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(Received for publication, October 9, 1996, and in revised form, February 10, 1997)
From the Mass Spectrometry Resource, Divisions of Endocrinology,
Diabetes, and Metabolism and of Laboratory Medicine, Departments of
Medicine and Pathology, Washington University School of Medicine,
St. Louis, Missouri 63110
Pancreatic islets express a
Ca2+-independent phospholipase A2
(CaI-PLA2) activity that is sensitive to inhibition by a
haloenol lactone suicide substrate that also attenuates glucose-induced hydrolysis of arachidonic acid from islet phospholipids and insulin secretion. A cDNA has been cloned from a rat islet cDNA library that encodes a protein with a deduced amino acid sequence of 751 residues that is homologous to a CaI-PLA2 enzyme recently
cloned from Chinese hamster ovary cells. Transient transfection of both COS-7 cells and Chinese hamster ovary cells with the cloned islet CaI-PLA2 cDNA resulted in an increase in cellular
CaI-PLA2 activity, and this activity was susceptible to
inhibition by haloenol lactone suicide substrate. The domain of the
islet CaI-PLA2 from amino acid residues 150-414 is
composed of eight stretches of a repeating sequence motif of
approximately 33-amino acid residues in length that is highly
homologous to domains of ankyrin that bind both tubulin and integral
membrane proteins, including several proteins that regulate ionic
fluxes across membranes. These findings complement previous
pharmacologic observations that suggest that CaI-PLA2 may
participate in regulating transmembrane ion flux in glucose-stimulated
Volume 272, Number 17,
Issue of April 25, 1997
pp. 11118-11127
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
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