Lecithin–cholesterol acyltransferase

Mammalian protein found in Homo sapiens
LCAT
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

4X96, 4XWG, 4XX1, 5BV7

Identifiers
AliasesLCAT, entrez:3931, lecithin-cholesterol acyltransferase
External IDsOMIM: 606967 MGI: 96755 HomoloGene: 68042 GeneCards: LCAT
Gene location (Human)
Chromosome 16 (human)
Chr.Chromosome 16 (human)[1]
Chromosome 16 (human)
Genomic location for LCAT
Genomic location for LCAT
Band16q22.1Start67,939,750 bp[1]
End67,944,131 bp[1]
Gene location (Mouse)
Chromosome 8 (mouse)
Chr.Chromosome 8 (mouse)[2]
Chromosome 8 (mouse)
Genomic location for LCAT
Genomic location for LCAT
Band8 D3|8 53.06 cMStart106,666,183 bp[2]
End106,670,014 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right lobe of liver

  • tibial nerve

  • left lobe of thyroid gland

  • right lobe of thyroid gland

  • ascending aorta

  • right coronary artery

  • canal of the cervix

  • left coronary artery

  • right lung

  • upper lobe of left lung
Top expressed in
  • left lobe of liver

  • cerebellar cortex

  • yolk sac

  • optic nerve

  • hippocampus proper

  • superior frontal gyrus

  • entorhinal cortex

  • urethra

  • superior colliculus

  • gallbladder
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • transferase activity
  • O-acyltransferase activity
  • apolipoprotein A-I binding
  • protein binding
  • acyltransferase activity
  • phosphatidylcholine-sterol O-acyltransferase activity
Cellular component
  • extracellular region
  • high-density lipoprotein particle
  • extracellular exosome
  • extracellular space
Biological process
  • steroid metabolic process
  • regulation of high-density lipoprotein particle assembly
  • lipid metabolism
  • cholesterol transport
  • cholesterol metabolic process
  • cholesterol esterification
  • very-low-density lipoprotein particle remodeling
  • phospholipid metabolic process
  • lipoprotein biosynthetic process
  • cholesterol homeostasis
  • phosphatidylcholine biosynthetic process
  • phosphatidylcholine metabolic process
  • reverse cholesterol transport
  • high-density lipoprotein particle remodeling
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

3931

16816

Ensembl

ENSG00000213398

ENSMUSG00000035237

UniProt

P04180

P16301

RefSeq (mRNA)

NM_000229

NM_008490

RefSeq (protein)

NP_000220

NP_032516

Location (UCSC)Chr 16: 67.94 – 67.94 MbChr 8: 106.67 – 106.67 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Lecithin–cholesterol acyltransferase (LCAT, also called phosphatidylcholine–sterol O-acyltransferase) is an enzyme, in many animals including humans, 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) (alpha-LCAT) and LDLs (beta-LCAT) in the blood plasma.[5] LCAT deficiency can cause impaired vision due to cholesterol corneal opacities, anemia, and kidney damage.[6] It belongs to the family of phospholipid:diacylglycerol acyltransferases.

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles. [§ 1]

[[File:
Statin_Pathway_WP430go to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to article
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Statin_Pathway_WP430go to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to article
|alt=Statin pathway edit]]
Statin pathway edit
  1. ^ The interactive pathway map can be edited at WikiPathways: "Statin_Pathway_WP430".

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000213398 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000035237 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ "Lecithin-Cholesterol Acyltransferase Deficiency: Overview, Presentation, Differential Diagnosis". 2016-08-08. {{cite journal}}: Cite journal requires |journal= (help)
  6. ^ Reference, Genetics Home. "LCAT gene". Genetics Home Reference. Retrieved 2016-12-11.

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. doi:10.1016/S0022-2275(20)37433-2. 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. S2CID 42785012.
  • 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. S2CID 26714265.
  • 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. doi:10.1093/oxfordjournals.jbchem.a123771. 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. doi:10.1016/S0021-9258(18)42038-8. 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. S2CID 9708282.
  • 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. Bibcode:1991PNAS...88.4855F. 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. S2CID 23994746.
  • 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. doi:10.1016/S0021-9258(18)61472-3. 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. Bibcode:1986PNAS...83.2335M. 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. S2CID 31911235.
  • 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 U.S. National Library of Medicine Medical Subject Headings (MeSH)
  • Overview of all the structural information available in the PDB for UniProt: P04180 (Phosphatidylcholine-sterol acyltransferase) at the PDBe-KB.
  • v
  • t
  • e
2.3.1: other than amino-acyl groups2.3.2: Aminoacyltransferases2.3.3: converted into alkyl on transfer
  • v
  • t
  • e
Lipids: lipoprotein particle metabolism
Lipoprotein particle classes
and subclasses
Apolipoproteins
Extracellular enzymes
Lipid transfer proteins
Cell surface receptors
ATP-binding
cassette transporter


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