MAP2K1, AATF, SHANK2, PRL, RBMS3, LOC107987479, MAP2K2, PAXIP1, CHCHD10, SBNO2, PTGES, SPHK1, LPAR2, PPIG, NRXN3, MED23, SPP1, MAPK8IP1, BAG3, APBA3, TAP2, PRDX6, CARTPT, SNAP91, SV2A, MALAT1, MAK16, SYVN1, GDF11, TAC1, TAT, SLC6A2, TRPV1, CISD3, TPT1, TSC2, TM7SF2, TXN, UBE2I, TLE1, TIMP2, XK, CNTN2, TGFBR2, YY1, GOLGA6A, ANP32A, TAM, TERT, DCP1B, TNFSF10, PPP1R1B, GPHN, RGS2, ADAM30, SAA1, METAP2, IMMT, SDS, ADAP1, RYR3, ECHDC3, RYR2, RXRA, SCD, RPS6KB1, CIT, RPS6, CTXN3, LMTK2, NLGN1, ROCK1, RGS4, ATXN2, SRL, STUB1, SHBG, LILRB2, AKR1A1, OLFM1, SKIL, SLC9A6, CREB3, PITRM1, SCGN, CXCR6, OCM, RIN3, SGCA, SFPQ, NCKAP1, CPLX2, TP73, EDAR, CCL3, NPS, BEST1, HPS1, CXCL1, GLO1, LIF, CDH1, LHCGR, CDK4, PCNA, PCK1, L1CAM, GPR42, GPX1, GRB2, ANGPT1, ANGPT2, CETN1, MYD88, GLB1, AKT2, LMNA, DNMT3B, TSC22D3, CD38, PER1, CD69, DRD3, LOX, CD74, LMNB1, DNM2, GAS6, AVP, GC, DMRT1, SARDH, GRIN1, ANXA5, BACH1, P2RY1, INPPL1, CSF1, CS, NEFM, NTS, APEX1, STS, HTC2, NEUROD1, NPTX1, NPPA, ATF2, HTR2C, ARRB2, IGFBP7, HMGCS2, CLK1, CKB, APBA2, CYP17A1, GSTM3, CHGA, CYBB, JUN, CTSS, ORM1, ITPR1, CHRM1, CHRM2, OPRK1, OPRD1, CTRL, HK1, ADRB1, LAMP2, CASP2, EDNRA, PLD2, CAPN2, F2RL1, ACO1, ERBB4, FAT1, FGFR3, CALM2, BRS3, CALCA, CAD, EGF, CASP4, FCGR3B, FDPS, LYZ, FCGR3A, FLNA, MECP2, FABP3, ADRA1A, PLXNA2, MBP, FAAH, ENPEP, F12, BAG1, MEOX2, HOMER1, ITGB2, DBA2, ITGAL, ITGB1, AIM2, AZIN2, CD80, ITIH4, CD46, VIP, CHRNA3, ATG5, TREML1, MCL1, GPRASP2, VWF, APOA5, TMEM119, KLF4, SOCS6, WNT1, XBP1P1, FOXQ1, C3AR1, OPN4, USF1, C1QA, CXCR2, VPS26A, MOGAT3, CCR3, IL6ST, IL5, IL1RAP, LMF2, IL1R1, CREB3L1, UNG, MCU, CLSTN3, SNPH, IL9R, NPEPPS, NAPSA, USF2, MEF2A, ING1, CGB8, FTMT, CHM, VAV1, IMPA1, C1R, ILK, ADAMTS3, IL16, MAP3K5, IL15, GDF15, CGB5, CA2, KCNB1, TSPOAP1, SMAD2, DPPA2, SGO1, LIG3, IFNL3, TNK1, CP20, APCDD1, HSD17B6, CDKN1A, TTBK2, CDKN1B, SLC2A14, CFLAR, STMN1, LIPC, TAB3, CHIT1, BRAP, SPARCL1, MLKL, PTCRA, CD47, LGR5, CD8A, CCT, NR4A3, USP9X, MSRB3, CDR3, CCK, LNPEP, CASP7, CHRFAM7A, CAMP, PER3, YES1, CGA, MARK3, CGB3, SYNGR1, CALCR, IL1RL1, ARHGEF2, PER2, SLC33A1, TPH2, CHEK1, RAB7B, NOG, MBL2, CFL2, HSPB6, AHSA2P, SLC30A1, CD200R1, SOCS3, KDR, KIF5A, HAP1, CALR, CES1, TRPA1, HSPB3, WASF1, SLC32A1, ARHGEF7, CAMK4, COL3A1, H3P40, SCRN1, PTCD1, SPHK2, ATN1, PPIL2, POU2F1, FOSB, GCA, FLT4, SH2B1, APPL1, DNMT1, FLG, FOXO1, DUSP1, DUSP6, HHAT, HSPB8, E2F1, PLXNA3, DOCK2, PNPLA2, ADI1, GMFB, GPI, GPC1, KIF21B, NMNAT2, TRIB3, ALS2, DLG2, DLG3, GLS, PDSS2, ASTN2, MCF2L, GLI2, KIDINS220, CBLIF, SYNE1, DMD, GGT1, FKBP1A, SIT1, SV2C, GDE1, FOXP3, ASCC1, TMED7, FIS1, PRLH, CRYL1, ADIPOR1, LSR, F11, MBL3P, SIRT6, TRMO, NRN1, LCMT1, PRRX2, ERN1, BIN2, UBR5, HEBP1, GEMIN4, PDCD4, TBK1, SLC25A38, FGF14, PCSK1N, TRPM7, DLL1, FLVCR1, AHI1, SETD2, ELK1, IL22, NCAPH2, ELN, PADI1, BPTF, NRBF2, FABP5, EP300, PLA2G3, GRHL3, CXCR3, NAV3, SIRPB1, FLOT1, MET, KCNMB2, CRISPLD2, ARHGAP24, HNMT, SNX27, NPL, BHLHB9, TRIM13, HMOX2, KLF2, CSNK1E, LPAL2, CPQ, PPP1R2C, RAPGEF3, TET1, CRYZ, SORBS3, CTBP1, BCL2L11, COL17A1, NCAPD2, COX10, UBASH3B, NR1I3, ACOT8, PTPN5, PPP1R9B, TOM1, MINDY4, CPE, HTR7, NR1H3, HTR1B, HTR1A, LRPPRC, PDIA6, RHBDD1, NAA25, HLA-C, TPX2, BCAN, ADAMTS13, MOAP1, TNMD, GRIA3, NEUROD6, CHEK2, PADI2, HRH3, PHB2, SIL1, MGLL, FFAR1, GADD45A, MMRN1, DEFA1, IL21, NLRC4, GPR17, AZI2, HHIP, CTF1, HCRTR2, HLA-B, CTNND2, HHEX, HGF, CTSG, HDAC1, CTCF, DHX40, PTGES3, STIP1, CTSZ, CXADR, CARD14, CYP1A2, PDE10A, LILRB1, EHMT2, PDIA2, UMOD, ANGPT4, MIR339, SYN2, MSD, ACP3, APEH, ST8SIA1, AZU1, PI4KA, NCAM1, MIR144, SMIM10L2B, MSI1, NAP1L1, PRSS3, PEBP1, MASP1, SIM2, TIA1, MIR15B, ATD, RPL29, ABCC1, NCAM2, MIR125A, TLR5, SERPINF2, TNFAIP1, CXADRP1, MAPK9, ZFHX3, GGTLC4P, AD10, SGCG, MIR451A, CDR1-AS, TPTEP2-CSNK1E, MIR384, ITSN1, CBSL, MPZ, NFATC4, PKM, NCL, NTF4, LOC643387, SLC1A3, APOA2, THAS, PSMB6, SERPINB6, PSMB9, RHOA, ARMCX5-GPRASP2, SMPD1, REG3A, ATP4A, MIR193B, RFC1, NOTCH4, SLPI, PGF, AEBP1, MIR214, MIR219A1, SLC19A1, MIR22, PCSK1, ALPP, AMD1, MTNR1A, TGFBR1, COX3, ATP12A, NM, ADD3, PSD, TGM1, ARR3, NPM1, PAK1, TMED7-TICAM2, PNP, MIR195, MTHFD1, ADH1B, AMPH, ND4, AMD1P2, ARG1, SULT2A1, RRAS, PDE7A, TTPA, TYK2, TXNRD1, PPP1R1A, PPP1R10, SPG7, SPAST, RAB4A, PPP2CA, OTC, PPP2R2B, MMP1, ARMS2, RAB3A, GGTLC3, RTL1, P2RX4, ST13, SPARC, ALAS1, PPP3CA, NEFH, SEL1L, TYR, RAB6A, MICB, PPIA, CCL4, BST1, TICAM2, BNIP3, MIR326, OPRL1, PON3, BMP6, OPRM1, AHSG, H3P17, SDC2, AGRN, TYRP1, PPP1CA, BMI1, TYRO3, PNMT, DEFA1B, GGT2, ORI6, SMIM10L2A, CISD2, ARSA, EIF2AK4, PRKAR1A, LRP1-AS, SRSF2, MIR98, MIRLET7B, CD200, PDCD1, RAP1A, GGTLC5P, CCND1, ANXA6, FXYD1, S100A6, NFATC3, PLK1, ABO, PTGER3, APC, S100A12, ASL, HSP90B2P, SETMAR, PRRX1, PZP, STAT1, ODC1, CFB, CDNF, ZBTB4, PARK16, SUGP1, DIO1, SORCS2, MAGEE1, ALDH1A1, MIR1306, DES, DIAPH1, LSM2, MIR1229, XPO5, HCN3, CFD, MIR664A, KIF17, WDR48, MTRNR2L12, PRX, DHFR, EPG5, SEPTIN1, FAS-AS1, RNF213, MIR320E, MIR1908, HECW2, LINC00672, NUFIP2, ABCD1, DLG1, QRFP, ZNF410, AOC2, NBEAL1, CYP11A1, OPN1MW2, AD6, P2RY12, NMNAT1, DEPTOR, TNS3, CYP2D7, FAM72A, NUCKS1, CLEC7A, CYP26A1, ARAP3, GREM2, CDKN2B-AS1, CYP2J2, UBE2Z, MIR1246, TSPY3, MIR632, CTSK, GTDC1, CTSL, MIR650, MIR660, SNORD118, TNFAIP8L2, LYNX1, MUL1, PAGR1, CYLD, MAPKAP1, APOF, PDCL3, CYP2C19, NOC3L, CYP27A1, DPEP2, MFT2, PROK2, HPSE2, AD14, AKR1C2, ALPI, TRPV4, NTN4, PRM3, PDF, JAM2, ALOX5AP, TSPY10, DEFB4A, DEFB4B, ALOX12, PTBP2, DCN, NECAB3, FKBPL, NEUROG2, DGKQ, SLC25A4, MIR873, MIR301B, CENPK, DAXX, GFRA4, GOLPH3, ERVK-6, MTUS1, DBI, MIR937, ANG, ACE3P, SOD2-OT1, ANK3, DRD2, ZNF608, NAT10, DYM, LOC102724334, TRIT1, EIF4G2, TET2, EIF5, SERPINB1, ELAVL4, PDP1, ACO2, THRA1/BTR, UGT1A1, CCHCR1, CPVL, SMOX, TOLLIP, TERF2IP, SNTG1, EMP1, LOC102723407, EIF4EBP1, MIR6845, EIF2S3, ADCY2, NUDT11, EGR2, MSTO1, ADARB1, SLC6A15, ADA, TAPBPL, TESC, MIR6840, ACVRL1, FOCAD, EIF4A1, CASZ1, QRICH1, PGPEP1, EIF4A2, NDE1, ASIC2, CTTN, ACADVL, GSKIP, LNCRNA-ATB, ATP6V1H, H3P7, TDP2, ERBB2, CINP, ZCCHC17, H3P13, DTL, GPRC5B, ERCC1, DCDC2, NAT8B, GULP1, H3P23, ERG, H3P28, H3P11, PPIL1, STIN2-VNTR, NANS, EPHA8, H2BS1, POLE3, ACACA, SLC29A1, FXYD6, LRP1B, CST12P, SIRT1-AS, INPP5K, MSRB1, ARID4B, EPOR, ABL1, AAVS1, NR2F6, ERVK-32, LOC110366354, MNS16A, EFNA5, SLC47A1, ALAD, EEF1A1, SNHG19, MICA, DNTT, SOX21-AS1, DOCK3, DPYSL3, MIR626, XAB2, MFF, DUSP22, ARNTL2, SPPL2B, MCCC1, TMX2-CTNND1, ANKS