lecithin-cholesterol acyltransferase

レシチン・コレステロールアシルトランスフェラーゼ LCAT

WordNet

1. a yellow phospholipid essential for the metabolism of fats; found in egg yolk and in many plant and animal cells; used commercially as an emulsifier
2. an animal sterol that is normally synthesized by the liver; the most abundant steroid in animal tissues (同)cholesterin

PrepTutorEJDIC

1. レシチン(神経細胞や卵黄などに含まれるリン脂質)
2. コレステロール(胆汁・血液・神経組織などの脂肪性成分)

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/06/29 13:56:35」(JST)

wiki en

[Wiki en表示]

LCAT
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4X96, 4XWG, 4XX1, 5BV7
Identifiers
Aliases	LCAT, entrez:3931
External IDs	OMIM: 606967 MGI: 96755 HomoloGene: 68042 GeneCards: 3931
Gene ontology Molecular function • transferase activity • phospholipase A2 activity • O-acyltransferase activity • apolipoprotein A-I binding • protein binding • transferase activity, transferring acyl groups • phosphatidylcholine-sterol O-acyltransferase activity Cellular component • extracellular space • extracellular region • high-density lipoprotein particle • extracellular exosome Biological process • lipoprotein metabolic process • steroid metabolic process • regulation of high-density lipoprotein particle assembly • response to copper ion • lipid metabolic process • cholesterol transport • response to glucocorticoid • cholesterol metabolic process • cholesterol esterification • high-density lipoprotein particle remodeling • small molecule metabolic process • very-low-density lipoprotein particle remodeling • phospholipid metabolic process • lipoprotein biosynthetic process • cholesterol homeostasis • phosphatidylcholine biosynthetic process • phosphatidylcholine metabolic process • reverse cholesterol transport Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	3931	16816
Ensembl	ENSG00000213398	ENSMUSG00000035237
UniProt	P04180	P16301
RefSeq (mRNA)	NM_000229	NM_008490
RefSeq (protein)	NP_000220.1	NP_032516.2
Location (UCSC)	Chr 16: 67.94 – 67.94 Mb	Chr 8: 105.94 – 105.94 Mb
PubMed search	[1]	[2]
Wikidata
View/Edit Human		View/Edit Mouse

Lecithin–cholesterol acyltransferase (LCAT, also called phosphatidylcholine–sterol O-acyltransferase) 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 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.

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles.

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File:StatinPathway_WP430.png

Statin Pathway edit

See also

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

References

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. PMID 10511297. 
• 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. doi:10.1111/j.1469-1809.1975.tb00617.x. PMID 806250. 
• Cogan DG, Kruth HS, Datilis MB, Martin N (1993). "Corneal opacity in LCAT disease". Cornea 11 (6): 595–9. doi:10.1097/00003226-199211000-00021. 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. doi:10.1016/0014-5793(92)80795-I. 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. doi:10.1016/0006-291X(92)91772-I. 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. doi:10.1016/0006-291X(91)92026-G. 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. doi:10.1016/0140-6736(91)90665-C. 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. doi:10.1172/JCI115612. PMC 442879. 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. doi:10.1016/0006-291X(91)90129-U. 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. doi:10.1073/pnas.88.11.4855. PMC 51765. 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. doi:10.1007/BF00193195. 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. doi:10.1016/0006-291X(87)91090-4. 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. doi:10.1016/0167-4781(87)90066-2. 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. doi:10.1073/pnas.83.8.2335. PMC 323291. 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. doi:10.1111/j.1469-1809.1987.tb01054.x. 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. doi:10.1093/nar/14.23.9397. PMC 311966. PMID 3797244. 

External links

• Lecithin Cholesterol Acyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH)

UpToDate Contents

全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.

• 1. リポ蛋白の分類、代謝、およびアテローム性動脈硬化症における役割 lipoprotein classification metabolism and role in atherosclerosis
• 2. HDLコレステロール：異常値の臨床的側面 hdl cholesterol clinical aspects of abnormal values
• 3. Treatment of lipid abnormalities in patients with nondialysis chronic kidney disease
• 4. アルコール性脂肪性肝炎およびアルコール性肝硬変の臨床症状および診断 clinical manifestations and diagnosis of alcoholic fatty liver disease and alcoholic cirrhosis
• 5. 成人における非アルコール性脂肪性肝疾患（NAFLD）の疫学、臨床的特徴、および診断 epidemiology clinical features and diagnosis of nonalcoholic fatty liver disease in adults

English Journal

• Lecithin-cholesterol acyltransferase in brain: Does oxidative stress influence the 24-hydroxycholesterol esterification?

• La Marca V1, Maresca B2, Spagnuolo MS3, Cigliano L4, Dal Piaz F5, Di Iorio G6, Abrescia P7.
• Neuroscience research.Neurosci Res.2015 Oct 9. pii: S0168-0102(15)00232-1. doi: 10.1016/j.neures.2015.09.008. [Epub ahead of print]
• 24-Hydroxycholesterol (24OH-C) is esterified by the enzyme lecithin-cholesterol acyltransferase (LCAT) in the cerebrospinal fluid (CSF). We report here that the level of 24OH-C esters was lower in CSF of patients with amyotrophic lateral sclerosis than in healthy subjects (54% vs 68% of total 24OH-C
• PMID 26454063

• Lack of LCAT reduces the LPS-neutralizing capacity of HDL and enhances LPS-induced inflammation in mice.

