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Insulin activates myelin basic protein (p42 MAP) kinase by a protein kinase C‐independent pathway in rat adipocytes
Author(s) -
Yang YunChung,
Farese Robert V.
Publication year - 1993
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(93)80672-h
Subject(s) - protein kinase c , mapk/erk pathway , mapk cascade , protein kinase a , mitogen activated protein kinase kinase , myelin basic protein , mitogen activated protein kinase , ask1 , map kinase kinase kinase , insulin , chemistry , cyclin dependent kinase 9 , phorbol , kinase , microbiology and biotechnology , medicine , endocrinology , myelin , biology , central nervous system
Myelin basic protein kinase (MBPK) activity of rat adipocytes was measured directly or in gels after purification of p42 microtubule‐associated protein kinase (MAPK). Insulin and phorbol esters provoked 2‐ to 3‐fold increases in MBPK/MAPK activity within 5–10 min. Whereas phorbol ester effects were blocked by protein kinase C (PKC) depletion or inhibition, insulin effects were fully intact, indicating that insulin activates MBPK/MAPK independently of PKC. In contrast, PKC depletion or inhibition markedly inhibited insulin effects on [ 3 H]2‐deoxyglucose uptake, suggesting that this effect requires PKC, rather than a factor within the ras/MAPK cascade.