1B, DPYSL5, FXYD6-FXYD2, BARHL1, DSC1, TWSG1, TLE5, DNASE1, DNA2, OCLN, NLN, AMIGO1, AHR, PLEKHG5, SLC24A3, SPC25, TTC7A, PELI1, JAG1, TMEM159, RTN4, APMAP, CD177, CAMK1D, PLAAT1, NR0B1, TIGAR, P2RX5-TAX1BP3, PARD3, GKN1, ADH6, INAVA, CDK5RAP2, OGDHL, LINC01080, ATF7IP, IPO9, VAC14, DVL1, PPP4R3A, OPN1MW3, EBM, OTUB1, SOX6, SLC30A10, SMPD3, MEG3, PLIN2, FBXW7, TDP1, ADORA1, DSC3, ACSS2, BTNL2, KIAA1217, ZNF253, CFC1, MIR4668, DSG1, APOM, MYO5C, MIR4487, NOTCH2NLC, USE1, SELENOS, GDNF-AS1, DSPP, ADCY10, ADRA2A, ZNF415, LINC-ROR, NARS2, CSF2RB, MIR616, MIR20A, CDC25C, PROM2, ATP6V1E1, IL23R, GLIS1, PM20D1, PHF13, CDH2, ZNF569, MIR191, CDK9, MIR192, PRIMA1, CDKN2D, MIR196A1, OR2AG1, LAYN, PIWIL4, MIR19B1, GPBAR1, CDC25B, GDF7, ZDHHC15, MIR139, CD63, SGMS2, MIR140, TMPRSS6, RHBDL3, AVPR2, MIR15A, CBLL2, MIR186, PRUNE2, AMOTL1, CD81, MIR18A, SLC2A12, CDA, MIR181A2, ATP5PO, SESN3, ATP6V1B2, UBR1, ATP5PF, PPME1, MIR224, LYZL4, KCNH8, MTERF4, MIR23A, CPO, ACMSD, MIR23B, BHLHE23, MIR25, CFL1, OSCAR, SPNS2, SEZ6, SLC38A10, MSI2, CFTR, MIR27A, MIR223, ALDH7A1, MIR221, SELENOM, ATP5MC2, CACUL1, HECTD2, SREK1, CTCFL, CBLN4, CDSN, ATP5MC1, DEFB104A, OCIAD2, MAGEC3, MIR210, CEACAM5, CECR, PPARGC1B, ATP5F1B, IL31RA, GNPDA2, SCARB2, NSMCE1, SOCS4, UBE2L1, BNC1, CACNA1C, SLC25A20, SERPINA13P, BLM, SREK1IP1, MIF-AS1, C20orf203, SYPL2, ZNF763, CCL4L1, BID, BGN, ZSCAN1, ZADH2, SMIM20, MILR1, PGP, GOLGA6L2, TMEM189-UBE2V1, TMEM189, IL31, C4BPA, BTK, AMIGO2, HCN1, NHLRC2, ATP9B, SBSN, BMP1, OSTN, C5, CFAP410, BARHL2, NANOS3, C9, STING1, GADL1, ARMH1, VPS51, HCAR2, CAPG, LINC00639, TMEM201, LIN28B, CD5L, MIR127, CD19, KIF6, MS4A1, MS4A3, HYLS1, STOX1, FOLH1B, OR8J1, TRIML2, CD28, KHDRBS2, GAPT, CENPV, KLHDC8B, MIR134, CD86, PIKFYVE, SLC29A4, CCNC, KRIT1, PTF1A, DAOA-AS1, BDKRB2, HCA1, BRD3OS, ASPM, BCS1L, SGMS1, BCR, MIRLET7D, MIR122, RUNX1, ANKK1, BCL6, PHYHD1, BAK1, MIR10A, EBF3, CCKAR, MIR28, FRMD6, MIR613, ADAMTS10, TMEM175, XIAP, MAF1, BIRC3, SLA2, ANTXR1, ASCC2, CRHBP, EVA1A, QRFPR, MAGT1, NCALD, LOC646506, ROPN1L, L3MBTL2, GMNC, SCFV, CSE1L, RNF146, PHF6, HOOK3, BRSK1, MBOAT4, COX15, MIR497, MFSD2A, MIR501, ACCS, ARG2, FAM126A, CPB1, CPN1, ECSCR, MAP1LC3A, MIR484, AQP9, CPS1, SNORD35B, CPT1A, ABLIM2, FASLG, NETO1, DOCK8, RNFT2, C1QBP, TM2D3, ASRGL1, PTGES2, PANK2, MIR590, SCD5, CSNK2A1, VCAN, ZC3H14, CSPG4, CTBS, MIR592, MIR598, CAMKMT, CTNS, SLTM, PTCD2, CTNND1, MIR603, NUBPL, WDR26, SPHKAP, GSTT2B, TMEM163, NCF1, LBH, SPAG11A, SFTPA1, CSF3R, ZNF436, CSN2, NDFIP1, MIR545, SLC44A4, SLC19A3, FAM72B, AIRE, IQCJ, CSNK1G2, DNAJC5, CSNK1G3, LINGO1, ATG4C, ATP2B4, MIR346, SERPINC1, CISH, ASPA, CLC, UCN3, TMEM54, ASS1P1, CLCN3, NACC1, ASIP, STX1B, IFT43, MIR133B, MIR151A, CLK2, TP53INP1, MIR330, MIR335, MIR338, MIR93, SLC26A7, OMA1, CHGB, PLD4, TDRD9, CHD1, MIR299, ATIC, ATHS, H4-16, LRIG3, EXOSC6, CHRM3, MIR30B, MIR30E, AGAP2, MIR31, MIR34C, MIR9-1, GRIN3B, GRIN3A, ASAH1, MIR369, H2BC12, KPRP, LRSAM1, MIR429, H4C15, SHF, GADD45GIP1, COL11A1, ZNF628, MIR431, HNP1, NAV2, MIR409, SLC31A1, RPPH1, SNORD14E, SNORD14D, SNORD14C, SNORD14B, COX6B1, MIR485, CNTN1, DNM1P33, CNTFR, CHRDL1, CLN3, MIR361, MYOCD, PRDM6, DNER, SPECC1, MIR377, CLN5, EXOC3L4, CNP, MIR425, ARRB1, ZNF804A, BDNF-AS, NLRP12, CCR6, ABCC2, DEFB104B, LRRC15, POU3F4, HOOK1, TERC, NAT1, MCM2, EZR, MDH1, VEGFC, MDH2, MDM4, MEF2D, UVRAG, UROD, UQCRC1, UGT1A, SLC35A2, UCP2, UBTF, UBP1, MID1, UBE3A, UBE2V1, CXCL9, ATXN3, UBE2D2, UBE2A, UBC, MAP3K10, MC1R, WARS1, WAS, ZMYM2, MANF, SCG2, FZD5, SMAD7, MAG, MAP3K12, MAP1A, MAP1B, ZNF236, ZNF224, ZNF217, RNF112, WEE1, MZF1, ZIC1, MARS1, MAS1, MAT1A, MAT2A, MAZ, XIST, WT1, WNT2B, WNT5A, UBA52, KMT2A, MLLT3, THBS1, TLR3, TLE3, MSH3, TKT, TIMP4, TIMP3, MSR1, MSRA, THRA, THOP1, THBS4, CYTB, MRE11, NUDT1, TGFBI, TGFB3, ND1, TFF3, TFDP1, MTNR1B, MTRR, TRNL1, MUC1, TERF2, TSPAN7, MRC1, TWIST1, TRAF2, TUBA4A, NR3C2, TTN, TSPY1, TSHR, TSG101, TSC1, MMP7, MMP8, TRPC1, TRH, NR2C2, TNFAIP6, MMP13, TPM1, MOG, MOV10, TP53BP2, TP53BP1, MPG, TNR, TNNI3, MPI, MPST, SLBP, REEP5, DEK, SNX3, TNFRSF6B, RAB11A, LDHA, LEPR, LGALS4, LGALS9, GPAA1, RNMT, GBF1, ADAM19, URI1, TRADD, LCK, B3GALT4, LIFR, LIG1, SOCS1, NUMB, LIMS1, AOC3, PDE8B, USO1, TNFSF11, STK16, LCT, CES2, KMO, KLRC1, BRSK2, KCNQ1, KIR2DL2, NOL3, ATP6V0E1, SELENBP1, USP13, KLKB1, CDK5R2, RAB29, MBD2, KIF11, TMEM11, ENDOU, EIF2S2, TAX1BP1, NAE1, KRT14, KRT18, LAMC1, LBR, PROM1, LCAT, SOCS2, PRKRA, DEGS1, DDX39B, PABPN1, EOMES, BAP1, LTF, H4C9, COLQ, DYSF, CHAF1B, LYN, NRIP1, COIL, SLC7A5, AD5, H4C1, FGF23, ADAM12, BRD3, PSCA, ARHGEF5, TFPI2, FZD3, GHS, M6PR, MARCKS, SMAD1, LTC4S, H4C4, BHLHE40, IRS4, MAPKAPK5, LMO4, LOXL1, CST7, DDO, DGKZ, GAS7, PIK3R3, PKP4, PPFIA1, LRPAP1, SORBS2, H4C6, CUL4A, GNPAT, LTB, H4C14, H4C13, H4C5, H4C2, H4C8, H4C3, H4C11, H4C12, TERF1, MUC4, KCNMA1, TDO2, PCP4, CDK18, RBM3, RBL2, RBBP6, RB1, RASGRF1, RASA1, RARRES2, RAN, RAF1, RAD52, PCYT1A, RAD23B, RAC2, PDB1, RAB27B, RAB27A, PDC, PDE2A, PURA, PDGFB, ENPP2, PDYN, PTPN13, PC, PAX6, PARN, RPL15, P2RX1, S100A8, P2RX3, P2RX5, P2RY4, RREB1, RPS23, RPS21, RPS6KB2, P2RY6, RPS3A, RPL13, RET, RPA1, PAFAH1B2, RORA, ROM1, SNORD15A, BRD2, RNASE1, RHO, RHD, PAK3, TRIM27, PTPN11, PENK, PTN, PMM2, PLAUR, PLCL1, PLEK, PRKCE, PRKCD, PLP1, PRKAR1B, PRKACB, PRKACA, PLXNB1, PML, PRG2, PLAT, PMP22, PRB1, PPT1, PPP2R5E, POLG, PPP2R1A, PPP1CB, PPL, PPIC, PPIB, POR, MAP2K3, PLAG1, PFDN5, PSMD2, PFKFB3, PTGER2, PTGER1, PGD, PTGDR, PTCH1, PGR, PHB, PSMD9, PSMD7, PSMD3, PSMB2, PITX2, SERPINE2, SERPINI1, KLK10, PIK3C3, PIK3R1, KLK7, PIK3R2, PRS, PROS2P, PIN4, PROC, S100A10, OXT, OXA1L, SQLE, STAR, ST14, ST2, NDUFA6, SSTR3, SSTR2, NDUFA9, NDUFB8, SRM, SRF, NEDD4, SEPTIN2, STC1, SP4, NEU1, SOX5, SOX3, SOS2, SOS1, SOD3, NFE2L1, NFKB2, SNRPG, SNRNP70, NDUFA5, STIM1, NME1, MYH9, TRBV20OR9-2, TCP1, TCN2, MMUT, MUTYH, TCF4, ELOC, TBX2, MX1, MYH6, TARBP2, MAP3K7, STK11, MYO6, TACR2, NACA, VAMP2, VAMP1, SURF1, ABCC8, SUOX, NDP, STXBP1, STX1A, NINJ2, NME2, SAA2, OMP, SFTPC, TRA2B, SRSF6, SRSF5, SRSF3, SRSF1, SFRP1, OCA2, MAP2K4, ODF1, SELE, OPA1, OAS3, CXCL11, CCL21, CCL20, CCL19, CCL8, CCL1, SCP2, SCN1A, ORM2, OSM, TSPAN31, OAT, SGSH, SUMO2, SLC8A3, SMPD2, SLN, SLIT3, SLC22A5, SLC22A2, NQO2, SLC18A1, SLC16A1, SLC12A3, SLC11A1, SLC10A2, SLC8A1, NUP98, SLC6A12, NPHP1, SLC6A1, SLC5A2, NRCAM, NRDC, SLC1A1, NRF1, PMEL, YBX1, NT5E, NAT8, SEMA5A, ESRRA, RAB31, MACF1, HEY2, BRD4, TRAM1, CBX5, ANGPTL2, OPN1MW, GRIP1, KCNH4, MSTN, GFER, GFRA1, SIRT5, COTL1, GFRA3, GHR, ZNF629, UBR4, GHSR, WASHC4, GLI1, NUP160, CLUH, GLI3, SCFD1, KCTD2, CLCF1, SEC14L2, NR5A1, SLC24A2, PRPF6, TFIP11, MAFF, EID1, RAB38, FSHR, TMEFF2, PLA2G15, SLC7A11, FTH1, SNHG1, TSPAN15, GAST, ACKR1, G6PD, GAB1, NTSR2, GABBR1, GAD2, GALNS, DDAH1, PADI4, GART, NBEAL2, GMPR, PLEKHM2, WDHD1, GPR39, CARD8, ARHGEF15, AAK1, SYNPO, GPX4, ECD, PARK7, KLF8, TREX1, WIF1, WDR45, ATF6, CORO1A, TBC1D8, SLC7A9, GRIA4, FAF1, GRIK4, RER1, GRM1, STMN2, RAPGEF4, ADRM1, MSRB2, RAB3GAP1, GNA12, ZNF423, ATG4B, UBXN4, RCOR1, SEPTIN8, STAB1, GNAI1, MAPK8IP3, GRAMD4, GNB3, NFASC, KIF1B, GOLGA2, GPER1, SETX, GOLGA4, PDZD2, SAMD4A, KDM1A, GPM6A, RAB21, GPR6, P2RX2, GPR20, SNW1, FRK, FBXO7, BRI3, SNX12, SOCS7, CD209, FABP6, TBX21, NOP53, FABP7, SLC2A8, UBQLN2, A1CF, PSAT1, FANCG, HOOK2, DELEC1, FASN, SNX8, NPC1L1, BLNK, MS4A2, FCGR1A, FCGR2A, MYLIP, SCG3, DROSHA, TMEM230, NOX4, PCA3, SPCS1, VRK3, ETFA, SLC25A37, TLR8, SLC22A17, ECSIT, CD320, EZH2, DNAJC27, CLEC1B, NT5C3A, MZB1, F2RL2, HP1BP3, F3, F9, IRAK4, SAR1B, UTP11, F13B, SH3GLB1, SIDT2, SHANK1, TRAT1, F11R, RGCC, TMEM176B, NOCT, FBXO2, NPTN, TPK1, VCX, GREM1, FKBP1AP2, FKBP1AP3, AGO1, SEZ6L2, FKBP1AP4, FGF21, CLDN17, NOC2L, SND1, FOXM1, EPC2, ATRNL1, LRP10, FLNB, FMR1, POU2F3, TXN2, FBXL2, FOLR1, FOLR2, FKBP1AP1, B3GAT1, IGHV1-68, TNFRSF21, FEB1, FES, FGF9, RABGEF1, PRPF19, FGF13, FGFR1, FGFR4, PDLIM3, RND1, KLHL20, COQ2, CACYBP, HCAR1, FHL2, VPS4A, IL37, GLS2, NAAA, CYTH4, DKK2, DKK3, BBC3, SDCBP2, GRM3, IL24, SPAG9, CXCL2, PCLAF, IGFBP1, ACAP1, IGFBP5, SART3, KDM4A, IGHG3, SDC3, SH3PXD2A, RGS6, SNCAIP, TCL1B, IL4R, IL7, BCAR1, CCL4L2, CXCR1, BAG2, IL12B, BAG5, TMEM59, TBPL1, GAL3ST1, AKAP5, STX8, PIEZO1, BMS1, PTDSS1, IDH1, SH2D3C, GNE, SH2B3, IRF8, SRA1, TANK, KCNE3, HNRNPDL, CCS, NUP153, MED12, HS3ST1, TOMM20, RBM8A, IDH2, CFI, SV2B, TECPR2, IFI27, TOMM70, KIAA0319, IFIT3, IFNAR1, IGBP1, INSRR, PCYT1B, IL27RA, CCNE2, NOLC1, TIAF1, JUND, ZMYM3, KCNC4, KCNJ13, HGS, SYNGR3, ATG12, CBFA2T2, RABEP1, P2RX6, RAB11B, SLC16A3, SLC16A4, ATP6V0D1, RGN, USP10, USP2, USP14, DNAJA3, CLDN1, CLDN8, ARTN, JUNB, GPR50, PICK1, ITPKB, IRAK1, HOMER2, IREB2, IRF3, IRF6, IRF7, ITGAV, CYP7B1, ITGB3, NRXN1, SLC22A8, ITPR2, AIMP1, JAG2, ITGBL1, LHX2, SLIT2, TAOK2, CD163, JAK2, GPR37L1, PIWIL1, MAPKAPK2, PDLIM7, IARS1, TNC, IL18BP, CCT2, HCK, NRG3, USP39, DCTN6, CD226, HDC, HDLBP, CAMKK2, HIP1, TXNRD2, NPC2, SLC35A1, HBG2, PRDX4, ZNRD2, HYOU1, HLA-DQA1, SEMA4D, HLA-DQB1, NXF1, HLA-DRA, ATP5PD, COG5, GPNMB, CHL1, HAS3, FAM3C, GYPA, GSK3A, COPS5, GSM1, GSTM2, EBNA1BP2, PRSS21, PRDX3, GSTZ1, GTS, GUSB, C1QL1, GYPB, HAS1, GYPC, CCL27, ALDH1L1, GYPE, HAGH, WASF3, HSPH1, GJB6, HARS1, ARPP19, DHS, HLA-DRB4, HLA-G, PQBP1, MPHOSPH6, STAM2, GLYAT, HOXA@, RABEPK, HPCA, CALCOCO2, HRC, OLIG2, DDX39A, TOPORS, EIF1, HSD17B1, RAMP2, WASF2, HSD17B4, HSPA2, HSP90AB1, DNAJB1, NAMPT, BCAP31, CTDSP2, TSPAN3, ACTR2, CERT1, ABCC4, HNRNPK, HMBS, NPM3, CFDP1, PRMT5, HMGB2, YAP1, IFITM3, SPAG11B, PEMT, RACK1, SYCP2, TUBB4B, SEMA3A, WARS2, HNRNPC, FOXA1, CCL26, TLR6, FOXA2, LAMC3, LANCL1, HNF4A, TCIRG1, APBB3, APC2, HNRNPA2B1, MTCH2

