Role of Ca2+-independent phospholipase A2 in exocytosis of amylase from parotid acinar cells.

Abstract:

:We evaluated the role of cytosolic phospholipase A2 (PLA2) in the exocytosis of amylase from parotid acinar cells. The exocytosis stimulated by isoproterenol was dose-dependently inhibited by bromoenol lactone (BEL), a potent suicide inhibitor of Ca2+-independent cytosolic PLA2. The IC50 value of BEL was approximately 7 microM. AACOCF3, a selective inhibitor of Ca2+-dependent cytosolic PLA2, did not inhibit the exocytosis at least up to 30 microM. BEL also inhibited amylase release evoked by forskolin and membrane-permeable cAMP, but it did not inhibit cAMP-dependent protein kinase activity. PLA2 activity in parotid acinar cells was found to be predominantly Ca2+-independent, and was strongly inhibited by BEL, whose IC50 value was approximately 2 microM when it was applied to intact acini. Although isoproterenol scarcely enhanced [3H]arachidonic acid release from intact acinar cells, BEL dose-dependently decreased the basal arachidonic acid release to approximately one half of the control value. These results suggest that the cytosolic Ca2+-independent PLA2 activity plays a role in the membrane fusion process of exocytosis in parotid acinar cells.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Takuma T,Ichida T

doi

10.1093/oxfordjournals.jbchem.a021688

subject

Has Abstract

pub_date

1997-06-01 00:00:00

pages

1018-24

issue

6

eissn

0021-924X

issn

1756-2651

journal_volume

121

pub_type

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