PMID: 9164852May 15, 1997Paper

Growth hormone and phorbol esters require specific protein kinase C isoforms to activate mitogen-activated protein kinases in 3T3-F442A cells

The Biochemical Journal
S J MacKenzieE Kilgour

Abstract

Previous studies have shown that the activation of p44 and p42 mitogen-activated protein (MAP) kinases (ERK1 and ERK2) by growth hormone (GH) and phorbol esters, but not by epidermal growth factor, in 3T3-F442A preadipocytes is dependent on protein kinase C (PKC). In the present study two approaches have been taken to determine the PKC isoform dependence of MAP kinase activation in these cells. By immunoblotting with specific antibodies, the cells were found to express PKC-alpha, -gamma,-delta, -epsilon and -zeta. Treatment of cells with 500 nM PMA for 3 h led to the complete depletion of PKC-delta and the partial depletion of PKC-alpha but did not significantly affect the expression of the other PKC isoforms. In parallel, such treatment severely attenuated the ability of GH to activate MAP kinase. The degree of this attenuation was not increased by more prolonged PMA pretreatment, indicating that PKC-delta and perhaps PKC-alpha are important for MAP kinase activation by GH. These experiments further revealed that additional PKC isoforms were required for the full activation of MAP kinases by acute treatment with PMA. A second approach involved the use of anti-sense oligodeoxynucleotides (ODNs) to deplete the individual PKC iso...Continue Reading

Citations

Jan 5, 2002·Expert Opinion on Investigational Drugs·P G Goekjian, M R Jirousek
Jul 18, 2002·Obesity Reviews : an Official Journal of the International Association for the Study of Obesity·S Y Nam, P E Lobie
Oct 13, 2006·American Journal of Physiology. Cell Physiology·Yingxin LiCarol A Heckman
Aug 6, 2002·The Journal of Biological Chemistry·Shaonin JiJoseph L Messina
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