Av Nodal Reentrant Tachycardia Wikipedia

Not to be confused with Atrioventricular reentrant tachycardia . AV-nodal reentrant tachycardia Other names Atrioventricular-nodal reentrant tachycardia An example of an ECG tracing typical of uncommon AV nodal reentrant tachycardia. ... The fast pathway is usually located just superior and posterior to the AV node. These pathways are formed from tissue that behaves very much like the AV node, and some authors regard them as part of the AV node. ... In AVNRT, the fast and slow pathways are located within the right atrium close to or within the AV node and exhibit electrophysiologic properties similar to AV nodal tissue. ... "Typical", "common", or "slow-fast" AVNRT uses the slow AV nodal pathway to conduct towards the ventricle (the anterograde limb of the circuit) and the fast AV nodal pathway to conduct to the atria (the retrograde limb). The re-entrant circuit can be reversed such that the fast AV nodal pathway is the anterograde limb and the slow AV nodal pathway is the retrograde limb, referred to as "atypical", "uncommon", or "fast-slow" AVNRT.

NLRP6, IL4I1

Second-Degree Atrioventricular Block Wikipedia

Second-degree atrioventricular block Other names Second-degree heart block ECGs demonstrating forms of second-degree AV block Specialty Cardiology Symptoms Dizziness , Fainting , Shortness of breath Types Type 1 (Wenckebach), Type 2 Causes Fibrosis in AV node, medication, vagal tone , electrolyte disturbances Diagnostic method Electrocardiogram Treatment Avoidance of AV-nodal-blocking medication, pacemaker Second-degree atrioventricular block (AV block) is a disease of the electrical conduction system of the heart . ... It is classified as a block of the AV node and is categorized in between first-degree (slowed conduction) and third degree blocks (complete block). ... Both types are named after Woldemar Mobitz . [3] [4] Type I is also named for Karel Frederik Wenckebach , [5] and type II is also named for John Hay . [6] [7] Type 1 (Mobitz I/Wenckebach) [ edit ] Type 1 Second-degree AV block , also known as Mobitz I or Wenckebach periodicity , is almost always a disease of the AV node . ... The definitive treatment for this form of AV Block is an implanted pacemaker . ... Thus one may leave out the type and refer to 3:1 Mobitz block or 4:3 Mobitz block, for example, without creating ambiguity, except in the case of 2:1 block. 2:1 AV block [ edit ] In the case of 2:1 block (2 P waves for every QRS complex) it is impossible to differentiate type I from type II Mobitz block based solely on the P:QRS ratio or on a pattern of lengthening PR intervals. [12] :182 In this case, a lengthened PR interval with a normal QRS width is most likely indicative of a type I-like pathology, and a normal PR interval with a widened QRS is most likely indicative of a type II-like pathology. [12] :182 See also [ edit ] Electrocardiogram (ECG or EKG) SA node AV node Atrioventricular block First-degree AV block Third-degree AV block References [ edit ] ^ "Lesson VI - ECG Conduction Abnormalities" .

