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J. Biol. Chem., Vol. 276, Issue 16, 13198-13208, April 20, 2001
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From the Mass Spectrometry Resource, Division of Endocrinology,
Diabetes, and Metabolism, Department of Medicine, Washington University
School of Medicine, St. Louis, Missouri 63110
A cytosolic 84-kDa group VIA phospholipase
A2 (iPLA2
Studies of Insulin Secretory Responses and of Arachidonic Acid
Incorporation into Phospholipids of Stably Transfected Insulinoma Cells
That Overexpress Group VIA Phospholipase A2
(iPLA2
) Indicate a Signaling Rather Than a Housekeeping
Role for iPLA2*
) that does not require
Ca2+ for catalysis has been cloned from several sources,
including rat and human pancreatic islet -cells and murine P388D1
cells. Many potential iPLA2 functions have been
proposed, including a signaling role in -cell insulin secretion and
a role in generating lysophosphatidylcholine acceptors for arachidonic
acid incorporation into P388D1 cell phosphatidylcholine (PC). Proposals
for iPLA2 function rest in part on effects of inhibiting
iPLA2 activity with a bromoenol lactone (BEL) suicide
substrate, but BEL also inhibits phosphatidate phosphohydrolase-1 and a
group VIB phospholipase A2. Manipulation of
iPLA2 expression by molecular biologic means is an
alternative approach to study iPLA2 functions, and we
have used a retroviral construct containing iPLA2
cDNA to prepare two INS-1 insulinoma cell clonal lines that stably
overexpress iPLA2. Compared with parental INS-1 cells or
cells transfected with empty vector, both
iPLA2-overexpressing lines exhibit amplified insulin
secretory responses to glucose and cAMP-elevating agents, and BEL
substantially attenuates stimulated secretion. Electrospray ionization
mass spectrometric analyses of arachidonic acid incorporation into
INS-1 cell PC indicate that neither overexpression nor inhibition of
iPLA2 affects the rate or extent of this process in
INS-1 cells. Immunocytofluorescence studies with antibodies directed against iPLA2 indicate that cAMP-elevating agents
increase perinuclear fluorescence in INS-1 cells, suggesting that
iPLA2 associates with nuclei. These studies are more
consistent with a signaling than with a housekeeping role for
iPLA2 in insulin-secreting -cells.
*
This work was supported by National Institutes of Health
Grants R37-DK-34388, P41-RR00954, PO1-HL57278, P60-DK20579, and
P30-DK56341; by Career Development Award 2-1999-55 (to Z. M.) from
the Juvenile Diabetes Foundation; and by a grant from the American
Diabetes Association.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Box 8127, Washington University School of Medicine, 660 S. Euclid Ave., St.
Louis, MO 63110. Tel.: 314-362-8190; Fax: 314-362-8188; E-mail:
jturk@imgate.wustl.edu.
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