Lecithin—cholesterol acyltransferase

Lecithin-cholesterol acyltransferase

Identifiers

External IDs

OMIM: 606967 MGI: 96755 HomoloGene: 68042 GeneCards: LCAT Gene

2.3.1.43

Gene Ontology
Molecular function	• phosphatidylcholine-sterol O-acyltransferase activity • phosphatidylcholine-sterol O-acyltransferase activity • phosphatidylcholine-sterol O-acyltransferase activity • phospholipase A2 activity • protein binding • transferase activity • apolipoprotein A-I binding
Cellular component	• extracellular region • extracellular region • extracellular space • high-density lipoprotein particle
Biological process	• lipid metabolic process • phospholipid metabolic process • phosphatidylcholine biosynthetic process • steroid metabolic process • cholesterol metabolic process • cholesterol transport • very-low-density lipoprotein particle remodeling • high-density lipoprotein particle remodeling • cholesterol esterification • lipoprotein metabolic process • lipoprotein biosynthetic process • cholesterol homeostasis • reverse cholesterol transport • response to copper ion • response to glucocorticoid stimulus
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 16:
67.97 – 67.98 Mb

Chr 8:
108.46 – 108.47 Mb

PubMed search

[1]

[2]

Lecithin-cholesterol acyltransferase (LCAT, also called phosphatidylcholine-sterol O-acyltransferase) is an enzyme that 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 Interactive pathway map
2 See also
3 References
4 Further reading
5 External links

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles. ^[1]

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Statin Pathway edit

References

^ The interactive pathway map can be edited at WikiPathways: "Statin_Pathway_WP430". http://www.wikipathways.org/index.php/Pathway:WP430.

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.
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. doi:10.1111/j.1469-1809.1975.tb00617.x. PMID 806250.
Cogan DG, Kruth HS, Datilis MB, Martin N (1993). "Corneal opacity in LCAT disease.". Cornea 11 (6): 595–9. doi:10.1097/00003226-199211000-00021. 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. doi:10.1016/0014-5793(92)80795-I. 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. doi:10.1016/0006-291X(92)91772-I. 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. doi:10.1016/0006-291X(91)92026-G. 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. doi:10.1016/0140-6736(91)90665-C. 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. doi:10.1172/JCI115612. PMC 442879. PMID 1737840. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=442879.
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. doi:10.1016/0006-291X(91)90129-U. 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. doi:10.1073/pnas.88.11.4855. PMC 51765. PMID 2052566. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=51765.
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. doi:10.1007/BF00193195. 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. doi:10.1016/0006-291X(87)91090-4. 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. doi:10.1073/pnas.83.8.2335. PMC 323291. PMID 3458198. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=323291.
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. doi:10.1111/j.1469-1809.1987.tb01054.x. 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. doi:10.1093/nar/14.23.9397. PMC 311966. PMID 3797244. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=311966.

External links

MeSH Lecithin+Cholesterol+Acyltransferase

Transferases: acyltransferases (EC 2.3)

2.3.1: other than amino-acyl groups	acetyltransferases: Acetyl-Coenzyme A acetyltransferase - N-Acetylglutamate synthase - Choline acetyltransferase - Dihydrolipoyl transacetylase - Acetyl-CoA C-acyltransferase - Beta-galactoside transacetylase - Chloramphenicol acetyltransferase - N-acetyltransferase (Serotonin N-acetyl transferase, HGSNAT, ARD1A) - Histone acetyltransferase (P300/CBP, NAT2) palmitoyltransferases: Carnitine O-palmitoyltransferase (CPT1, CPT2) - Serine C-palmitoyltransferase (SPTLC1, SPTLC2) other: Acyltransferase like 2 - Aminolevulinic acid synthase - Beta-ketoacyl-ACP synthase - Glyceronephosphate O-acyltransferase - Lecithin-cholesterol acyltransferase Glycerol-3-phosphate O-acyltransferase - 1-acylglycerol-3-phosphate O-acyltransferase - 2-acylglycerol-3-phosphate O-acyltransferase - ABHD5

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

B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6