CACNA1D, CACNA1S, GABRA3, LMNA, KCNJ18

Ventricular Escape Beat Wikipedia

Contents 1 Causes 2 Diagnosis 3 Management 3.1 Cilostazol 3.2 Ouabain 4 References Causes [ edit ] Ventricular escape beats occur when the rate of electrical discharge reaching the ventricles (normally initiated by the heart's sinoatrial node (SA node), transmitted to the atrioventricular node (AV node), and then further transmitted to the ventricles) falls below the base rate determined by the rate of Phase 4 spontaneous depolarisation of ventricular pacemaker cells. [1] An escape beat usually occurs 2–3 seconds after an electrical impulse has failed to reach the ventricles. [2] This phenomenon can be caused by the sinoatrial node (SA node) failing to initiate a beat, by a failure of the conductivity from the SA node to the atrioventricular node (AV node), or by atrioventricular block (especially third degree AV block ). Normally, the pacemaker cells of the sinoatrial node discharge at the highest frequency and are thus dominant over other cells with pacemaker activity. The AV node normally has the second fastest discharge rate. When the sinus rate falls below the discharge rate of the AV node, this becomes the dominant pacemaker, and the result is called a junctional escape beat . If the rate from both the SA and AV node fall below the discharge rate of ventricular pacemaker cells, a ventricular escape beat ensues. ... Ventricular pacemaker cells discharge at a slower rate than the SA or AV node. While the SA node typically initiates a rate of 70 beats per minute (BPM), the atrioventricular node (AV node) is usually only capable of generating a rhythm at 40-60 BPM or less.

Atrial Septal Defect 7 With Or Without Atrioventricular Conduction Defects OMIM

His mother had the same mutation and ASD with atrial fibrillation; her elder sister had ASD secundum with AV block and sick sinus syndrome requiring permanent pacemaker implantation, and a nephew had ASD with AV block. ... In 3 members of the other family (see 600584.0010), surgical closure of a secundum ASD had been performed; all 3 had ECG evidence of first- or second-degree AV block. In 1 member of the family, first-degree AV block was the only manifestation of heart disease. Hirayama-Yamada et al. (2005) reported that 4 sibs from a family with ASD and AV conduction defects had the same deletion mutation (600584.0012) in the NKX2E gene. The proband was diagnosed with ASD secundum and first-degree AV block that progressed to second-degree block; in 2 of her sibs, AV block also progressed to second degree, although 1 of those sibs had no cardiac malformation. ... One apparent asymptomatic carrier was found to have first-degree AV block on Holter monitoring. The conduction defect in this family was at the AV node, manifesting as first-degree block and evolving toward second-degree block; 3 patients also had atrial fibrillation, and 1 had unexplained ventricular tachycardia seen on Holter monitoring.

NKX2-5

Junctional Ectopic Tachycardia Wikipedia

(See electrical conduction system of the heart ). The AV node acts as a gatekeeper, limiting the electrical activity that reaches the ventricles of the heart. This function of the AV node is important, because if the signals generated in the atria of the heart were to increase in rate (as they do during atrial fibrillation or atrial flutter ), the AV node will limit the electrical activity that conducts to the ventricles. For instance, if the atria are electrically activated at 300 beats per minute, half those electrical impulses are blocked by the AV node, so that the ventricles are activated at 150 beats per minute (giving a pulse of 150 beats per minute). Another important property of the AV node is that it slows down individual electrical impulses. ... Tachycardia (from the Greek takhys , meaning "swift", and kardia , meaning heart) means a swift heart rate. [11] By this definition, junctional ectopic tachycardia is an abnormally swift heart rhythm due to cells firing within the heart near the AV node. References [ edit ] ^ Sarubbi B, Vergara P, D'Alto M, Calabro R (2003).

ACE, REN

His Bundle Tachycardia Orphanet

His bundle tachycardia is a very rare congenital genetic tachyarrhythmia characterized by incessant tachycardia and high morbidity and mortality.
Junctional Tachycardia Wikipedia

