Lecithin-cholesterol acyltransferase
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| Lecithin-cholesterol acyltransferase
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| Identifiers | ||||||||||||||
| Symbol(s) | LCAT; | |||||||||||||
| External IDs | OMIM: 606967 MGI: 96755 Homologene: 68042 | |||||||||||||
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| Orthologs | ||||||||||||||
| Human | Mouse | |||||||||||||
| Entrez | 3931 | 16816 | ||||||||||||
| Ensembl | na | ENSMUSG00000035237 | ||||||||||||
| Uniprot | na | Q791M3 | ||||||||||||
| Refseq | NM_000229 (mRNA) NP_000220 (protein) | NM_008490 (mRNA) NP_032516 (protein) | ||||||||||||
| Location | na | Chr 8: 108.83 - 108.83 Mb | ||||||||||||
| Pubmed search | [1] | [2] | ||||||||||||
Lecithin-cholesterol acyltransferase (LCAT, also called phosphatidylcholine-sterol O-acyltransferase) is an enzyme which converts free cholesterol into cholesteryl ester (a more hydrophobic form of cholesterol) which is then sequestered into the core of a lipoprotein particle eventually making the newly synthesized HDL spherical and forcing the reaction to become unidirectional since the particles are removed from the surface. The enzyme is bound to high-density lipoproteins (HDLs) and low-density lipoproteins in the blood plasma
See also
References
- Dobiásová M, Frohlich J (1999). "Advances in understanding of the role of lecithin cholesterol acyltransferase (LCAT) in cholesterol transport.". Clin Chim Acta 286 (1-2): 257-71. PMID 10511297.
Further reading
- Kuivenhoven JA, Pritchard H, Hill J, et al. (1997). "The molecular pathology of lecithin:cholesterol acyltransferase (LCAT) deficiency syndromes.". J. Lipid Res. 38 (2): 191-205. PMID 9162740.
- de Vries R, Borggreve SE, Dullaart RP (2004). "Role of lipases, lecithin:cholesterol acyltransferase and cholesteryl ester transfer protein in abnormal high density lipoprotein metabolism in insulin resistance and type 2 diabetes mellitus.". Clin. Lab. 49 (11-12): 601-13. PMID 14651331.
- Teisberg P, Gjone E, Olaisen B (1975). "Genetics of LCAT (lecithin: cholesterol acyltransferase) deficiency.". Ann. Hum. Genet. 38 (3): 327-31. PMID 806250.
- Cogan DG, Kruth HS, Datilis MB, Martin N (1993). "Corneal opacity in LCAT disease.". Cornea 11 (6): 595-9. PMID 1468226.
- Skretting G, Blomhoff JP, Solheim J, Prydz H (1992). "The genetic defect of the original Norwegian lecithin:cholesterol acyltransferase deficiency families.". FEBS Lett. 309 (3): 307-10. PMID 1516702.
- Skretting G, Prydz H (1992). "An amino acid exchange in exon I of the human lecithin: cholesterol acyltransferase (LCAT) gene is associated with fish eye disease.". Biochem. Biophys. Res. Commun. 182 (2): 583-7. PMID 1571050.
- Furukawa Y, Urano T, Hida Y, et al. (1992). "Interaction of rat lecithin-cholesterol acyltransferase with rat apolipoprotein A-I and with lecithin-cholesterol vesicles.". J. Biochem. 111 (3): 413-8. PMID 1587806.
- Minnich A, Collet X, Roghani A, et al. (1992). "Site-directed mutagenesis and structure-function analysis of the human apolipoprotein A-I. Relation between lecithin-cholesterol acyltransferase activation and lipid binding.". J. Biol. Chem. 267 (23): 16553-60. PMID 1644835.
- Bujo H, Kusunoki J, Ogasawara M, et al. (1992). "Molecular defect in familial lecithin:cholesterol acyltransferase (LCAT) deficiency: a single nucleotide insertion in LCAT gene causes a complete deficient type of the disease.". Biochem. Biophys. Res. Commun. 181 (3): 933-40. PMID 1662503.
- Gotoda T, Yamada N, Murase T, et al. (1991). "Differential phenotypic expression by three mutant alleles in familial lecithin:cholesterol acyltransferase deficiency.". Lancet 338 (8770): 778-81. PMID 1681161.
- Klein HG, Lohse P, Pritchard PH, et al. (1992). "Two different allelic mutations in the lecithin-cholesterol acyltransferase gene associated with the fish eye syndrome. Lecithin-cholesterol acyltransferase (Thr123----Ile) and lecithin-cholesterol acyltransferase (Thr347----Met).". J. Clin. Invest. 89 (2): 499-506. PMID 1737840.
