ACSL4

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Acyl-CoA synthetase long-chain family member 4
Identifiers
Symbols ACSL4 ; ACS4; FACL4; LACS4; MRX63; MRX68
External IDs Template:OMIM5 Template:MGI HomoloGene56282
RNA expression pattern
More reference expression data
Orthologs
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

Acyl-CoA synthetase long-chain family member 4, also known as ACSL4, is a human gene.[1]

The protein encoded by this gene is an isozyme of the long-chain fatty-acid-coenzyme A ligase family. Although differing in substrate specificity, subcellular localization, and tissue distribution, all isozymes of this family convert free long-chain fatty acids into fatty acyl-CoA esters, and thereby play a key role in lipid biosynthesis and fatty acid degradation. This isozyme preferentially utilizes arachidonate as substrate. The absence of this enzyme may contribute to the mental retardation or Alport syndrome. Alternative splicing of this gene generates 2 transcript variants.[1]

References

  1. 1.0 1.1 "Entrez Gene: ACSL4 acyl-CoA synthetase long-chain family member 4".

Further reading

  • Knights KM, Jones ME (1992). "Inhibition kinetics of hepatic microsomal long chain fatty acid-CoA ligase by 2-arylpropionic acid non-steroidal anti-inflammatory drugs". Biochem. Pharmacol. 43 (7): 1465–71. PMID 1567471.
  • Piccini M, Vitelli F, Bruttini M; et al. (1998). "FACL4, a new gene encoding long-chain acyl-CoA synthetase 4, is deleted in a family with Alport syndrome, elliptocytosis, and mental retardation". Genomics. 47 (3): 350–8. doi:10.1006/geno.1997.5104. PMID 9480748.
  • Cao Y, Traer E, Zimmerman GA; et al. (1998). "Cloning, expression, and chromosomal localization of human long-chain fatty acid-CoA ligase 4 (FACL4)". Genomics. 49 (2): 327–30. doi:10.1006/geno.1998.5268. PMID 9598324.
  • Jonsson JJ, Renieri A, Gallagher PG; et al. (1998). "Alport syndrome, mental retardation, midface hypoplasia, and elliptocytosis: a new X linked contiguous gene deletion syndrome?". J. Med. Genet. 35 (4): 273–8. PMID 9598718.
  • Knights KM, Gasser R, Klemisch W (2000). "In vitro metabolism of acitretin by human liver microsomes: evidence of an acitretinoyl-coenzyme A thioester conjugate in the transesterification to etretinate". Biochem. Pharmacol. 60 (4): 507–16. PMID 10874125.
  • Cao Y, Dave KB, Doan TP, Prescott SM (2002). "Fatty acid CoA ligase 4 is up-regulated in colon adenocarcinoma". Cancer Res. 61 (23): 8429–34. PMID 11731423.
  • Meloni I, Muscettola M, Raynaud M; et al. (2002). "FACL4, encoding fatty acid-CoA ligase 4, is mutated in nonspecific X-linked mental retardation". Nat. Genet. 30 (4): 436–40. doi:10.1038/ng857. PMID 11889465.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Longo I, Frints SG, Fryns JP; et al. (2003). "A third MRX family (MRX68) is the result of mutation in the long chain fatty acid-CoA ligase 4 (FACL4) gene: proposal of a rapid enzymatic assay for screening mentally retarded patients". J. Med. Genet. 40 (1): 11–7. PMID 12525535.
  • Sung YK, Hwang SY, Park MK; et al. (2003). "Fatty acid-CoA ligase 4 is overexpressed in human hepatocellular carcinoma". Cancer Sci. 94 (5): 421–4. PMID 12824887.
  • Verot L, Alloisio N, Morlé L; et al. (2004). "Localization of a non-syndromic X-linked mental retardation gene (MRX80) to Xq22-q24". Am. J. Med. Genet. A. 122 (1): 37–41. doi:10.1002/ajmg.a.20221. PMID 12949969.
  • Mashek DG, Bornfeldt KE, Coleman RA; et al. (2005). "Revised nomenclature for the mammalian long-chain acyl-CoA synthetase gene family". J. Lipid Res. 45 (10): 1958–61. doi:10.1194/jlr.E400002-JLR200. PMID 15292367.
  • Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
  • Liang YC, Wu CH, Chu JS; et al. (2005). "Involvement of fatty acid-CoA ligase 4 in hepatocellular carcinoma growth: roles of cyclic AMP and p38 mitogen-activated protein kinase". World J. Gastroenterol. 11 (17): 2557–63. PMID 15849811.
  • Bhat SS, Schmidt KR, Ladd S; et al. (2006). "Disruption of DMD and deletion of ACSL4 causing developmental delay, hypotonia, and multiple congenital anomalies". Cytogenet. Genome Res. 112 (1–2): 170–5. doi:10.1159/000087531. PMID 16276108.
  • Sung YK, Park MK, Hong SH; et al. (2007). "Regulation of cell growth by fatty acid-CoA ligase 4 in human hepatocellular carcinoma cells". Exp. Mol. Med. 39 (4): 477–82. PMID 17934335.

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