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Familial Lipoprotein Lipase Deficiency GeneReviews

Diagnosis/testing. The diagnosis of LPL deficiency is established in a proband by the identification of biallelic pathogenic variants in LPL on molecular genetic testing. ... Affected individuals have low or absent LPL enzyme activity in an assay system that contains either normal plasma or apolipoprotein C-II (apoC-II; a cofactor of LPL) and excludes hepatic lipase (HL). ... The absence of LPL enzyme activity in postheparin plasma is diagnostic of familial LPL deficiency. LPL enzyme activity may be assayed directly in biopsies of adipose tissue. ... Consanguinity is observed in some families with familial LPL deficiency caused by homozygous pathogenic LPL variants.

LPL, APOC2, GPIHBP1, APOA5, APOB, APOC3, LMF1, APOL1, APOE, AMT, LCAT, ADA, NR1I3, DGAT1, PNPLA2, TRIM13, SACS, ANGPTL3, TNFSF4, CXADRP1, TNFRSF4, PRKAR1A, TNF, TBX1, SPG7, LAMC2, HDLBP, CXADR, CSF2, CETP, CD19, CASR, CCND1, ARR3, APOA1, HLP
- Familial Lipoprotein Lipase Deficiency GARD
  
  Familial lipoprotein lipase deficiency is caused by changes (mutations) in the LPL gene. It is inherited in an autosomal recessive pattern.
- Lipoprotein Lipase Deficiency Wikipedia
  
  Typically, the plasma in a fasting blood sample appears creamy (plasma lactescence). [ medical citation needed ] Familial LPL deficiency should be considered in anyone with severe hypertriglyceridemia and the chylomicronemia syndrome. The absence of secondary causes of severe hypertriglyceridemia (like e.g. diabetes, alcohol, estrogen -, glucocorticoid -, antidepressant - or isotretinoin -therapy, certain antihypertensive agents , and paraproteinemic disorders) increases the possibility of LPL deficiency. In this instance besides LPL also other loss-of-function mutations in genes that regulate catabolism of triglyceride-rich lipoproteins (like e.g. ... Lipid measurements · Milky, lipemic plasma revealing severe hyperchylomicronemia; [ citation needed ] · Severely elevated fasting plasma triglycerides (>2000 mg/dL); [ citation needed ] LPL enzyme · Low or absent LPL activity in post- heparin plasma; · LPL mass level reduced or absent in post-heparin plasma; Molecular genetic testing The LPL gene is located on the short (p) arm of chromosome 8 at position 22. More than 220 mutations in the LPL gene have been found to cause familial lipoprotein lipase deficiency so far. ... Supplements . 11 (1): 55–60. doi : 10.1016/j.atherosclerosissup.2010.03.004 . PMID 20427244 . "LPL gene" . NIH Genetics Home Reference.
- Hyperlipoproteinemia, Type I OMIM
  
  Slight to moderate hemolysis is often present in plasma from patients with primary LPL deficiency. Cantin et al. (1995) found that, while osmotic fragility was similar to that in control subjects, plasma prehemoglobin was significantly increased. ... In the absence of the LPL-dependent pathway, the removal of triglyceride-rich lipoproteins occurs through a less efficient LPL-independent pathway, resulting in massively elevated triglyceride levels. APOC3 (107720) is known to inhibit LPL (609708), although there is also evidence that APOC3 increases the level of plasma triglycerides through an LPL-independent mechanism. Gaudet et al. (2014) administered an inhibitor of APOC3 mRNA, called ISIS 304801, to treat 3 patients with familial chylomicronemia syndrome due to LPL deficiency and triglyceride levels ranging from 1,406 to 2,083 mg/dl (15.9-23.5 mM/l). ... Gaudet et al. (2014) concluded that these data supported the role of APOC3 as a key regulator of LPL-independent pathways of triglyceride metabolism.
- Familial Chylomicronemia Syndrome GARD
  
  Hyperlipoproteinemia type 1 is caused by mutations in the LPL gene. This condition is inherited in an autosomal recessive pattern.
- Familial Lipoprotein Lipase Deficiency MedlinePlus
  
  It is much more common in certain areas of the province of Quebec, Canada. Causes Mutations in the LPL gene cause familial lipoprotein lipase deficiency. The LPL gene provides instructions for producing an enzyme called lipoprotein lipase, which is found primarily on the surface of cells that line tiny blood vessels (capillaries ) within muscles and fatty (adipose) tissue. ... Learn more about the gene associated with Familial lipoprotein lipase deficiency LPL Inheritance Pattern This condition is inherited in an autosomal recessive pattern , which means both copies of the gene in each cell have mutations. ... Researchers speculate that if family members of affected individuals have a mutation in one copy of the LPL gene in each cell, they may have a mild increase in fat levels in the blood, which could increase their risk of health problems such as heart disease or diabetes.
Lipase Deficiency, Combined OMIM

Clinical Features Auwerx et al. (1990) described a large family with familial hepatic triglyceride lipase (HTGL; 151670) deficiency and a coexisting reduced lipoprotein lipase (LPL; 609708) similar to the heterozygous state of LPL deficiency. ... The mutation, however, affects neither the LPL nor the HTGL gene, but a transmembrane protein designated Lmf1 by Peterfy et al. (2007). ... The severe hypertriglyceridemia was found to be due to LPL deficiency, as determined by a 93% decrease in LPL activity in the plasma of the affected individual. ... In cld mice, Davis et al. (1990) found Lpl synthetic rates to be 70% of control rates; values for Lpl in cld post-heparin plasma were markedly reduced to only 7% of control values, suggesting that most of the Lpl was not secreted. Davis et al. (1990) concluded that a selective impairment of intracellular transport and secretion of Lpl and Hl underlies the disorder in the mouse.

