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J. Biol. Chem., Vol. 263, Issue 32, 16645-16651, 11, 1988
JH Gronich, JV Bonventre and RA Nemenoff
The activity of phospholipase A2 (PLA2), the regulatory enzyme in
arachidonic acid release and prostaglandin synthesis, was measured in
cell-free extracts of rat renal mesangial cells. Arginine vasopressin (AVP)
and phorbol myristate acetate (PMA) both stimulated PLA2 activity as
assayed by the release of free arachidonic acid from exogenously added
[14C]arachidonyl-phosphatidylcholine. This represents a direct in vitro
demonstration of hormone-induced changes in PLA2 activity. The stimulated
activity was recovered following fractionation by DEAE- cellulose anion
exchange and FPLC Superose 12 gel filtration. Stimulated activity from AVP-
and PMA-treated cells comigrated as a single peak, suggesting that these
agents are stimulating a single form of the enzyme. The molecular weight of
this hormonally regulated form of PLA2 is approximately 60,000. The enzyme
has an obligate requirement for Ca2+, having no activity in the presence of
EGTA, and has a pH optimum in the alkaline range. Following cell disruption
in the presence of chelators, the enzyme is recovered in a high speed
supernatant. However, it appears that it can bind to a crude membrane
fraction in a Ca2+-dependent manner, similar to other Ca2+-phospholipid
binding proteins. The observed stable modification in PLA2 activity by AVP
and PMA suggests a phosphorylation of PLA2 or PLA2 modulators by protein
kinase C.
Identification and characterization of a hormonally regulated form of phospholipase A2 in rat renal mesangial cells
Howard Hughes Medical Institute Laboratories, Harvard Medical School, Boston, Massachusetts 02114.
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