Junctional tachycardia is a form of supraventricular tachycardia characterized by involvement of the AV node . [1] It can be contrasted to atrial tachycardia . It is a tachycardia associated with the generation of impulses in a focus in the region of the atrioventricular node due to an A-V disassociation. [2] In general, the AV junction's intrinsic rate is 40-60 bpm so an accelerated junctional rhythm is from 60-100bpm and then becomes junctional tachycardia at a rate of >100 bpm. ... Contents 1 Cause 2 Diagnosis 3 Treatment 4 See also 5 References 6 External links Cause [ edit ] It can be associated with digitalis toxicity. [3] It may also be due to onset of acute coronary syndrome , heart failure , conduction system diseases with enhanced automaticity , or administration of theophylline . [4] Diagnosis [ edit ] On an EKG, junctional tachycardia exhibits the following classic criteria: [2] P-Waves: The p-wave may be inverted in leads II, III and aVF or may not be visible Narrow QRS complexes (which is consistent with arrhythmias that conduct through the ventricles using the His-Purkinje system and often originate from the atria or AV junction.) It can coexist with other superventricular tachycardias due to the disassociation between the SA node and the AV node. ... External links [ edit ] Classification D ICD - 10 : I47.1 ICD - 9-CM : xxx v t e Cardiovascular disease (heart) Ischaemic Coronary disease Coronary artery disease (CAD) Coronary artery aneurysm Spontaneous coronary artery dissection (SCAD) Coronary thrombosis Coronary vasospasm Myocardial bridge Active ischemia Angina pectoris Prinzmetal's angina Stable angina Acute coronary syndrome Myocardial infarction Unstable angina Sequelae hours Hibernating myocardium Myocardial stunning days Myocardial rupture weeks Aneurysm of heart / Ventricular aneurysm Dressler syndrome Layers Pericardium Pericarditis Acute Chronic / Constrictive Pericardial effusion Cardiac tamponade Hemopericardium Myocardium Myocarditis Chagas disease Cardiomyopathy Dilated Alcoholic Hypertrophic Tachycardia-induced Restrictive Loeffler endocarditis Cardiac amyloidosis Endocardial fibroelastosis Arrhythmogenic right ventricular dysplasia Endocardium / valves Endocarditis infective endocarditis Subacute bacterial endocarditis non-infective endocarditis Libman–Sacks endocarditis Nonbacterial thrombotic endocarditis Valves mitral regurgitation prolapse stenosis aortic stenosis insufficiency tricuspid stenosis insufficiency pulmonary stenosis insufficiency Conduction / arrhythmia Bradycardia Sinus bradycardia Sick sinus syndrome Heart block : Sinoatrial AV 1° 2° 3° Intraventricular Bundle branch block Right Left Left anterior fascicle Left posterior fascicle Bifascicular Trifascicular Adams–Stokes syndrome Tachycardia ( paroxysmal and sinus ) Supraventricular Atrial Multifocal Junctional AV nodal reentrant Junctional ectopic Ventricular Accelerated idioventricular rhythm Catecholaminergic polymorphic Torsades de pointes Premature contraction Atrial Junctional Ventricular Pre-excitation syndrome Lown–Ganong–Levine Wolff–Parkinson–White Flutter / fibrillation Atrial flutter Ventricular flutter Atrial fibrillation Familial Ventricular fibrillation Pacemaker Ectopic pacemaker / Ectopic beat Multifocal atrial tachycardia Pacemaker syndrome Parasystole Wandering atrial pacemaker Long QT syndrome Andersen–Tawil Jervell and Lange-Nielsen Romano–Ward Cardiac arrest Sudden cardiac death Asystole Pulseless electrical activity Sinoatrial arrest Other / ungrouped hexaxial reference system Right axis deviation Left axis deviation QT Short QT syndrome T T wave alternans ST Osborn wave ST elevation ST depression Strain pattern Cardiomegaly Ventricular hypertrophy Left Right / Cor pulmonale Atrial enlargement Left Right Athletic heart syndrome Other Cardiac fibrosis Heart failure Diastolic heart failure Cardiac asthma Rheumatic fever This article about a medical condition affecting the circulatory system is a stub .

Aortic Valve Stenosis GARD

Aortic valve stenosis (AVS) is a condition characterized by narrowing of the heart's aortic valve opening. This narrowing prevents the valve from opening fully, which obstructs blood flow from the heart into the aorta, and onward to the rest of the body. AVS can range from mild to severe. Signs and symptoms typically develop when the narrowing of the opening is severe and may include chest pain (angina) or tightness; shortness of breath or fatigue (especially during exertion); feeling faint or fainting; heart palpitations; and heart murmur. Individuals with less severe congenital AVS (present at birth) may not develop symptoms until adulthood. ... The condition can eventually lead to heart failure. AVS can have several causes including abnormal development before birth (such as having 1 or 2 valve leaflets instead of 3); calcium build-up on the valve in adulthood; and rheumatic fever .

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Bradycardia Wikipedia

This usually appears on an electrocardiogram (EKG) with a normal QRS complex accompanied with an inverted P wave either before, during, or after the QRS complex. [5] An AV-junctional escape beat is a delayed heartbeat originating from an ectopic focus somewhere in the AV junction . It occurs when the rate of depolarization of the SA node falls below the rate of the AV node . [5] This dysrhythmia also may occur when the electrical impulses from the SA node fail to reach the AV node because of SA or AV block . [7] This is a protective mechanism for the heart, to compensate for an SA node that is no longer handling the pacemaking activity, and is one of a series of backup sites that can take over pacemaker function when the SA node fails to do so. ... Those above the bundle of His, also known as junctional, will typically range between 40 and 60 BPM with a narrow QRS complex. [8] [9] In a third-degree heart block , about 61% take place at the bundle branch-Purkinje system, 21% at the AV node, and 15% at the bundle of His. [9] AV block may be ruled out with an EKG indicating "a 1:1 relationship between P waves and QRS complexes." [8] Ventricular bradycardias occurs with sinus bradycardia, sinus arrest, and AV block. ... Second-degree sinoatrial blocks can be detected only by use of a 12-lead EKG. [11] It is difficult and sometimes impossible to assign a mechanism to any particular bradycardia, but the underlying mechanism is not clinically relevant to treatment, which is the same in both cases of sick sinus syndrome: a permanent pacemaker . AV conduction disturbances (AV block; primary AV block , secondary type I AV block , secondary type II AV block , tertiary AV block ) may result from impaired conduction in the AV node, or anywhere below it, such as in the bundle of His. ... Clinical Sports Medicine. p. 259. ^ "AV Junctional Rhythm Disturbances (for Professionals)" .

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Partial Atrioventricular Septal Defect Orphanet

Shunting is restricted to the atrial level because of fusion of the leaflets of the common AV valve with the crest of the ventricular septum. ... An elevated pulmonary arterial pressure and moderate to severe left atrioventricular valve regurgitation may be observed. First-degree AV block, right bundle branch block, and a superior QRS axis may be noted on electrocardiogram. ... A pacemaker insertion may be required for complete AV block, which may spontaneously develop after repair. ... High morbidity and need for reoperation, often related to residual problems of the systemic AV valve or LAVV regurgitation, may be observed. ... Norwood-type intervention in infancy can be required, as well as prosthetic replacement of the left AV valve.

GATA4, GATA6, NR2F2, CRELD1, CCN1, NTF3, GJA1, TRAF7, ACVR1