LMF1, LPL
Hyperlipoproteinemia, Type V OMIM

Nagasaka et al. (2003) described 2 unrelated premature females with transient type V hyperlipidemia and low lipoprotein lipase (LPL; 238600) activity at 1 to 2 months of age without deficiencies of LPL or apoCII (608083) proteins or detectable inhibitors and without mutations in the LPL or APOC2 genes. The authors postulated the presence of an unidentified LPL inhibitor, perhaps a maternal factor such as estrogen. ... Additionally, they demonstrated that severe hypertriglyceridemia in Q139X mutation carriers resulted from an LPL defect leading to lipolysis impairment. ... Marcais et al. (2005) showed that severe hyperchylomicronemia in homozygote and heterozygote Q139X carriers was caused by profound LPL defect, and they provided what appeared to be the first clear evidence in humans of a functional interplay between APOA5 and LPL.

APOA5, APOE, LPL
Hyperlipoproteinemia, Type Id OMIM

Olivecrona et al. (2010) reported a family from northern Sweden in which 3 of 4 sibs had congenital chylomicronemia. Lipoprotein lipase (LPL; 609708) activity and mass in pre- and postheparin plasma were low, and LPL release into plasma after heparin injection was delayed. LPL activity and mass in adipose tissue biopsies appeared normal. ... He remained mostly hyperchylomicronemic with recurrent acute pancreatitis. His LPL activity was undetectable; his mother and daughter had normal lipid parameters. ... She had a low HDL of 11 mg/dL and reduced LPL activity. Plengpanich et al. (2014) reported 3 sibs with chylomicronemia. ... When this patient was given a 6-hour infusion of heparin, a significant amount of LPL appeared in the plasma, resulting in a fall in the plasma triglyceride levels from 1,780 to 120 mg/dL.

GPIHBP1
Familial Hypertriglyceridemia Wikipedia

Individuals with the disorder are mostly heterozygous in an inactivating mutation of the gene encoding for lipoprotein lipase (LPL). This sole mutation can markedly elevate serum triglyceride levels. ... Individuals with insulin resistance can have even further elevated levels of hypertriglyceridemia due to the fact that insulin is a potent activator of LPL. Therefore, an individual who is resistant to the bioactivity of insulin will have decreased LPL activity and will therefore lead to further hypertriglyceridemia, helping push serum triglycerides to pathologic levels. ... The frequency of heterozygous carriers of certain pathologic mutations in the LPL gene can range from 0.06% to 20%. ... LPL plays a role in the metabolism of triglycerides within VLDL molecules. Inactivation mutations in LPL will create an environment with an increased concentration of VLDL molecules and therefore, triglycerides.

APOA5, LIPI, LPL, APOA1, APOB, APOE, LPA, SLC10A2, ALB, APOC3, HLP
- Hyperlipoproteinemia, Type Iv OMIM
  
  Description On a regular diet patients with type IV hyperlipoproteinemia demonstrate increased plasma VLDL. Plasma triglycerides are persistently increased, while plasma cholesterol and phospholipids are usually within normal limits. Precocious atherosclerosis, abnormal glucose tolerance, and atheroeruptive xanthoma may occur. The disorder is undoubtedly heterogeneous and the phenotype strongly influenced by environmental factors, particularly carbohydrate and ethanol consumption. Clinical Features In an old American family living in New England, Schreibman et al. (1969) described hyperprebetalipoproteinemia behaving as an autosomal dominant with reduced penetrance.
Coronary Heart Disease, Susceptibility To, 9 OMIM

Probands had at least 50% stenosis in at least 2 coronary arteries before the age of 62 or 66 years for men and women, respectively; patients with familial hypercholesterolemia or with family members known to be homozygous for mutations in the lipoprotein lipase gene (LPL; 609708) were excluded. Mapping Engert et al. (2008) performed a genomewide scan on 119 affected and 165 unaffected individuals from 42 French Canadian families with early-onset coronary heart disease and obtained a nonparametric linkage score of 3.14 (p = 0.001) at D8S1106 on chromosome 8p22. ... Engert et al. (2008) analyzed 10 candidate genes in the region, including the LPL gene, located 13 cM from the peak, but did not identify a disease-associated mutation.
Macroglobulinemia, Waldenstrom, Susceptibility To, 1 OMIM

Somatic Mutation in Bone Marrow Lymphoplasmacytic Lymphoma Cells Treon et al. (2012) performed whole-genome sequencing of bone marrow lymphoplasmacytic lymphoma (LPL) cells in 30 patients with Waldenstrom macroglobulinemia, with paired normal-tissue and tumor-tissue sequencing in 10 patients. Sanger sequencing was used to validate the findings from an expanded cohort of patients with LPL, those with other B-cell disorders that have some of the same features as LPL, and healthy donors. ... Sanger sequencing identified MYD88 L265P in tumor samples from 49 of 54 patients with Waldenstrom macroglobulinemia and in 3 of 3 patients with non-IgM-secreting LPL (91% of all patients with LPL). MYD88 L265P was absent in paired normal-tissue samples from patients with Waldenstrom macroglobulinemia or non-IgM LPL and in B cells from healthy donors and was absent or rarely expressed in samples from patients with multiple myeloma, marginal-zone lymphoma, or IgM monoclonal gammopathy of unknown significance. ... Treon et al. (2012) concluded that MYD88 L265P is a commonly recurring mutation in patients with Waldenstrom macroglobulinemia that can be useful in differentiating Waldenstrom macroglobulinemia and non-IgM LPL from B-cell disorders that have phenotypic overlap.