• Petropoulou PI1, Berbée JF1, Theodoropoulos V1, Hatziri A1, Stamou P2, Karavia EA1, Spyridonidis A2, Karagiannides I3, Kypreos KE4.
• Biochimica et biophysica acta.Biochim Biophys Acta.2015 Oct;1852(10 Pt A):2106-15. doi: 10.1016/j.bbadis.2015.07.010. Epub 2015 Jul 10.
• HDL has important immunomodulatory properties, including the attenuation of lipopolysaccharide (LPS)-induced inflammatory response. As lecithin-cholesterol acyltransferase (LCAT) is a critical enzyme in the maturation of HDL we investigated whether LCAT-deficient (Lcat(-/-)) mice present an increase
• PMID 26170061

• Suppression of Remodeling Behaviors with Arachidonic Acid Modification for Enhanced in vivo Antiatherogenic Efficacies of Lovastatin-loaded Discoidal Recombinant High Density Lipoprotein.

• He H1, Zhang M1, Liu L1, Zhang S1, Liu J2, Zhang W2.
• Pharmaceutical research.Pharm Res.2015 Oct;32(10):3415-31. doi: 10.1007/s11095-015-1719-x. Epub 2015 Jun 4.
• PURPOSE: A series of in vitro evaluation in our previous studies had proved that arachidonic acid (AA) modification could suppress the remodeling behaviors of lovastatin-loaded discoidal reconstituted high density lipoprotein (LT-d-rHDL) by restraining the reactivity with lecithin cholesterol acyltr
• PMID 26040661

Japanese Journal

• RSウイルス感染が疑われた育成乳牛における病態指標としての血清レシチン : コレステロールアシルトランスフェラーゼ活性値

• 家畜衛生学雑誌 = The Japanese journal of animal hygiene 42(1), 11-18, 2016-05
• NAID 40020869153

• 疾病治療用タンパク質分泌加工ヒト脂肪細胞の創薬開発と難病治療

• YAKUGAKU ZASSHI 136(5), 705-709, 2016
• NAID 130005148576

• Role of LCAT in Atherosclerosis

• Journal of Atherosclerosis and Thrombosis 23(2), 119-127, 2016
• NAID 130005122035

Related Links

• Lecithin-Cholesterol Acyltransferase Deficiency

The 2 familial forms of lecithin-cholesterol acyltransferase (LCAT) deficiency are termed familial LCAT deficiency (complete LCAT deficiency) and fish eye disease (partial LCAT deficiency). LCAT is an enzyme bound to high-density lipoproteins (HDLs) and low-density lipoproteins (LDLs) in the ...

• LCAT lecithin-cholesterol acyltransferase [Homo sapiens ...

This gene encodes the extracellular cholesterol esterifying enzyme, lecithin-cholesterol acyltransferase. The esterification of cholesterol is required for cholesterol transport. Mutations in this gene have been found to ...

Related Pictures

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★リンクテーブル★

リンク元	「レシチン・コレステロールアシルトランスフェラーゼ」
関連記事	「acyltransferase」「cholesterol」

「レシチン・コレステロールアシルトランスフェラーゼ」

　　[★]

英

lecithin-cholesterol acyltransferase, lecithin cholesterol acyltransferase, LCAT, lecithin:cholesterol acyltransferase

同

レシチンコレステロールアシルトランスフェラーゼ

[show details]

レシチンコレステロールアシル転移酵素 : 32 件
レシチンコレステロールアシル基転移酵素 : 25 件
レシチンコレステロールアシルトランスフェラーゼ : 約 20,100 件

レシチンコレステロールアシル転移酵素 LCAT : 21 件
レシチンコレステロールアシル基転移酵素 LCAT : 28 件
レシチンコレステロールアシルトランスフェラーゼ LCAT : 約 11,200 件

産生臓器

• 肝臓

局在

• 血液(血漿)

機能

• 血漿中にあってコレステロールにアシル基を転移しエステル化する酵素　→　コレステロールエステルの産生
• つまりHDLが有するコレステロールをエステル化する
• ホスファチジルコリンのC-2位の脂肪酸(特にオレイン酸を好む)をコレステロールの3'のヒドロキシ基転移する。基質はHDLであるが、これよりやや劣るがLDLも基質となりうる。 (WIL.1603)

コレステロールエステルの運命

HDLのコレステロールエステルはCETPによりIDL、LDLに受け渡され、肝臓に逆輸送される

臨床関連

• 肝実質細胞の障害

• LCAT活性の低下　→　コレステロールエステルの減少

• レシチン・コレステロールアシルトランスフェラーゼ欠損症(LCAT deficiency)

「acyltransferase」

　　[★]

アシルトランスフェラーゼ、アシル転移酵素、アシル基転移酵素

関

transacylase

「cholesterol」

　　[★] コレステロール