A novel arachidonate-preferring acyl-CoA synthetase is present in steroidogenic cells of the rat adrenal, ovary, and testis

Man Jong Kang, Takahiro Fujino, Hironobu Sasano, Hiroyuki Minekura, Noritaka Yabuki, Hiroshi Nagura, Hiroaki Iijima, Tokuo T. Yamamoto

Research output: Contribution to journalArticle

183 Citations (Scopus)

Abstract

We report herein the cDNA cloning of a novel rat acyl-CoA synthetase (ACS) that preferentially uses arachidonate and eicosapentaenoate. This newly identified ACS (designated ACS4) contains 670 amino acids and is 68% identical to rat ACS3, a previously characterized ACS that is highly expressed in brain. ACS4 was overproduced in Escherichia coli and the resulting enzyme was purified to homogeneity. The purified enzyme utilizes arachidonate and eicosapentaenoate most preferentially among C8-C22 saturated fatty acids and C14-C22 unsaturated fatty acids. Kinetic analyses revealed that the enzyme has a high affinity for arachidonate and eicosapentaenoate and low affinity for palmitate. ACS4 transcripts are detectable in a wide range of tissues, with the highest level in adrenal gland. Immunoreactivity to ACS4 was detected in the zona fasciculata and reticularis of adrenal gland, in the corpus luteum and stromal luteinized cells in ovary, and in the Leydig cells of testis.

Original languageEnglish
Pages (from-to)2880-2884
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume94
Issue number7
DOIs
Publication statusPublished - 1997 Apr 1

Keywords

  • cholesterol ester
  • fatty acid
  • high density lipoprotein
  • leukotrienes
  • prostaglandins

ASJC Scopus subject areas

  • General

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