A novel arachidonic acid-selective cytosolic PLA2 contains a Ca2+-dependent translocation domain with homology to PKC and GAP

We report the cloning and expression of a cDNA encoding a high molecular weight cytosolic phospholipase A2 that has no detectable sequence homology with the secreted forms of PLA2

James D. Clark; Lih-Ling Lin; Ronald W. Kriz; Chakkodabylu S. Ramesha; Lisa A. Sultzman; Alice Y. Lin; Nina Milona; John L. Knopf

2004

Scholarcy highlights

  • We report the cloning and expression of a cDNA encoding a high molecular weight cytosolic phospholipase A2 that has no detectable sequence homology with the secreted forms of PLA2
  • We show that cytosolic phospholipase A2 selectively cleaves arachidonic acid from natural membrane vesicles and demonstrate that cPLA2 translocates to membrane vesicles in response to physiologically relevant changes in free calcium
  • We demonstrate that an amino-terminal 140 amino acid fragment of cPLA2 translocates to natural membrane vesicles in a Ca2+-dependent fashion. We note that this 140 amino acid domain of cPLA2 contains a 45 amino acid region with homology to PKC, p65, GAP, and PLC
  • We suggest that this homology delineates a Ca2+-dependent phospholipid-binding motif, providing a mechanism for the second messenger Ca2+ to translocate and activate cytosolic proteins
  • We recommend that commenters identify themselves with full names and affiliations

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