Biology:Lecithin–cholesterol acyltransferase

Short description: Mammalian protein found in Homo sapiens

Generic protein structure example

Lecithin–cholesterol acyltransferase (LCAT, also called phosphatidylcholine–sterol O-acyltransferase) is an enzyme, in many animals including humans, 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) (alpha-LCAT) and LDLs (beta-LCAT) in the blood plasma. LCAT deficiency can cause impaired vision due to cholesterol corneal opacities, anemia, and kidney damage. It belongs to the family of phospholipid:diacylglycerol acyltransferases.

See also

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

Further reading

• "Advances in understanding of the role of lecithin cholesterol acyltransferase (LCAT) in cholesterol transport.". Clin Chim Acta 286 (1–2): 257–71. 1999. doi:10.1016/S0009-8981(99)00106-0. PMID 10511297. 
• "The molecular pathology of lecithin:cholesterol acyltransferase (LCAT) deficiency syndromes". J. Lipid Res. 38 (2): 191–205. 1997. doi:10.1016/S0022-2275(20)37433-2. PMID 9162740. 
• "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. 2004. PMID 14651331. 
• "Genetics of LCAT (lecithin: cholesterol acyltransferase) deficiency". Ann. Hum. Genet. 38 (3): 327–31. 1975. doi:10.1111/j.1469-1809.1975.tb00617.x. PMID 806250. 
• "Corneal opacity in LCAT disease". Cornea 11 (6): 595–9. 1993. doi:10.1097/00003226-199211000-00021. PMID 1468226. https://zenodo.org/record/1234782. 
• "The genetic defect of the original Norwegian lecithin:cholesterol acyltransferase deficiency families". FEBS Lett. 309 (3): 307–10. 1992. doi:10.1016/0014-5793(92)80795-I. PMID 1516702. 
• "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. 1992. doi:10.1016/0006-291X(92)91772-I. PMID 1571050. 
• "Interaction of rat lecithin-cholesterol acyltransferase with rat apolipoprotein A-I and with lecithin-cholesterol vesicles". J. Biochem. 111 (3): 413–8. 1992. doi:10.1093/oxfordjournals.jbchem.a123771. PMID 1587806. 
• "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. 1992. doi:10.1016/S0021-9258(18)42038-8. PMID 1644835. 
• "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. 1992. doi:10.1016/0006-291X(91)92026-G. PMID 1662503. 
• "Differential phenotypic expression by three mutant alleles in familial lecithin:cholesterol acyltransferase deficiency". Lancet 338 (8770): 778–81. 1991. doi:10.1016/0140-6736(91)90665-C. PMID 1681161. 
• "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. 1992. doi:10.1172/JCI115612. PMID 1737840. 
• "Lecithin-cholesterol acyltransferase (LCAT) deficiency with a missense mutation in exon 6 of the LCAT gene". Biochem. Biophys. Res. Commun. 178 (2): 460–6. 1991. doi:10.1016/0006-291X(91)90129-U. PMID 1859405. 
• "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. 1991. doi:10.1073/pnas.88.11.4855. PMID 2052566. Bibcode: 1991PNAS...88.4855F. 
• "Lecithin cholesterol acyl transferase deficiency: molecular analysis of a mutated allele". Hum. Genet. 85 (2): 195–9. 1990. doi:10.1007/BF00193195. PMID 2370048. 
• "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. 1987. doi:10.1016/0006-291X(87)91090-4. PMID 2823801. 
• "The isolation and characterisation of cDNA and genomic clones for human lecithin: cholesterol acyltransferase". Biochim. Biophys. Acta 910 (2): 142–8. 1987. doi:10.1016/0167-4781(87)90066-2. PMID 2823898. 
• "Lecithin:cholesterol acyltransferase. Functional regions and a structural model of the enzyme". J. Biol. Chem. 262 (7): 3086–91. 1987. doi:10.1016/S0021-9258(18)61472-3. PMID 2880847. 
• "Cloning and expression of human lecithin-cholesterol acyltransferase cDNA". Proc. Natl. Acad. Sci. U.S.A. 83 (8): 2335–9. 1986. doi:10.1073/pnas.83.8.2335. PMID 3458198. Bibcode: 1986PNAS...83.2335M. 
• "The structural gene for lecithin:cholesterol acyl transferase (LCAT) maps to 16q22". Ann. Hum. Genet. 51 (Pt 2): 129–36. 1987. doi:10.1111/j.1469-1809.1987.tb01054.x. PMID 3674753. 
• "Human lecithin-cholesterol acyltransferase gene: complete gene sequence and sites of expression". Nucleic Acids Res. 14 (23): 9397–406. 1987. doi:10.1093/nar/14.23.9397. PMID 3797244. 

External links

• Lecithin+Cholesterol+Acyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH)
• Overview of all the structural information available in the PDB for UniProt: P04180 (Phosphatidylcholine-sterol acyltransferase) at the PDBe-KB.