MYD88, IL6, BTK, PAX5, CXCR4, BCL2, IGH, KRT20, CD19, MS4A1, MIR155, TP53, CXCL12, IRAK1, STOML2, IL4, IRF4, UCHL5, CD40LG, CD27, HAS1, MYOM2, USP14, SDC1, CDR3, SYK, TP73, ZAP70, IL10, ANPEP, MALT1, NAMPT, TNFSF13B, LPL, TNFSF13, MYC, PIK3CD, SMUG1, AKT1, BACH2, MTOR, AICDA, FCGR3A, FCER2, BCR, TCL1A, RAPH1, ARHGAP24, SLC28A1, EGLN3, TNFSF10, TNFRSF13C, TNFSF11, ARID1A, PRIMA1, IGHV3OR16-7, AIMP2, GRAP2, SLC35B2, LAPTM5, MIR206, MIR23B, XPO1, XBP1, VWF, VEGFA, MIR363, LOC102723407, CLEC12A, HDAC9, TCL1B, ANP32B, POLDIP2, IBTK, RNF19A, IGHV4-34, MAPK8IP2, TNFAIP3, ACSBG1, IGHV3-69-1, IGHV3-23, CD274, BLNK, ZHX2, ADAMTS13, IRAK4, LEF1, TLR7, AHSA1, COLEC10, CXCL13, EGLN1, EXOC2, TNFRSF13B, PXN, TNF, CD70, HCK, HAS2, GLI2, FGFR3, EFNB2, CTRL, CTNNB1, MAPK14, CRP, CRK, CD52, CDKN2A, CD79B, CD79A, CD40, HMMR, CD38, TNFRSF8, CD22, CD6, CCND3, CBL, SERPING1, BSG, BRAF, BLM, BCL9, BCL6, CCND1, ANXA5, HCLS1, IL1B, AURKA, PLCG2, STAT5B, STAT5A, SPIB, SPI1, SOAT1, CCL3, RAF1, PTPRC, MAPK3, MAPK1, PRKCD, POU2F2, POU2F1, POU2AF1, PIK3CG, IL2RA, PIK3CB, PIK3CA, NOTCH2, NOS2, NOS1, NCAM1, CD200, MMP8, MCL1, KIT, ITGAM, ITGA4, ISG20, IL4R, LOC102724971
- Macroglobulinemia Wikipedia
  
  This article needs more medical references for verification or relies too heavily on primary sources . Please review the contents of the article and add the appropriate references if you can. Unsourced or poorly sourced material may be challenged and removed . Find sources: "Macroglobulinemia" – news · newspapers · books · scholar · JSTOR ( July 2020 ) Macroglobulinemia Specialty Hematology Macroglobulinemia is the presence of increased levels of macroglobulins in the circulating blood . It is a plasma cell dyscrasia , resembling leukemia , with cells of lymphocytic, plasmacytic, or intermediate morphology, which secrete a monoclonal immunoglobulin M component. There is diffuse infiltration by the malignant cells of the bone marrow and also, in many cases, of the spleen, liver, or lymph nodes.
- Waldenstrom Macroglobulinemia Mayo Clinic
  
  Overview Waldenstrom macroglobulinemia (mak-roe-glob-u-lih-NEE-me-uh) is a rare type of cancer that begins in the white blood cells. If you have Waldenstrom macroglobulinemia, your bone marrow produces too many abnormal white blood cells that crowd out healthy blood cells. The abnormal white blood cells produce a protein that accumulates in the blood, impairs circulation and causes complications. Waldenstrom macroglobulinemia is considered a type of non-Hodgkin's lymphoma. It's sometimes called lymphoplasmacytic lymphoma. Symptoms Waldenstrom macroglobulinemia is slow growing and may not cause signs and symptoms for many years.
- Waldenström Macroglobulinemia Orphanet
  
  Waldenström macroglobulinemia (WM) is an indolent B-cell lymphoproliferative disorder characterized by the accumulation of monoclonal cells in the bone marrow and peripheral lymphoid tissues, and associated with the production of serum immunoglobulin M (IgM) monoclonal protein. Epidemiology WM has an overall incidence of 1/260,000 persons/year in the USA and a prevalence estimate of about 1/102,220 in Europe. It accounts for approximately 2% of all hematological malignancies. Clinical description The median age at diagnosis is 72 years and it is twice as frequent in men. The main clinical features are hepatosplenomegaly, lymphadenopathy, constitutional symptoms, oronasal bleeding, hyperviscosity syndrome and cytopenia. Fatigue related to normochromic normocytic anemia is the most common presenting symptom.
- Macroglobulinemia, Waldenstrom, Susceptibility To, 2 OMIM
  
  For a phenotypic description and a discussion of genetic heterogeneity of susceptibility to Waldenstrom macroglobulinemia, see 153600. Mapping McMaster et al. (2006) performed a genomewide linkage analysis in 11 high-risk families with WM that were informative for linkage, for a total of 122 individuals with DNA samples, including 34 patients with WM and 10 patients with IgM monoclonal gammopathy of undetermined significance (IgM MGUS). The strongest evidence of linkage was found on chromosome 1q and 4q when patients with WM and with IgM MGUS were both considered affected; nonparametric linkage scores were 2.5 (p = 0.0089) and 3.1 (p = 0.004), respectively. Other locations suggestive of linkage were found on chromosomes 3 and 6. Results of 2-locus linkage analysis were consistent with independent effects.
Hyperlipidemia, Familial Combined, 3 OMIM

A number sign (#) is used with this entry because susceptibility to familial combined hyperlipidemia-3 (FCHL3) can be conferred by mutation in the LPL gene (609708) on chromosome 8p21. ... Molecular Genetics Individuals heterozygous for lipoprotein lipase deficiency (238600) also show an FCHL phenotype. Indeed, a defect in the LPL gene may occur in up to a fifth of FCHL families (Babirak et al., 1989). One of 20 FCHL patients studied by Yang et al. (1995) was found to be compound heterozygous for mutations in the promoter region of the lipoprotein lipase gene (LPL; 609708.0032 and 609708.0038), and most heterozygous parents of patients who are homozygous for the recessive disorder LPL deficiency (238600) have a lipid phenotype resembling that of mild FCHL. ... INHERITANCE - Autosomal dominant LABORATORY ABNORMALITIES - Hyperlipidemia, mild, variable - Elevated serum cholesterol - Elevated triglycerides - Reduced HDL cholesterol MOLECULAR BASIS - Susceptibility conferred by mutation in the lipoprotein lipase gene (LPL, 609708.0033 ) ▲ Close

LPL, USF1, FASLG, APOB, ABCG8, APOE, ABCG5, APOA1, APOC3, APOA2, LDLR, C3, LPA, LIPC, LIPE, SERPINE1, ADIPOQ, PPARG, LPAL2, APOA5, PCSK9, TXNIP, HNF4A, TNF, JPH3, PPARA, FABP2, GPT, TNFRSF1B, IL6, C5AR2, TCF7L2, SCD, OSBPL10, NECTIN2, TCF3, SELP, ZBTB7C, TGIF1, RXRG, PCDH15, UCP1, OSBPL9, TNFRSF1A, ATAD1, VLDLR, KHSRP, LYPLA2, ATF6, SIGLEC7, MLXIPL, PNPLA2, PSIP1, ABCA1, PON1, EGR1, CYP7A1, CUX1, CRP, CRABP2, CHIT1, CETP, CDKN2B, CD59, CD36, VPS51, AR, APOA4, ANGPT2, ALB, AGT, DLX4, EIF4EBP1, PLG, FAT1, SERPINB2, OSBP, NIDDM1, MTTP, ADD1, FADS3, LEPR, LEP, LCAT, IRS1, IL2RB, IGFBP2, HMGCR, HCLS1, FN1, HLP
Hypertriglyceridemia, Familial OMIM

In a 59-year-old man with severe hypertriglyceridemia, Breckenridge et al. (1978) found deficiency of apolipoprotein C-II (APOC2; 207750), which is an activator for lipoprotein lipase (LPL; 609708). After transfusion of 1 unit of plasma the patient's triglycerides fell, within 1 day, from 1000 to 250 mg per deciliter and remained below preinfusion concentration for 6 days. ... Other Associations In a study of a total of 555 individuals with hypertriglyceridemia, diagnosed with Fredrickson hyperlipoproteinemia phenotypes 2B (144250), 3 (107741), 4 (144600), or 5 (144650), and 1,319 controls, Johansen et al. (2010) first performed a genomewide association study and identified common variants in the APOA5, GCKR (600842), LPL, and APOB (107730) genes that were associated with hypertriglyceridemia. ... Evidence has connected MI risk with coding-sequence mutations at 2 genes functionally related to APOA5, namely lipoprotein lipase (LPL; 609708) and apolipoprotein C-III (APOC3; 107720).
Microvascular Complications Of Diabetes, Susceptibility To, 1 OMIM

Associations Pending Confirmation Association with Variation in APOC3, APOE, and LPL In a case-control study of 374 Chinese patients with type 2 diabetes and nephropathy and 392 Chinese diabetics without nephropathy, Ng et al. (2006) examined the association of the APOC3 -455T-C SNP (107720), APOE E2 (107741.0001), E3 (107741.0015), and E4 alleles (107741.0016), and the LPL S447X SNP (609708.0014) with diabetic nephropathy. LPL 447X-containing genotypes were significantly decreased in diabetic nephropathy patients, as were APOE 3/3 genotypes. In addition, certain combinations of genotypes (APOE 3/3 and LPL 447X, APOC3 C/C and LPL 447X, and APOE 3/3 and APOC3 C/C) were protective for diabetic nephropathy compared with the most common combination of the respective polymorphisms.
Obesity OMIM

