The distribution and metabolism of arachidonate-containing phospholipids in cellular nuclei

M. E. Surette, F. H. Chilton

Research output: Contribution to journalArticlepeer-review


The nucleus has been identified as the subcellular site to which many arachidonate-metabolizing enzymes are associated following cell activation. However, little is known about the subcellular distribution of arachidonate (AA) itself nor about the location of the central enzyme involved in AA-phospholipid remodeling, CoA-independent transacylase (CoA-IT). Nuclei from human monocyte-like THF-1 cells were isolated and the AA content of phospholipid (PL) subclasses was measured by negative ion chemical ionization GC/MS. Approximately 25% of the cellular AA in THP-1 cells was associated with the nucleus. Pronounced differences were observed in AA-containing phospholipid subclasses of nuclear and non-nuclear membranes.; cell nuclei were enriched in AA-containing 1-acyl-linked PL species whereas other cellular membranes were more enriched in AA-containing PL possessing 1-ether linkages. While whole cells readily remodeled labeled AA from 1-acyl-to 1-ether-linked phospholipids, isolated nuclei were not able to remodel AA incorporated into nuclear membrane PL. Isolated nuclei contained approximately 40% of the total cellular CoA-IT activity. Together, these data reveal that nuclei contain the major donor substrates for the CoA-IT reaction as well as some CoA-IT activity while non-nuclear membranes contain predominantly acceptor substrates for the CoA-IT reaction and some CoA-IT activity. Hence the CoA-IT reaction may be responsible for not only maintaining the distribution of AA among PL subclasses but also for regulating the movement of AA between subcellular locations.

Original languageEnglish (US)
Pages (from-to)A138
JournalFASEB Journal
Issue number3
StatePublished - 1997
Externally publishedYes

ASJC Scopus subject areas

  • Biotechnology
  • Biochemistry
  • Molecular Biology
  • Genetics


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