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Translocation of protein kinase C in rat islets of Langerhans Effects of a phorbol ester, carbachol and glucose
Author(s) -
Persaud Shanta J.,
Jones Peter M.,
Sugden David,
Howell Simon L.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80196-6
Subject(s) - phorbol ester , protein kinase c , carbachol , chemistry , chromosomal translocation , phorbol , microbiology and biotechnology , islet , medicine , endocrinology , kinase , biochemistry , biology , diabetes mellitus , receptor , gene
In unstimulated rat islets (2 mM glucose), most of the ion‐exchange purified protein kinase C (PKC) activity was associated with the cytosolic fraction. Both carbachol and phorbol myristate acetate caused a significant translocation of PKC activity from cytosolic to membrane fractions, but under the same conditions, glucose (20 mM) did not cause such a redistribution of PKC activity. PMA‐induced translocation of PKC to the membrane fraction was also observed in electrically permeabilised islets, in which recovery of the enzyme activity was enhanced by buffering the intracellular Ca 2+ concentration to 50 nM and supplying the permeabilised islets with protease inhibitors.