Three genes in this network, lipoprotein lipase (LPL; 609708), lactamase beta (LACTB; 608440), and protein phosphatase 1-like (PPM1L; 611931), were validated as previously unknown obesity genes, strengthening the association between this network and metabolic disease traits. Given the prediction that LPL and LACTB have a causal relationship with obesity, Chen et al. (2008) recorded weight, fat mass, and lean mass for Lpl heterozygous null mice, Lactb transgenic mice, and wildtype littermate controls every 2 weeks starting at 11 weeks of age using quantitative nuclear magnetic resonance (NMR). As predicted, the growth curves for the Lpl heterozygous null and Lactb transgenic animals were significantly different from those of controls, with the fat mass/lean mass ratio difference generally increasing over time. At the final quantitative NMR measurement the fat mass/lean mass ratios in the Lpl heterozygous null mouse and the Lactb transgenic mice were increased by 22% and 20%, respectively, over the wildtype controls (p = 1.09 x 10(-5) and p = 4.48 x 10(-5)), respectively. LPL is the principal enzyme responsible for the hydrolysis of circulating triglycerides and is active in differentiated macrophages, consistent with its presence in the MEMN.

POMC, MC4R
- Proopiomelanocortin Deficiency GARD
  
  Proopiomelanocortin (POMC) deficiency is characterized by severe obesity that begins at an early age. Affected infants are usually a normal weight at birth, but they are constantly hungry, which leads to excessive feeding and weight gain during the first year and throughout life. In addition, people with this condition have low levels of a hormone known as adrenocorticotropic hormone (ACTH) which leads to adrenal insufficiency . They also tend to have red hair and pale skin. POMC deficiency is caused by mutations in the POMC gene. The condition is inherited in an autosomal recessive pattern. Adrenal insufficiency requires prompt treatment with hydrocortisone to avoid life-threatening complications.
- Obesity, Early-Onset, With Adrenal Insufficiency And Red Hair OMIM
  
  A number sign (#) is used with this entry because of evidence that early-onset obesity, adrenal insufficiency, and red hair (OBAIRH) is caused by homozygous or compound heterozygous mutation in the POMC gene (176830) on chromosome 2p23. Description OBAIRH is an autosomal recessive endocrine disorder characterized by early-onset obesity due to severe hyperphagia, pigmentary abnormalities, mainly pale skin and red hair, and secondary hypocortisolism. In the neonatal period, affected individuals are prone to hypoglycemia, hyperbilirubinemia, and cholestasis that may result in death if not treated. The disorder results from mutation in the POMC gene, which encodes a preproprotein that is processed into a range of bioactive peptides, including alpha-melanocyte-stimulating hormone (MSH) and ACTH (summary by Kuhnen et al., 2016 and Clement et al., 2008). Clinical Features Krude et al. (1998) observed an unrelated 3-year-old girl and 5-year-old boy who had obesity, red hair pigmentation, and ACTH deficiency.
- Obesity Due To Pro-Opiomelanocortin Deficiency Orphanet
  
  Pro-opiomelanocortin (POMC) deficiency is a form of monogenic obesity resulting in severe early-onset obesity, adrenal insufficiency, red hair and pale skin. Epidemiology It is has been described in less than 10 patients. Clinical description Patients with POMC deficiency usually present in the neonatal period with hypoglycaemic seizures, hyperbilirubinaemia and cholestasis to due to secondary congenital hypocortisolism. Hyperphagia is noted from the first weeks of life leading to severe obesity before one year of age. Subclinical hypothyroidism was also reported. Etiology Complete POMC deficiency is caused by homozygous or compound heterozygous loss-of-function mutations in the POMC gene (chromosome 2p23.3). POMC is regulated by leptin and is cleaved by prohormone convertases to produce the melanocortin receptor (MC-R) ligands adrenocorticotrophin (ACTH) and melanocyte-stimulating hormones (MSH) alpha, beta and gamma.
- Proopiomelanocortin Deficiency MedlinePlus
  
  Proopiomelanocortin (POMC) deficiency causes severe obesity that begins at an early age. In addition to obesity, people with this condition have low levels of a hormone known as adrenocorticotropic hormone (ACTH) and tend to have red hair and pale skin. Affected infants are usually a normal weight at birth, but they are constantly hungry, which leads to excessive feeding (hyperphagia). The babies continuously gain weight and are severely obese by age 1. Affected individuals experience excessive hunger and remain obese for life. It is unclear if these individuals are prone to weight-related conditions like cardiovascular disease or type 2 diabetes.
Yao Syndrome Wikipedia

The American Journal of Medicine . 130 (3): 365.e13–365.e18. doi : 10.1016/j.amjmed.2016.09.028 .

NOD2, MEFV, S100A12, NLRP12, NLRP3
- Yao Syndrome MedlinePlus
  
  Yao syndrome (formerly called NOD2 -associated autoinflammatory disease) is a disorder involving episodes of fever and abnormal inflammation affecting many parts of the body, particularly the skin, joints, and gastrointestinal system. Inflammation is a normal immune system response to injury and foreign invaders (such as bacteria). In people with Yao syndrome, part of the immune system called the innate immune response is turned on (activated) abnormally, which causes fevers and inflammation-related damage to tissues and organs. Based on this process, Yao syndrome is classified as an autoinflammatory disease. Autoinflammatory diseases are distinct from autoimmune diseases; these two groups of diseases involve abnormalities in different parts of the immune system.
- Yao Syndrome OMIM
  
