Lecithin-cholesterol acyltransferase: Difference between revisions
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==Overview== | ==Overview== | ||
'''Lecithin-cholesterol acyltransferase''' ('''LCAT''', also called '''phosphatidylcholine-sterol O-acyltransferase''') is an [[enzyme]] that esterifies the free cholesterol into [[chlesteryl ester]] by transferring an acyl chain from the R2 position of a [[phosphatidylcholine]] to the 3′-hydroxy residue of [[cholesterol]]. Cholesteryl ester is then sequestered into the core of a [[lipoprotein]] particle eventually making the newly synthesized [[High density lipoprotein|HDL]] spherical and forcing the reaction to become unidirectional since the particles are removed from the surface. The enzyme is bound to [[high-density lipoprotein]]s (HDLs) and [[low-density lipoprotein]]s in the [[ | '''Lecithin-cholesterol acyltransferase''' ('''LCAT''', also called '''phosphatidylcholine-sterol O-acyltransferase''') is an [[enzyme]] that esterifies the free cholesterol into [[chlesteryl ester]] by transferring an acyl chain from the R2 position of a [[phosphatidylcholine]] to the 3′-hydroxy residue of [[cholesterol]]. Cholesteryl ester is then sequestered into the core of a [[lipoprotein]] particle eventually making the newly synthesized [[High density lipoprotein|HDL]] spherical and forcing the reaction to become unidirectional since the particles are removed from the surface. The enzyme is bound to [[high-density lipoprotein]]s (HDLs) and [[low-density lipoprotein]]s in the [[plasma]]. | ||
==Historical Perspective== | |||
In 1935, Sperry first recognized the esterification of free cholesterol occurred when human plasma was incubated at 37°C and considered it as an enzymatic process since the effect was abolished when the plasma was heated to 55-60°C.<ref name="www.jbc.org">{{Cite web | last = | first = | title = CHOLESTEROL ESTERASE IN BLOOD | url = http://www.jbc.org/content/111/2/467.citation | publisher = | date = | }}</ref> In 1962, Glomset identified the enzyme lecithin-cholesterol acyltransferase (LCAT) that accounts for esterification of most of the free cholesterol in plasma.<ref name="GLOMSET-1962">{{Cite journal | last1 = GLOMSET | first1 = JA. | title = The mechanism of the plasma cholesterol esterification reaction: plasma fatty acid transferase. | journal = Biochim Biophys Acta | volume = 65 | issue = | pages = 128-35 | month = Nov | year = 1962 | doi = | PMID = 13948499 }}</ref> | |||
==See also== | ==See also== | ||
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==References== | ==References== | ||
{{Reflist|2}} | |||
==Further reading== | ==Further reading== | ||
Revision as of 16:25, 8 November 2013
| Lecithin-cholesterol acyltransferase | |||||||||||
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| Identifiers | |||||||||||
| Symbols | LCAT ; | ||||||||||
| External IDs | Template:OMIM5 Template:MGI HomoloGene: 68042 | ||||||||||
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| Template:GNF Ortholog box | |||||||||||
| Species | Human | Mouse | |||||||||
| Entrez | n/a | n/a | |||||||||
| Ensembl | n/a | n/a | |||||||||
| UniProt | n/a | n/a | |||||||||
| RefSeq (mRNA) | n/a | n/a | |||||||||
| RefSeq (protein) | n/a | n/a | |||||||||
| Location (UCSC) | n/a | n/a | |||||||||
| PubMed search | n/a | n/a | |||||||||
Editor-In-Chief: C. Michael Gibson, M.S., M.D. [1]
Overview
Lecithin-cholesterol acyltransferase (LCAT, also called phosphatidylcholine-sterol O-acyltransferase) is an enzyme that esterifies the free cholesterol into chlesteryl ester by transferring an acyl chain from the R2 position of a phosphatidylcholine to the 3′-hydroxy residue of cholesterol. Cholesteryl ester 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 plasma.
Historical Perspective
In 1935, Sperry first recognized the esterification of free cholesterol occurred when human plasma was incubated at 37°C and considered it as an enzymatic process since the effect was abolished when the plasma was heated to 55-60°C.[1] In 1962, Glomset identified the enzyme lecithin-cholesterol acyltransferase (LCAT) that accounts for esterification of most of the free cholesterol in plasma.[2]
See also
References
Further reading
- 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. PMID 806250.
- Cogan DG, Kruth HS, Datilis MB, Martin N (1993). "Corneal opacity in LCAT disease". Cornea. 11 (6): 595–9. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. PMID 3797244.
External links
- Lecithin+Cholesterol+Acyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH)