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.[5]LCAT deficiency can cause impaired vision due to cholesterol corneal opacities, anemia, and kidney damage.[6] It belongs to the family of phospholipid:diacylglycerol acyltransferases.
Interactive pathway map
Click on genes, proteins and metabolites below to link to respective articles.[§ 1]
^Reference, Genetics Home. "LCAT gene". Genetics Home Reference. Retrieved 2016-12-11.
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. PMID10511297.
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. PMID14651331.
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. PMID1516702. S2CID26714265.
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. PMID1571050.
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. doi:10.1093/oxfordjournals.jbchem.a123771. PMID1587806.
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. PMID1662503.
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. PMID1681161. S2CID9708282.
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. PMID1859405.
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. PMID2370048. S2CID23994746.
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. PMID2823801.
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. PMID2823898.