- Maeda E, Naka Y, Matozaki T, et al. (1991). "Lecithin-cholesterol acyltransferase (LCAT) deficiency with a missense mutation in exon 6 of the LCAT gene.". Biochem. Biophys. Res. Commun. 178 (2): 460-6. PMID 1859405.
- Funke H, von Eckardstein A, Pritchard PH, et al. (1991). "A molecular defect causing fish eye disease: an amino acid exchange in lecithin-cholesterol acyltransferase (LCAT) leads to the selective loss of alpha-LCAT activity.". Proc. Natl. Acad. Sci. U.S.A. 88 (11): 4855-9. PMID 2052566.
- Taramelli R, Pontoglio M, Candiani G, et al. (1990). "Lecithin cholesterol acyl transferase deficiency: molecular analysis of a mutated allele.". Hum. Genet. 85 (2): 195-9. PMID 2370048.
- Rogne S, Skretting G, Larsen F, et al. (1987). "The isolation and characterisation of a cDNA clone for human lecithin:cholesterol acyl transferase and its use to analyse the genes in patients with LCAT deficiency and fish eye disease.". Biochem. Biophys. Res. Commun. 148 (1): 161-9. PMID 2823801.
- Tata F, Chaves ME, Markham AF, et al. (1987). "The isolation and characterisation of cDNA and genomic clones for human lecithin: cholesterol acyltransferase.". Biochim. Biophys. Acta 910 (2): 142-8. PMID 2823898.
- Yang CY, Manoogian D, Pao Q, et al. (1987). "Lecithin:cholesterol acyltransferase. Functional regions and a structural model of the enzyme.". J. Biol. Chem. 262 (7): 3086-91. PMID 2880847.
- McLean J, Fielding C, Drayna D, et al. (1986). "Cloning and expression of human lecithin-cholesterol acyltransferase cDNA.". Proc. Natl. Acad. Sci. U.S.A. 83 (8): 2335-9. PMID 3458198.
- Azoulay M, Henry I, Tata F, et al. (1987). "The structural gene for lecithin:cholesterol acyl transferase (LCAT) maps to 16q22.". Ann. Hum. Genet. 51 (Pt 2): 129-36. PMID 3674753.
- McLean J, Wion K, Drayna D, et al. (1987). "Human lecithin-cholesterol acyltransferase gene: complete gene sequence and sites of expression.". Nucleic Acids Res. 14 (23): 9397-406. PMID 3797244.
External links
Transferases: acyltransferases (EC 2.3) | |
|---|---|
| 2.3.1: other than amino-acyl groups (mostly acetyltransferases) | N-Acetylglutamate synthase - Choline acetyltransferase - Acetyl-Coenzyme A acetyltransferase - Dihydrolipoyl transacetylase - Acetyl-CoA C-acyltransferase - Beta-galactoside transacetylase - Carnitine O-palmitoyltransferase (CPT1, CPT2) - Acyltransferase like 2 - Chloramphenicol acetyltransferase - Aminolevulinic acid synthase - Beta-ketoacyl-ACP synthase - Glyceronephosphate O-acyltransferase - Lecithin-cholesterol acyltransferase - Histone acetyltransferase (P300/CBP) - Serotonin N-acetyl transferase |
| 2.3.2 - Aminoacyltransferases | Gamma glutamyl transpeptidase - Peptidyl transferase - Transglutaminase (Tissue transglutaminase, Keratinocyte transglutaminase, Factor XIII) |
| 2.3.3 - converted into alkyl on transfer | Citrate synthase - ATP citrate lyase - HMG-CoA synthase |
Acknowledgement and Attribution Regarding Sources of Content
Some of the initial content on this page may be incorporated in part from copyleft sources in the public domain including wikis such as Wikipedia and AskDrWiki. Drug information for patients came from the The National Library of Medicine. Infectious disease information may have come from the Centers for Disease Control (CDC). Differential Diagnoses are drawn from clinicians as well as an amalgamation of 3 sources: 1.The Disease Database; 2. Kahan, Scott, Smith, Ellen G. In A Page: Signs and Symptoms. Malden, Massachusetts: Blackwell Publishing, 2004:3; 3. Sailer, Christian, Wasner, Susanne. Differential Diagnosis Pocket. Hermosa Beach, CA: Borm Bruckmeir Publishing LLC, 2002:7 .