  A number sign (#) is used with this entry because of evidence that susceptibility to Yao syndrome (YAOS) is conferred by variation in the NOD2 gene (605956) on chromosome 16q12. Description Yao syndrome is an autoinflammatory disease characterized by periodic fever, dermatitis, arthritis, and swelling of the distal extremities, as well as gastrointestinal and sicca-like symptoms. The disorder is associated with specific NOD2 variants (Yao and Shen, 2017). Clinical Features Yao et al. (2011) described 7 unrelated patients with apparent autoinflammatory disease with multisystem involvement. Mean age at disease onset was 40.7 years, and the patients characteristically presented with periodic fever, dermatitis, and inflammatory polyarthritis.
Dysbetalipoproteinemia Orphanet

Dietary, metabolic, hormonal factors may aggravate the disease, as well as chronic inflammation, xenobiotics (e.g. immune suppressants, retinoids, antidepressants) or other genetic cofactors (e.g. APOA5 , APOC3 , LIPC , LPL variants). Diagnostic methods Diagnosis is based on the evidence of an abnormal lipoprotein profile with increased fasting serum concentrations of total cholesterol, triglycerides and Apolipoprotein B, and lowered plasma high-density lipoprotein (HDL) cholesterol (<40 mg/dL).

APOE, APOA5, LDLR, APOB, LPL, APOA2, LPAL2, CETP, LPA, SERPINA13P, HLP, TNFRSF25, SULF2, LSR, SMUG1, HPSE, TNFRSF10A, ABCA1, ALB, ITGB2, IAPP, CD44, CAD, APOC3, APOC2, APOC1, APOA1, LINC01672
- Hyperlipoproteinemia, Type Iii OMIM
  
  Frikke-Schmidt et al. (2007) presented evidence that combinations of SNPs in APOE and LPL (609708) identify subgroups of individuals at substantially increased risk of ischemic heart disease beyond that associated with smoking, diabetes, and hypertension.
- Familial Dysbetalipoproteinemia Wikipedia
  
  Familial dysbetalipoproteinemia Other names Remnant hyperlipidemia , Remnant hyperlipoproteinaemia , Broad beta disease [1] and Remnant removal disease [1] Familial dysbetalipoproteinemia is caused by this point mutation in ApoE Specialty Medical genetics , endocrinology Familial dysbetalipoproteinemia or type III hyperlipoproteinemia is a condition characterized by increased total cholesterol and triglyceride levels, and decreased HDL levels. [2] : 534 Contents 1 Signs and symptoms 2 Causes 3 Diagnosis 4 Treatment 5 See also 6 References 7 External links Signs and symptoms [ edit ] Signs of familial dysbetaproteinemia include xanthoma striatum palmare (orange or yellow discoloration of the palms) and tuberoeruptive xanthomas over the elbows and knees. The disease leads to premature atherosclerosis and therefore a possible early onset of coronary artery disease and peripheral vascular disease leading to a heart attack, i.e. myocardial infarction , chest pain on exercise, i.e. angina pectoris or stroke in young adults or middle aged patients. [3] Causes [ edit ] This condition is caused by a mutation in apolipoprotein E (ApoE), that serves as a ligand for the liver receptor for chylomicrons , IDL and VLDL , also known as very-low-density-lipoprotein receptor . The normal ApoE turns into the defective ApoE2 form due to a genetic mutation. [4] This defect prevents the normal metabolism of chylomicrons, IDL and VLDL, otherwise known as remnants, and therefore leads to accumulation of cholesterol within scavenger cells (macrophages) to enhance development and acceleration of atherosclerosis. Diagnosis [ edit ] This section is empty. You can help by adding to it . ( November 2017 ) Treatment [ edit ] First line of management are fibrates. See also [ edit ] Primary hyperlipoproteinemia Apolipoprotein B deficiency List of cutaneous conditions References [ edit ] ^ a b Rapini, Ronald P.; Bolognia, Jean L.; Jorizzo, Joseph L. (2007).
- Hyperlipidemia Type 3 GARD
  
  Hyperlipidemia type 3 is an inherited condition that disrupts the normal breakdown of fats (lipids) in the body, causing a large amount of certain fatty materials to build up in the body. Some individuals never have symptoms of this condition. Symptoms usually do not appear unless a second genetic or environmental factor adds to increased lipid levels. Symptoms may include: yellowish lipid-filled bumps on the skin (xanthomas), inflammation of the pancreas (pancreatitis), and a buildup of fat in the blood vessels (atherosclerosis). Hyperlipidemia type 3 may lead to the development of cardiovascular disease . This condition is caused by mutations in the APOE gene. The inheritance of this condition is considered to be complicated, as having mutations in the APOE gene often does not lead to the development of symptoms without the influence of other factors.
Lipoprotein Glomerulopathy OMIM

Apolipoprotein E may accumulate in glomerular capillaries because the mutation diminishes the capacity of apolipoprotein E to bind to the low-density lipoprotein (LDL) receptor and also decreases its uptake by endothelial cells. Impaired LPL binding was also seen with APOE Sendai (Ishigaki et al., 2000).

APOE, FCER1G, LDLR, IGAN1, HLP
- Lipoprotein Glomerulopathy Orphanet
  
  A rare genetic renal disease characterized by the formation of intraglomerular lipoprotein thrombi due to lipid deposition in severely dilated glomerular capillaries. Laboratory examination reveals abnormal serum lipid profiles, in particular markedly elevated apolipoprotein E. Clinical manifestations include proteinuria or nephrotic syndrome with hypertension and potential progression to chronic renal failure. Systemic complications of dyslipidemia are not observed.
Phospholipid Transfer Protein OMIM

Molecular Genetics In an evaluation of the hypothesis that multiple high density lipoprotein cholesterol (HDL-C) levels reflect the cumulative contributions of multiple common DNA sequence variants, each of which has a small effect, Spirin et al. (2007) identified a single-nucleotide polymorphism (SNP) of the PLTP gene (172425.0001) that acts in concert with other SNPs in the CETP (118470.0005) and LPL (118470.0042) genes to affect plasma levels of high density lipoprotein cholesterol.
Ornithophobia Wikipedia

The Psychiatric Quarterly . 26 (1): 365–371. doi : 10.1007/BF01568473 . PMID 14949213 . ^ Irena Milosevic; Randi E.
Plasma Triglyceride Level Quantitative Trait Locus OMIM

Functional studies revealed that all mutant alleles of ANGPTL4 that were associated with low plasma triglyceride levels interfered either with the synthesis or secretion of the protein or with the ability of the ANGPTL to inhibit lipoprotein lipase (LPL). A total of 1% of the Dallas Heart Study population and 4% of those participants with a plasma triglyceride in the lowest quartile had a rare loss-of-function mutation in ANGPTL3, ANGPTL4, or ANGPTL5.

ANGPTL4
Anaplastic Carcinoma Wikipedia

Anaplastic carcinoma is a general term for a malignant neoplasm arising from the uncontrolled proliferation of transformed cells of epithelial origin, or showing some epithelial characteristics, but that reveal no cytological or architectural features associated with more differentiated tumors , such as the glandular formation or special cellular junctions that are typical of adenocarcinoma and squamous cell carcinoma , respectively. Specific types include: anaplastic astrocytoma anaplastic large-cell lymphoma anaplastic meningioma anaplastic thyroid cancer References [ edit ]

TP53, BCL2, PTEN, CSF3, KRAS, EGFR, TSHR, TP63, PADI4, PTGS2, CORO1A, BRCA1, STAT3, CDH1, FN1, MGP, RB1, MDH2, EPCAM, PTN, LPL, RAN, RASA1, RASGRF2, RBP4, RBP1, MET, RCN1, RPL3, RPL6, RPS14, S100A6, LGALS7, SCD, PTGS1, PSME1, PTBP1, MIF, COX1, MYC, KITLG, NDN, OXT, PEBP1, FURIN, PDGFA, PGAM1, PGR, ABCB1, PHB, PIK3R1, ACTG1, PLAUR, SRSF2, PPARA, PRLR, PSMA4, SELENOP, ACTB, SGK1, PLK2, LIN7A, TSC22D1, MPZL1, TP53I3, GDA, MRC2, BASP1, MERTK, SPINT2, LY96, VAMP8, NSMF, G0S2, ANGPTL4, LSR, ACKR3, KRT71, TMEM37, TUBB2B, GLYCAM1, URI1, CASK, SLC12A2, THRSP, SNCG, SNRPD3, STMN1, SOX9, STAT5A, PRDX2, TF, TGFB1, TGFBR2, TKT, YWHAZ, TLE4, TLR4, TPM3, TRPS1, UBE2I, UCP2, VHL, EZR, XDH, SOD2, PKM, KRT5, HNRNPA1, CSN2, EPHX1, CSN3, HBA1, SLC25A10, DBI, DES, DNMT1, GSTT1, GSTP1, GSS, DNMT3B, DUSP6, TYMP, GNAI2, S1PR1, GGT1, GATM, GATA3, EEF1A1, FHIT, EFEMP1, ACSL1, FABP4, ESR2, ESR1, EIF5A, CSF2, HIF1A, HRAS, CAPZB, ACTN4, ADCY5, INSIG1, ALCAM, ANXA1, IL6ST, ANXA4, AQP1, RHOA, ATP7B, CCND1, COL5A1, BCL2L1, ENO1, KYAT1, ID3, CCNH, SCARB1, ID4, CDC42, CDK4, CNN3, CDS1, H3-3B, ATP5IF1, BRAF, SMARCA4, NKX2-1, CDKN2A, TG, RET, SMARCB1, SMARCA1, PDLIM7, H3P10, PTCH1, IDH2, PAX8, VEGFA, IDH1, PIK3CA, CKAP4, MSH2, SPARC, UVRAG, RPE65, CLDN4, CTNNB1, TTF1, TERT, MSN, NUPR1, CADM1, ADGRE2, CCL22, IFNA13, COX2, TMED10, BNIP3, PTGES3, MUC1, MUC2, IFNA2, MSLN, IFNA1, CD1D, SMARCAL1, MLH1, AQP4, MUC16, H3P47, H3P17, LOC110806263, MTCO2P12, LMNA, MIR126, ITGAM, TMED10P1, NUTM1, IL18, IL10, IFNG, AQP3, MAP1LC3A, MRO, MAP1LC3B, ARID1B, AKR1B10, IFNA17, SLC12A9, EMSY, FBXW7, TET2, NPC1, NFKBIA, CDKN1C, ADGRE5, GPLD1, TIE1, MAPK3, MSH6, TAS2R38, ITGB2, DPYD, DUSP1, ZEB1, GRP, SSTR4, POLE, SRF, GPC3, LPAR1, GAPDH, EGR1, F9, SMARCA2, RRAS, ERBB2, PPP2R1A, CYLD, CDK5R1, CCDC6, NRAS, CDK2, IFN1@, CDKN1A, EMD, ARID1A, HMGA2, FOSL1, NCOA4, SCLC1, PMS2, CDX2, VTN, CIRBP, PCNA, HSP90AA1, TYMS, SERPINB5, TPT1, HHEX, TFF1
Chymosin Pseudogene OMIM

