Lecithin–cholesterol acyltransferase

LCAT
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4X96, 4XWG, 4XX1, 5BV7
Identifiers
Aliases	LCAT, entrez:3931
External IDs	OMIM: 606967 MGI: 96755 HomoloGene: 68042 GeneCards: LCAT
Gene ontology Molecular function • transferase activity • phospholipase A2 activity • O-acyltransferase activity • apolipoprotein A-I binding • protein binding • transferase activity, transferring acyl groups • phosphatidylcholine-sterol O-acyltransferase activity Cellular component • extracellular space • extracellular region • high-density lipoprotein particle • extracellular exosome Biological process • lipoprotein metabolic process • steroid metabolic process • regulation of high-density lipoprotein particle assembly • response to copper ion • lipid metabolic process • cholesterol transport • response to glucocorticoid • cholesterol metabolic process • cholesterol esterification • high-density lipoprotein particle remodeling • very-low-density lipoprotein particle remodeling • phospholipid metabolic process • lipoprotein biosynthetic process • cholesterol homeostasis • phosphatidylcholine biosynthetic process • phosphatidylcholine metabolic process • reverse cholesterol transport Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	3931	16816
Ensembl	ENSG00000213398	ENSMUSG00000035237
UniProt	P04180	P16301
RefSeq (mRNA)	NM_000229	NM_008490
RefSeq (protein)	NP_000220.1	NP_032516.2
Location (UCSC)	Chr 16: 67.94 – 67.94 Mb	Chr 8: 105.94 – 105.94 Mb
PubMed search	[1]	[2]
Wikidata

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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.

Interactive pathway map

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

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Statin Pathway edit

1. The interactive pathway map can be edited at WikiPathways: "Statin_Pathway_WP430".

See also

• Lecithin cholesterol acyltransferase deficiency
• Acyl-CoA:cholesterol acyltransferase (ACAT)

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".

Further reading

• 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.
• 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.
• 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. doi:10.1016/0167-4781(87)90066-2. 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.
• 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.

External links

• Lecithin Cholesterol Acyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH)