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Ovarian Kaleidoscope Database (OKdb)

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Fatty Acid Coa Ligase, Long-chain 2 OKDB#: 3019
 Symbols: FACL2 Species: human
 Synonyms: ACS1, LACS, FACL1, FACL2, LACS1, LACS2,LONG-CHAIN ACYL-CoA SYNTHETASE 2, LACS2|PALMITOYL-CoA LIGASE 2|FATTY ACID CoA LIGASE, LONG-CHAIN 1, FACL1|LONG-CHAIN ACYL-CoA SYNTHETASE, LACS|ACYL-CoA SYNTHETASE 1, ACS1|PALMITOYL-CoA LIGASE 1  Locus: 4q34-q35 in Homo sapiens


For retrieval of Nucleotide and Amino Acid sequences please go to: OMIM Entrez Gene
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General Comment NCBI Summary: 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.
General function Enzyme
Comment
Cellular localization Cytoplasmic
Comment
Ovarian function Cumulus cell differentiation, Steroid metabolism
Comment Regulation of Fatty Acid Oxidation in Mouse Cumulus-Oocyte Complexes during Maturation and Modulation by PPAR Agonists. Dunning KR 2014 et al. Fatty acid oxidation is an important energy source for the oocyte; however, little is known about how this metabolic pathway is regulated in cumulus-oocyte complexes. Analysis of genes involved in fatty acid oxidation showed that many are regulated by the luteinizing hormone surge during in vivo maturation, including acyl-CoA synthetases, carnitine transporters, acyl-CoA dehydrogenases and acetyl-CoA transferase, but that many are dysregulated when cumulus-oocyte complexes are matured under in vitro maturation conditions using follicle stimulating hormone and epidermal growth factor. Fatty acid oxidation, measured as production of (3)H2O from [(3)H]palmitic acid, occurs in mouse cumulus-oocyte complexes in response to the luteinizing hormone surge but is significantly reduced in cumulus-oocyte complexes matured in vitro. Thus we sought to determine whether fatty acid oxidation in cumulus-oocyte complexes could be modulated during in vitro maturation by lipid metabolism regulators, namely peroxisome proliferator activated receptor (PPAR) agonists bezafibrate and rosiglitazone. Bezafibrate showed no effect with increasing dose, while rosiglitazone dose dependently inhibited fatty acid oxidation in cumulus-oocyte complexes during in vitro maturation. To determine the impact of rosiglitazone on oocyte developmental competence, cumulus-oocyte complexes were treated with rosiglitazone during in vitro maturation and gene expression, oocyte mitochondrial activity and embryo development following in vitro fertilization were assessed. Rosiglitazone restored Acsl1, Cpt1b and Acaa2 levels in cumulus-oocyte complexes and increased oocyte mitochondrial membrane potential yet resulted in significantly fewer embryos reaching the morula and hatching blastocyst stages. Thus fatty acid oxidation is increased in cumulus-oocyte complexes matured in vivo and deficient during in vitro maturation, a known model of poor oocyte quality. That rosiglitazone further decreased fatty acid oxidation during in vitro maturation and resulted in poor embryo development points to the developmental importance of fatty acid oxidation and the need for it to be optimized during in vitro maturation to improve this reproductive technology. /////////////////////////
Expression regulated by
Comment
Ovarian localization
Comment Tissue-cell- and species-specific expression of gonadotropin-regulated long chain acyl-CoA synthetase (GR-LACS) in gonads, adrenal and brain Identification of novel forms in the brain. Li J,et al . Gonadotropin-regulated long chain acyl-CoA synthetase (GR-LACS) is a novel hormonally regulated fatty acyl-CoA synthetase (FACS) with activity for long-chain fatty acids. The presence of this enzyme in the Leydig cells of the mature rat testis and its mode of regulation suggest that it participates in testicular steroidogenesis. This study demonstrates that GR-LACS expression is tissue, cell and species-specific. The 79kDa GR-LACS protein is expressed in rodent gonads and brain, and only in the mouse in the adrenal cortex. In the ovary of both species it is associated with follicles undergoing atresia. It is present in the newborn and immature testis tubules and after puberty only in the Leydig cells. A distinct GR-LACS protein species of 64kDa that was more abundant than the 79kDa long form was found in the rat brain. Also, a minor 73kDa form was observed in the rat brain and mouse ovary. Two novel species resulting from alternatively splicing of the GR-LACS gene were identified in a rat brain cDNA library: a short form 1 (S1) lacking exon 8 and short form 2 (S2) lacking exons 6-8. Expression studies revealed that the sizes of the S1/S2 proteins are comparable to those of the endogenous variant species. Neither S form contains FACSs activity, suggesting that exon 8 is essential for the enzymatic function. GR-LACS variants exhibit small but significant dominant negative effects on the FACS activity of the long form. GR-LACS variants may regulate the long form's activity in the brain.
Follicle stages
Comment
Phenotypes
Mutations 0 mutations
Genomic Region show genomic region
Phenotypes and GWAS show phenotypes and GWAS
Links
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created: Feb. 15, 2006, 8:47 a.m. by: hsueh   email:
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last update: Feb. 10, 2014, 3:45 p.m. by: hsueh    email:



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