Abstract:
:The Na+/Ca2+ exchanger is an important element in the maintenance of calcium homeostasis in bovine chromaffin cells. The Na+/Ca2+ exchanger from other cell types has been extensively studied, but little is known about its regulation in the cell. We have investigated the role of reversible protein phosphorylation in the activity of the Na+/Ca2+ exchanger of these cells. Cells treated with 1 mM dibutyryl cyclic AMP (dbcAMP), 1 microM phorbol 12,13-dibutyrate, 1 microM okadaic acid, or 100 nM calyculin A showed lowered Na+/Ca2+ exchange activity and prolonged cytosolic Ca2+ transients caused by depolarization. A combination of 10 nM okadaic acid and 1 microM dbcAMP synergistically inhibited Na+/Ca2+ exchange activity. Conversely, 50 microM 1-(5-isoquinolinyl-sulfonyl)-2-methylpiperazine, a protein kinase inhibitor, enhanced Na+/Ca2+ exchange activity. Moreover, we used cyclic AMP-dependent protein kinase and calcium phospholipid-dependent protein kinase catalytic subunits to phosphorylate isolated membrane vesicles and found that the Na+/Ca2+ exchange activity was inhibited by this treatment. These results indicate that reversible protein phosphorylation modulates the activity of the Na+/Ca2+ exchanger and suggest that modulation of the exchanger may play a role in the regulation of secretion.
journal_name
J Neurochemjournal_title
Journal of neurochemistryauthors
Lin LF,Kao LS,Westhead EWdoi
10.1046/j.1471-4159.1994.63051941.xsubject
Has Abstractpub_date
1994-11-01 00:00:00pages
1941-7issue
5eissn
0022-3042issn
1471-4159journal_volume
63pub_type
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