Premium
Insulin increases membrane protein kinase C activity in rat diaphragm
Author(s) -
Walaas S.I.,
Horn R.S.,
Adler A.,
Albert K.A.,
Walaas O.
Publication year - 1987
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(87)80837-2
Subject(s) - protein kinase c , prkcq , biochemistry , cytosol , protein kinase a , mitogen activated protein kinase kinase , insulin , map2k7 , chemistry , phorbol , phosphorylation , biology , enzyme , cyclin dependent kinase 2 , endocrinology
Calcium/phospholipid‐dependent protein kinase activity (protein kinase C) was identified in rat diaphragm membrane and cytosol fractions by means of in vitro phosphorylation either of histones or of a specific 87 kDa protein substrate, combined with phosphopeptide‐mapping techniques. Both insulin and tumor‐promoting phorbol ester treatment of the diaphragm preparations led to increased protein kinase C activity in the membrane fractions. In contrast to the phorbol ester, however, insulin did not induce a concomitant decrease in cytosolic activity, indicating that translocation of the enzyme had not taken place. Thus, insulin appears to increase specifically membrane protein kinase C activity in rat skeletal muscle, possibly through a mechanism not identical to that induced by phorbol esters.