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Protein kinase Calpha regulates insulin receptor signaling in skeletal muscle.

Abstract：

:Certain PKC isoforms are stimulated by insulin and interact with IR as well as with IRS, but it is still not clear if specific PKC isoforms regulate IR signaling directly or through IRS-1. PKCalpha may regulate IRS activity in response to insulin. We investigated the possibility that PKCalpha may be important in insulin signaling. Studies were conducted on skeletal muscle in adult mice and on L6 skeletal cells. PKCalpha is constitutively associated with IRS-1, and insulin stimulation of PKCalpha causes disassociation of the two proteins within 5 min. Blockade of PKCalpha inhibited insulin-induced disassociation of PKCalpha from IRS1. Selective inhibition of PKCalpha increased the ability of insulin to reduce blood glucose levels. Insulin stimulation activates PKB and increases the association of PKCalpha with PKB. Blockade of PKCalpha increased threonine phosphorylation of PKB. We suggest that PKCalpha regulates insulin signaling in skeletal muscle through its disassociation from IRS-1 and association with PKB.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Cipok M,Aga-Mizrachi S,Bak A,Feurstein T,Steinhart R,Brodie C,Sampson SR

doi

10.1016/j.bbrc.2006.05.008

subject

Has Abstract

pub_date

2006-06-30 00:00:00

pages

817-24

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(06)01049-7

journal_volume

345

pub_type

杂志文章

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