Lecithin-cholesterol acyltransferase

Lecithin-cholesterol acyltransferase
Identifiers
Symbol(s)	LCAT;
External IDs	OMIM: 606967 MGI: 96755 Homologene: 68042
Gene ontology Molecular Function: • phosphatidylcholine-sterol O-acyltransferase activity • protein binding • acyltransferase activity • transferase activity Cellular Component: • extracellular region Biological Process: • lipid metabolic process • steroid metabolic process • cholesterol metabolic process • protein amino acid esterification
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]

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List of terms related to Lecithin-cholesterol acyltransferase

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

• Lecithin cholesterol acyltransferase deficiency

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

• MeSH Lecithin+Cholesterol+Acyltransferase