Lecithin-cholesterol acyltransferase

From Wikipedia, the free encyclopedia

Identifiers

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

n/a

n/a

Refseq

NM_000229 (mRNA)
NP_000220 (protein)

NM_008490 (mRNA)
NP_032516 (protein)

Location

n/a

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

1 See also
2 References
3 Further reading
4 External links

[edit] See also

Lecithin cholesterol acyltransferase deficiency

[edit] 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. doi:10.1016/S0009-8981(99)00106-0. PMID 10511297.

[edit] 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.

[edit] External links

MeSH Lecithin+Cholesterol+Acyltransferase

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v • d • e 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 - Serine C-palmitoyltransferase (SPTLC1, SPTLC2) - HGSNAT

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

v • d • e Lipids: lipoprotein metabolism

General	Chylomicron - HDL - LDL - IDL - VLDL - Lp(a)

Apolipoproteins	APOA (1, 2, 5) - APOB - APOC (1, 2, 3, 4) - APOD - APOE - APOH

Other	Lipoprotein lipase - HDL (Cholesterylester transfer protein Acetyl-CoA C-acyltransferase, LCAT) - LDL receptor - Microsomal triglyceride transfer protein - ABCA1 - Lecithin-cholesterol acyltransferase

see also disorders