In the process of secretion, preprochymosin, comprising 381 amino acids, is processed by the signal peptidase into an inactive 365-amino acid prochymosin. At low pH, prochymosin undergoes autocatalytic cleavage of 42 N-terminal amino acids, yielding active chymosin.
Spindle Cell Carcinoma Wikipedia

Spindle cell carcinoma Specialty Oncology Spindle cell carcinoma is a type of cancer that begins in the skin or in tissues that line or cover internal organs and that contains long spindle-shaped cells. It is also called sarcomatoid carcinoma . See also [ edit ] Spindle cell sarcoma Spindle cell squamous cell carcinoma External links [ edit ] Classification D ICD-O : M8032/3 Spindle cell cancer entry in the public domain NCI Dictionary of Cancer Terms This article incorporates public domain material from the U.S. National Cancer Institute document: "Dictionary of Cancer Terms" . This oncology article is a stub . You can help Wikipedia by expanding it . v t e

TP53, KRAS, MET, EGFR, TP63, ACTB, TGFB1, HRAS, BRCA1, KRT5, DES, RBP4, RBP1, RPL6, RCN1, RPL3, RB1, S100A6, RPS14, SCD, SELENOP, SRSF2, SGK1, SLC12A2, SNCG, SNRPD3, RASGRF2, RAN, RASA1, SOX9, PEBP1, FURIN, PDGFA, PGAM1, PGR, ABCB1, PHB, PIK3R1, PKM, PLAUR, ACTG1, PRLR, PSMA4, PSME1, PTBP1, PTEN, PTGS1, PTGS2, PTN, SOD2, TF, STAT3, STAT5A, TP53I3, GDA, MRC2, BASP1, MERTK, SPINT2, PLK2, CORO1A, PADI4, LY96, NSMF, G0S2, ANGPTL4, LSR, ACKR3, KRT71, TMEM37, TUBB2B, GLYCAM1, MPZL1, TSC22D1, LIN7A, TRPS1, PRDX2, NDN, TGFBR2, THRSP, TKT, TLE4, TLR4, TPM3, TSHR, URI1, UBE2I, UCP2, VHL, EZR, XDH, YWHAZ, CASK, VAMP8, OXT, PPARA, DNMT3B, GNAI2, EEF1A1, EIF5A, KYAT1, ENO1, EPHX1, CAPZB, ESR1, ESR2, FABP4, ACSL1, EFEMP1, FHIT, FN1, GATA3, GATM, S1PR1, TYMP, DUSP6, SCARB1, CDH1, CDK4, CDS1, CNN3, COL5A1, CSF2, CSF3, MYC, CSN2, CSN3, SLC25A10, CCNH, DBI, DNMT1, GGT1, BCL2L1, GSS, EPCAM, ANXA4, GSTP1, STMN1, ALCAM, LGALS7, LPL, MDH2, INSIG1, KITLG, MGP, MIF, ADCY5, ACTN4, COX1, AQP1, ANXA1, RHOA, HNRNPA1, GSTT1, HBA1, BCL2, CCND1, HIF1A, ATP7B, CDC42, ID3, IL6ST, ID4, H3-3B, ATP5IF1, VIM, CD274, ALK, CDKN2A, YAP1, CKAP4, ZEB2, ARMH1, ARHGEF2, RABEPK, H3P28, LANCL1, EBNA1BP2, NTRK1, H3P10, NKX2-1, KRT7, RPE65, PSMD7, RPSA, MAPK1, KIT, IL9, UVRAG, GADL1, PDGFRA, NUTM1, AZIN2, MIR205, MMP2, LOC110806263, NANOG, MMP9, IMP3, LOXL2, SLC9A3R2, KDR, ENG, SCAF11, CD47, GEMIN2, BAP1, CTNNB1, CYLD, TERT, NAPSA, BRCA2, ZEB1, TAZ, SNAI1, HGF, HTC2, IGF1
- Sarcomatoid Carcinoma Wikipedia
  
  Sarcomatoid carcinoma Metaplastic (sarcomatoid) carcinoma of the breast. Specialty Oncology Sarcomatoid carcinoma , sometimes referred to as pleomorphic carcinoma , [1] is a relatively uncommon form of cancer whose malignant cells have histological, cytological, or molecular properties of both epithelial tumors (" carcinoma ") and mesenchymal tumors (" sarcoma "). It is believed that sarcomatoid carcinomas develop from more common forms of epithelial tumors. [2] Sarcomatoid carcinoma locations [ edit ] Histological variants of lung cancer classified as sarcomatoid carcinoma include giant cell carcinoma , spindle cell carcinoma , carcinosarcoma , and pulmonary blastoma . Sarcomatoid carcinomas have been identified in the small intestine in rare cases. They may have epithelioid and mesenchymal properties or be composed only of mesenchymal-type spindle cells , and are negative for CD117 and DOG1 . [3] Some cases of sacromatoid carcinoma of the larynx are resistant to radiotherapy . [2] References [ edit ] ^ Tumors and Tumor-like Conditions of the Lung and Pleura .