Lecithin-cholesterol acyltransferase

Lecithin-cholesterol acyltransferase

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

ee also

* Lecithin cholesterol acyltransferase deficiency

References

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Further reading

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citations =
*cite journal | author=Kuivenhoven JA, Pritchard H, Hill J, "et al." |title=The molecular pathology of lecithin:cholesterol acyltransferase (LCAT) deficiency syndromes. |journal=J. Lipid Res. |volume=38 |issue= 2 |pages= 191–205 |year= 1997 |pmid= 9162740 |doi=
*cite journal | author=de Vries R, Borggreve SE, Dullaart RP |title=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. |journal=Clin. Lab. |volume=49 |issue= 11-12 |pages= 601–13 |year= 2004 |pmid= 14651331 |doi=
*cite journal | author=Teisberg P, Gjone E, Olaisen B |title=Genetics of LCAT (lecithin: cholesterol acyltransferase) deficiency. |journal=Ann. Hum. Genet. |volume=38 |issue= 3 |pages= 327–31 |year= 1975 |pmid= 806250 |doi=
*cite journal | author=Cogan DG, Kruth HS, Datilis MB, Martin N |title=Corneal opacity in LCAT disease. |journal=Cornea |volume=11 |issue= 6 |pages= 595–9 |year= 1993 |pmid= 1468226 |doi=
*cite journal | author=Skretting G, Blomhoff JP, Solheim J, Prydz H |title=The genetic defect of the original Norwegian lecithin:cholesterol acyltransferase deficiency families. |journal=FEBS Lett. |volume=309 |issue= 3 |pages= 307–10 |year= 1992 |pmid= 1516702 |doi=
*cite journal | author=Skretting G, Prydz H |title=An amino acid exchange in exon I of the human lecithin: cholesterol acyltransferase (LCAT) gene is associated with fish eye disease. |journal=Biochem. Biophys. Res. Commun. |volume=182 |issue= 2 |pages= 583–7 |year= 1992 |pmid= 1571050 |doi=
*cite journal | author=Furukawa Y, Urano T, Hida Y, "et al." |title=Interaction of rat lecithin-cholesterol acyltransferase with rat apolipoprotein A-I and with lecithin-cholesterol vesicles. |journal=J. Biochem. |volume=111 |issue= 3 |pages= 413–8 |year= 1992 |pmid= 1587806 |doi=
*cite journal | author=Minnich A, Collet X, Roghani A, "et al." |title=Site-directed mutagenesis and structure-function analysis of the human apolipoprotein A-I. Relation between lecithin-cholesterol acyltransferase activation and lipid binding. |journal=J. Biol. Chem. |volume=267 |issue= 23 |pages= 16553–60 |year= 1992 |pmid= 1644835 |doi=
*cite journal | author=Bujo H, Kusunoki J, Ogasawara M, "et al." |title=Molecular defect in familial lecithin:cholesterol acyltransferase (LCAT) deficiency: a single nucleotide insertion in LCAT gene causes a complete deficient type of the disease. |journal=Biochem. Biophys. Res. Commun. |volume=181 |issue= 3 |pages= 933–40 |year= 1992 |pmid= 1662503 |doi=
*cite journal | author=Gotoda T, Yamada N, Murase T, "et al." |title=Differential phenotypic expression by three mutant alleles in familial lecithin:cholesterol acyltransferase deficiency. |journal=Lancet |volume=338 |issue= 8770 |pages= 778–81 |year= 1991 |pmid= 1681161 |doi=
*cite journal | author=Klein HG, Lohse P, Pritchard PH, "et al." |title=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). |journal=J. Clin. Invest. |volume=89 |issue= 2 |pages= 499–506 |year= 1992 |pmid= 1737840 |doi=
*cite journal |author=Maeda E, Naka Y, Matozaki T, "et al." |title=Lecithin-cholesterol acyltransferase (LCAT) deficiency with a missense mutation in exon 6 of the LCAT gene. |journal=Biochem. Biophys. Res. Commun. |volume=178 |issue= 2 |pages= 460–6 |year= 1991 |pmid= 1859405 |doi=
*cite journal | author=Funke H, von Eckardstein A, Pritchard PH, "et al." |title=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. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 11 |pages= 4855–9 |year= 1991 |pmid= 2052566 |doi=
*cite journal | author=Taramelli R, Pontoglio M, Candiani G, "et al." |title=Lecithin cholesterol acyl transferase deficiency: molecular analysis of a mutated allele. |journal=Hum. Genet. |volume=85 |issue= 2 |pages= 195–9 |year= 1990 |pmid= 2370048 |doi=
*cite journal | author=Rogne S, Skretting G, Larsen F, "et al." |title=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. |journal=Biochem. Biophys. Res. Commun. |volume=148 |issue= 1 |pages= 161–9 |year= 1987 |pmid= 2823801 |doi=
*cite journal | author=Tata F, Chaves ME, Markham AF, "et al." |title=The isolation and characterisation of cDNA and genomic clones for human lecithin: cholesterol acyltransferase. |journal=Biochim. Biophys. Acta |volume=910 |issue= 2 |pages= 142–8 |year= 1987 |pmid= 2823898 |doi=
*cite journal | author=Yang CY, Manoogian D, Pao Q, "et al." |title=Lecithin:cholesterol acyltransferase. Functional regions and a structural model of the enzyme. |journal=J. Biol. Chem. |volume=262 |issue= 7 |pages= 3086–91 |year= 1987 |pmid= 2880847 |doi=
*cite journal | author=McLean J, Fielding C, Drayna D, "et al." |title=Cloning and expression of human lecithin-cholesterol acyltransferase cDNA. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 8 |pages= 2335–9 |year= 1986 |pmid= 3458198 |doi=
*cite journal | author=Azoulay M, Henry I, Tata F, "et al." |title=The structural gene for lecithin:cholesterol acyl transferase (LCAT) maps to 16q22. |journal=Ann. Hum. Genet. |volume=51 |issue= Pt 2 |pages= 129–36 |year= 1987 |pmid= 3674753 |doi=
*cite journal | author=McLean J, Wion K, Drayna D, "et al." |title=Human lecithin-cholesterol acyltransferase gene: complete gene sequence and sites of expression. |journal=Nucleic Acids Res. |volume=14 |issue= 23 |pages= 9397–406 |year= 1987 |pmid= 3797244 |doi=

External links

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