レシチン・コレステロールアシルトランスフェラーゼ
WordNet
- 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
- an animal sterol that is normally synthesized by the liver; the most abundant steroid in animal tissues (同)cholesterin
PrepTutorEJDIC
- レシチン(神経細胞や卵黄などに含まれるリン脂質)
- 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)』「2014/12/13 12:05:59」(JST)
[Wiki en表示]
Lecithin-cholesterol acyltransferase |
Identifiers |
Symbol |
LCAT |
External IDs |
OMIM: 606967 MGI: 96755 HomoloGene: 68042 ChEMBL: 5942 GeneCards: LCAT Gene |
EC number |
2.3.1.43 |
Gene ontology |
Molecular function |
• phosphatidylcholine-sterol O-acyltransferase activity
• protein binding
• apolipoprotein A-I binding
|
Cellular component |
• extracellular region
• extracellular space
• high-density lipoprotein particle
• extracellular vesicular exosome
|
Biological process |
• phospholipid metabolic process
• phosphatidylcholine biosynthetic process
• cholesterol metabolic process
• cholesterol transport
• very-low-density lipoprotein particle remodeling
• high-density lipoprotein particle remodeling
• cholesterol esterification
• lipoprotein metabolic process
• lipoprotein biosynthetic process
• cholesterol homeostasis
• reverse cholesterol transport
• small molecule metabolic process
• regulation of high-density lipoprotein particle assembly
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Sources: Amigo / QuickGO |
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Orthologs |
Species |
Human |
Mouse |
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Entrez |
3931 |
16816 |
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Ensembl |
ENSG00000213398 |
ENSMUSG00000035237 |
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UniProt |
P04180 |
P16301 |
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RefSeq (mRNA) |
NM_000229 |
NM_008490 |
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RefSeq (protein) |
NP_000220 |
NP_032516 |
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Location (UCSC) |
Chr 16:
67.97 – 67.98 Mb |
Chr 8:
105.94 – 105.94 Mb |
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PubMed search |
[1] |
[2] |
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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.
Contents
- 1 Interactive pathway map
- 2 See also
- 3 References
- 4 Further reading
- 5 External links
Interactive pathway map
Click on genes, proteins and metabolites below to link to respective articles. [§ 1]
[[File:
|{{{bSize}}}px|alt=Statin Pathway edit|]]
- ^ The interactive pathway map can be edited at WikiPathways: "Statin_Pathway_WP430".
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)
Transferases: acyltransferases (EC 2.3)
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2.3.1: other than amino-acyl groups |
- acetyltransferases: Acetyl-Coenzyme A acetyltransferase
- N-Acetylglutamate synthase
- Choline acetyltransferase
- Dihydrolipoyl transacetylase
- Acetyl-CoA C-acyltransferase
- Beta-galactoside transacetylase
- Chloramphenicol acetyltransferase
- N-acetyltransferase
- Serotonin N-acetyl transferase
- HGSNAT
- ARD1A
- Histone acetyltransferase
- palmitoyltransferases: Carnitine O-palmitoyltransferase
- Serine C-palmitoyltransferase
- other: Acyltransferase like 2
- Aminolevulinic acid synthase
- Beta-ketoacyl-ACP synthase
- Glyceronephosphate O-acyltransferase
- Lecithin-cholesterol acyltransferase
- Glycerol-3-phosphate O-acyltransferase
- 1-acylglycerol-3-phosphate O-acyltransferase
- 2-acylglycerol-3-phosphate O-acyltransferase
- ABHD5
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2.3.2: Aminoacyltransferases |
- Gamma-glutamyl transpeptidase
- Peptidyl transferase
- Transglutaminase
- Tissue transglutaminase
- Keratinocyte transglutaminase
- Factor XIII
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2.3.3: converted into alkyl on transfer |
- Citrate synthase
- ATP citrate lyase
- HMG-CoA synthase
- Malate synthase
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- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
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Lipids: lipoprotein particle metabolism
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Lipoprotein particle classes and subclasses |
- delivery of TGs: Chylomicron
- VLDL
- delivery of C and CE: IDL
- LDL
- lb LDL
- sd LDL
- Lp(a)
- HDL
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Apolipoproteins |
- APOA
- APOB
- APOC
- APOD
- APOE
- APOH
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Extracellular enzymes |
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Lipid transfer proteins |
