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Long‐Term Activation of Protein Kinase C by Angiotensin II in Cultured Bovine Adrenal Medullary Cells
Author(s) -
Tuominen Raimo K.,
Hudson Pearlie M.,
McMillian Michael K.,
Ye Hong,
Stachowiak Michal K.,
Hong JauShyong
Publication year - 1991
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1991.tb11424.x
Subject(s) - protein kinase c , endocrinology , medicine , angiotensin ii , incubation , receptor , agonist , biology , catecholamine , chemistry , kinase , biochemistry
Previous studies from our laboratory suggest that protein kinase C (PKC) is involved in the angiotensin II (AII)‐induced increase in the expression of genes encoding proen‐kephalin and catecholamine biosynthesizing enzymes in primary cultured bovine adrenal medullary (BAM) cells. The purpose of this study was to examine the effects of [Sar 1 ]‐AII (S 1 ‐AII), an AII agonist, on PKC activity in BAM cells. Thirty‐minute incubation with S 1 ‐AII produced a dose‐dependent activation of PKC. The particulate PKC activity was significantly increased by 2 n M S 1 ‐AII after both 30 min and 12 h of incubation. A high concentration of S 1 ‐AII (200 n M ) caused an increase in particulate PKC activity after 30 min of incubation and this increase was still observed after 18 h of continuous incubation. [Sar 1 ,Thr 8 ]‐angiotensin II (S 1 ,T 8 ‐AII) (100 μ M ), an AII antagonist, inhibited the effect of S 1 ‐AII (20 n M ) on PKC activity, suggesting a specific AII receptor‐mediated effect. An increase in BAM cell particulate PKC immunoreactivity after 18 h of S 1 ‐AII treatment was observed in Western blot analysis of PKC‐immunoreactive protein (82 kDa). The persistent activation of PKC seen in this study is consistent with our hypothesis that PKC may mediate the S 1 ‐AII‐induced increase in the expression of genes encoding proenkephalin and catecholamine synthesizing enzymes in BAM cells.