Insulin stimulates novel protein kinase C in rat adipocytes.
Insulin is known to rapidly stimulate and/or translocate Ca2+/phospholipid-dependent protein kinase (conventional PKC; cPKC) in rat adipocytes. Presently we examined whether insulin also stimulates/translocates Ca(2+)-independent, phospholipid-dependent protein kinase (novel PKC; nPKC). Total Mono Q column-elutable nPKC (like cPKC) activities were decreased in cytosolic and increased in membrane fractions with insulin treatment. Immunoblot study of novel PKC epsilon also showed insulin-induced translocation of immunoreactive PKC from cytosol to membrane, similar to the translocation of cPKC, PKC beta. These results suggest that nPKC has an important role in insulin-induced signal transduction.
Ishizuka
T
T
Third Department of Internal Medicine, Gifu University School of Medicine, Japan.
Yamamoto
M
M
Kajita
K
K
Nagashima
T
T
Yasuda
K
K
Miura
K
K
Cooper
D R
DR
Farese
R V
RV
D000273:Adipose Tissue / Q000187:drug effects / Q000201:enzymology*; D000818:Animals; D001692:Biological Transport; D015153:Blotting, Western; D002462:Cell Membrane / Q000201:enzymology; D003600:Cytosol / Q000201:enzymology; D007328:Insulin / Q000494:pharmacology*; D007527:Isoenzymes; D005810:Multigene Family; D011493:Protein Kinase C / Q000187:drug effects / Q000302:isolation & purification / Q000378:metabolism*; D051381:Rats; D013234:Stem Cells / Q000187:drug effects / Q000201:enzymology*
D007328:Insulin; D007527:Isoenzymes; D011493:Protein Kinase C