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Cell surface receptors |
- IDL: LRP
- LRP1
- LRP1B
- LRP2
- LRP3
- LRP4
- LRP5
- LRP5L
- LRP6
- LRP8
- LRP10
- LRP11
- LRP12
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ATP-binding cassette transporter |
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mt, k, c/g/r/p/y/i, f/h/s/l/o/e, a/u, n, m
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k, cgrp/y/i, f/h/s/l/o/e, au, n, m, epon
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m (A16/C10), i (k, c/g/r/p/y/i, f/h/s/o/e, a/u, n, m)
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UpToDate Contents
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- 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 [show details]
…transporter, activator of lecithin-cholesterol acyltransferase (LCAT). A-II – Structural protein for HDL; activator of hepatic lipase. A-IV – Activator of lipoprotein lipase (LPL) and LCAT. B-100 – Structural …
- 2. 棘状細胞(棘状赤血球および有棘赤血球)と標的細胞の原因causes of spiculated cells echinocytes and acanthocytes and target cells [show details]
…spherocytes. Target cells are also seen in hereditary LCAT deficiency, a rare autosomal recessive disease due to a mutation in the LCAT gene . As in acquired LCAT deficiency , plasma unesterified cholesterol …
- 3. リポ蛋白および止血因子に対する運動の影響effects of exercise on lipoproteins and hemostatic factors [show details]
…cholesteryl ester transfer protein (CETP) concentration and an elevation in the serum lecithin cholesterol acyltransferase (LCAT) concentration . CETP catalyzes the net flux of cholesterol from HDL-cholesterol …
- 4. 人工透析を受けていない慢性腎臓病患者の脂質管理lipid management in patients with nondialysis chronic kidney disease [show details]
…properties may be different among CKD patients. As an example, there is downregulation of lecithin-cholesterol acyltransferase, which results in reduced esterification of cholesterol and therefore contributes…
- 5. HDLコレステロール:異常値の臨床的側面hdl cholesterol clinical aspects of abnormal values [show details]
…hypertriglyceridemia . Familial LCAT deficiency – After acquisition of free cholesterol onto HDL, the cholesterol is esterified to cholesterol esters by lecithin:cholesterol acyltransferase (LCAT). Patients with homozygous …
English Journal
- Role of apolipoproteins, ABCA1 and LCAT in the biogenesis of normal and aberrant high density lipoproteins.
- Zannis VI1, Su S2, Fotakis P1.
- Journal of biomedical research.J Biomed Res.2017 Nov 4. doi: 10.7555/JBR.31.20160082. [Epub ahead of print]
- PMID 29109329
- ABCA1-Derived Nascent High-Density Lipoprotein-Apolipoprotein AI and Lipids Metabolically Segregate.
- Xu B1, Gillard BK1, Gotto AM Jr1, Rosales C1, Pownall HJ2.
- Arteriosclerosis, thrombosis, and vascular biology.Arterioscler Thromb Vasc Biol.2017 Oct 26. pii: ATVBAHA.117.310290. doi: 10.1161/ATVBAHA.117.310290. [Epub ahead of print]
- PMID 29074589
- A retractable lid in lecithin:cholesterol acyltransferase provides a structural mechanism for activation by apolipoprotein A-I.
- Manthei KA1, Ahn J2, Glukhova A3, Yuan W1, Larkin C2, Manett TD1, Chang L1, Shayman JA1, Axley MJ2, Schwendeman A1, Tesmer JJG4.
- The Journal of biological chemistry.J Biol Chem.2017 Oct 13. pii: jbc.M117.802736. doi: 10.1074/jbc.M117.802736. [Epub ahead of print]
- PMID 29030428
Japanese Journal
- Role of LCAT in Atherosclerosis
- 脂質異常症の遺伝子細胞治療 : LCAT欠損症患者への新規治療法の開発 (代謝) -- (臨床分野での進歩)
- Valosin-containing protein(<i>VCP</i>)遺伝子変異を認めた家族性筋萎縮性側索硬化症の1例
Related Links
- lecithin–cholesterol acyltransferase /lec·i·thin–cho·les·ter·ol ac·yl·trans·fer·ase/ (LCAT) (kah-les´ter-ol a″sil-trans´fer-ās) an enzyme that catalyzes the formation of cholesteryl esters in high-density lipoproteins; deficiency of enzyme ...
- 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 plasma.
★リンクテーブル★
[★]
- 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]
産生臓器
局在
機能
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
[★]
- 英
- lecithin acyltransferase、lecithin cholesterol acyltransferase
- 関
- レシチン・コレステロールアシルトランスフェラーゼ、ホスファチジルコリン・ステロール-O-アシルトランスフェラーゼ、レシチンアシル基転移酵素、レシチン・コレステロールアシル基転移酵素
[★]
ホスファチジルコリン・ステロール-O-アシル転移酵素、ホスファチジルコリン・ステロール-O-アシルトランスフェラーゼ
- 関
- lecithin acyltransferase、lecithin cholesterol acyltransferase
[★]
レシチンアシル基転移酵素、レシチンアシルトランスフェラーゼ
- 関
- lecithin cholesterol acyltransferase、phosphatidylcholine-sterol O-acyltransferase
[★]
- 英
- lecithin cholesterol acyltransferase
- 関
- レシチンアシルトランスフェラーゼ、レシチン・コレステロールアシルトランスフェラーゼ
[★]
レシチン・コレステロールアシルトランスフェラーゼ LCAT
[★]
レシチン・コレステロールアシルトランスフェラーゼ
[★]
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
[★]
コレステロール