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		<id>https://www.wikidoc.org/index.php?title=Lecithin%E2%80%93cholesterol_acyltransferase&amp;diff=1417204</id>
		<title>Lecithin–cholesterol acyltransferase</title>
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		<updated>2017-11-14T07:53:56Z</updated>

		<summary type="html">&lt;p&gt;38.86.163.9: &lt;/p&gt;
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&lt;div&gt;{{Infobox_gene}}&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;Lecithin–cholesterol acyltransferase&#039;&#039;&#039; (&#039;&#039;&#039;LCAT&#039;&#039;&#039;, also called &#039;&#039;&#039;phosphatidylcholine–sterol O-acyltransferase&#039;&#039;&#039;) 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 [[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) (alpha-LCAT) and LDLs (beta-LCAT) in the [[blood plasma]].&amp;lt;ref&amp;gt;{{Cite journal|date=2016-08-08|title=Lecithin-Cholesterol Acyltransferase Deficiency: Overview, Presentation, Differential Diagnosis|url=http://emedicine.medscape.com/article/122958-overview#a1}}&amp;lt;/ref&amp;gt; [[Lecithin cholesterol acyltransferase deficiency|LCAT deficiency]] can cause impaired vision due to cholesterol corneal opacities, anemia, and kidney damage.&amp;lt;ref&amp;gt;{{Cite web|url=https://ghr.nlm.nih.gov/gene/LCAT|title=LCAT gene|last=Reference|first=Genetics Home|website=Genetics Home Reference|access-date=2016-12-11}}&amp;lt;/ref&amp;gt;&lt;br /&gt;
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==Interactive pathway map==&lt;br /&gt;
{{StatinPathway_WP430|highlight=Lecithin-cholesterol_acyltransferase}}&lt;br /&gt;
&lt;br /&gt;
==See also==&lt;br /&gt;
* [[Lecithin cholesterol acyltransferase deficiency]]&lt;br /&gt;
* [[Sterol O-acyltransferase|Acyl-CoA:cholesterol acyltransferase]] (ACAT)&lt;br /&gt;
&lt;br /&gt;
==References==&lt;br /&gt;
{{Reflist|2}}&lt;br /&gt;
&lt;br /&gt;
==Further reading==&lt;br /&gt;
{{refbegin | 2}}&lt;br /&gt;
* {{cite journal |vauthors=Dobiásová M, Frohlich J | title = Advances in understanding of the role of lecithin cholesterol acyltransferase (LCAT) in cholesterol transport. | journal = Clin Chim Acta | volume = 286 | issue = 1–2 | pages = 257–71 | year = 1999 | pmid = 10511297 | doi = 10.1016/S0009-8981(99)00106-0}}&lt;br /&gt;
*{{cite journal   |vauthors=Kuivenhoven JA, Pritchard H, Hill J, etal |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=  }}&lt;br /&gt;
*{{cite journal  |vauthors=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=[[Clinical Laboratory|Clin. Lab.]] |volume=49 |issue= 11–12 |pages= 601–13 |year= 2004 |pmid= 14651331 |doi=  }}&lt;br /&gt;
*{{cite journal  |vauthors=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=10.1111/j.1469-1809.1975.tb00617.x  }}&lt;br /&gt;
*{{cite journal  |vauthors=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=10.1097/00003226-199211000-00021  }}&lt;br /&gt;
*{{cite journal  |vauthors=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=10.1016/0014-5793(92)80795-I  }}&lt;br /&gt;
*{{cite journal  |vauthors=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=10.1016/0006-291X(92)91772-I  }}&lt;br /&gt;
*{{cite journal   |vauthors=Furukawa Y, Urano T, Hida Y, etal |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=  }}&lt;br /&gt;
*{{cite journal   |vauthors=Minnich A, Collet X, Roghani A, etal |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=  }}&lt;br /&gt;
*{{cite journal   |vauthors=Bujo H, Kusunoki J, Ogasawara M, etal |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=10.1016/0006-291X(91)92026-G  }}&lt;br /&gt;
*{{cite journal   |vauthors=Gotoda T, Yamada N, Murase T, etal |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=10.1016/0140-6736(91)90665-C  }}&lt;br /&gt;
*{{cite journal   |vauthors=Klein HG, Lohse P, Pritchard PH, etal |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=10.1172/JCI115612  | pmc=442879  }}&lt;br /&gt;
*{{cite journal   |vauthors=Maeda E, Naka Y, Matozaki T, etal |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=10.1016/0006-291X(91)90129-U  }}&lt;br /&gt;
*{{cite journal   |vauthors=Funke H, von Eckardstein A, Pritchard PH, etal |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=10.1073/pnas.88.11.4855  | pmc=51765  }}&lt;br /&gt;
*{{cite journal   |vauthors=Taramelli R, Pontoglio M, Candiani G, etal |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=10.1007/BF00193195  }}&lt;br /&gt;
*{{cite journal   |vauthors=Rogne S, Skretting G, Larsen F, etal |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=10.1016/0006-291X(87)91090-4  }}&lt;br /&gt;
*{{cite journal   |vauthors=Tata F, Chaves ME, Markham AF, etal |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=  10.1016/0167-4781(87)90066-2}}&lt;br /&gt;
*{{cite journal   |vauthors=Yang CY, Manoogian D, Pao Q, etal |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=  }}&lt;br /&gt;
*{{cite journal   |vauthors=McLean J, Fielding C, Drayna D, etal |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=10.1073/pnas.83.8.2335  | pmc=323291  }}&lt;br /&gt;
*{{cite journal   |vauthors=Azoulay M, Henry I, Tata F, etal |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=10.1111/j.1469-1809.1987.tb01054.x  }}&lt;br /&gt;
*{{cite journal   |vauthors=McLean J, Wion K, Drayna D, etal |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=10.1093/nar/14.23.9397  | pmc=311966  }}&lt;br /&gt;
{{refend}}&lt;br /&gt;
&lt;br /&gt;
==External links==&lt;br /&gt;
* {{MeshName|Lecithin+Cholesterol+Acyltransferase}}&lt;br /&gt;
&lt;br /&gt;
{{Acyltransferases}}&lt;br /&gt;
{{Lipoprotein metabolism}}&lt;br /&gt;
&lt;br /&gt;
{{DEFAULTSORT:Lecithin-cholesterol acyltransferase}}&lt;br /&gt;
[[Category:Enzymes]]&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
{{transferase-stub}}&lt;/div&gt;</summary>
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