Ethanol Enhances the Stimulatory Effects of Insulin and Insulin-like Growth Factor-I on DNA Synthesis in NIH 3T3 Fibroblasts

1995 ◽  
Vol 208 (1) ◽  
pp. 63-67 ◽  
Author(s):  
M. Tomono ◽  
Z. Kiss
Keyword(s):  
Growth Factor ◽  
Dna Synthesis ◽  
Insulin Like Growth Factor ◽  
Factor I ◽  
3T3 Fibroblasts ◽  
Growth Factor I ◽  
Nih 3T3

Expression of human choline kinase in NIH 3T3 fibroblasts increases the mitogenic potential of insulin and insulin-like growth factor I

2000 ◽  
Vol 12 (5) ◽  
pp. 279-288 ◽  
Author(s):  
Taeowan Chung ◽  
Jin-Sheng Huang ◽  
Jagat J. Mukherjee ◽  
Karan S. Crilly ◽  
Zoltan Kiss
Keyword(s):  
Growth Factor ◽  
Choline Kinase ◽  
Insulin Like Growth Factor ◽  
Factor I ◽  
3T3 Fibroblasts ◽  
Growth Factor I ◽  
Nih 3T3 ◽  
Mitogenic Potential

scholarly journals Protein Kinase C-δ Is an Important Signaling Molecule in Insulin-Like Growth Factor I Receptor-Mediated Cell Transformation

1998 ◽  
Vol 18 (10) ◽  
pp. 5888-5898 ◽  
Author(s):  
Weiqun Li ◽  
Yi-Xing Jiang ◽  
Jiachang Zhang ◽  
Lilian Soon ◽  
Lawrence Flechner ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Growth Factor ◽  
Protein Kinase ◽  
Transcriptional Activation ◽  
Cell Transformation ◽  
Insulin Like Growth Factor ◽  
Factor I ◽  
Kinase C ◽  
Growth Factor I ◽  
Nih 3T3

ABSTRACT To investigate the potential role of protein kinase C-δ (PKC-δ) in insulin-like growth factor I receptor (IGF-IR)-mediated cell transformation, an oncogenic gag-IGF-IR β-fusion receptor lacking the entire extracellular domain, which was designated NM1, and a full-length IGF-IR were coexpressed with either wild-type PKC-δ (PKC-δWT) or an ATP-binding mutant of PKC-δ (PKC-δK376R) in NIH 3T3 fibroblasts. While overexpression of PKC-δWT did not affect NM1- and IGF-IR-induced focus and colony formation of NIH 3T3 cells, expression of PKC-δK376R severely impaired these events. In contrast, NM1-mediated cell growth in monolayer was not affected by coexpressing PKC-δK376R. PKC-δWT and PKC-δK376R were constitutively phosphorylated on a tyrosine residue(s) in the NM1- and IGF-IR-expressing cells and were associated with them in an IGF-I-independent manner. Activated IGF-IR was able to phosphorylate purified PKC-δ in vitro and stimulated its kinase activity. Furthermore, the level of endogenous PKC-δ protein was up-regulated through transcriptional activation in response to long-term IGF-IR activation. Taken together, our results demonstrate that PKC-δ plays an important role in IGF-IR-mediated cell transformation, probably via association of the receptor with PKC-δ and its activation through protein up-regulation and tyrosine phosphorylation. Competition with endogenous PKC-δ for NM1 and IGF-IR association by PKC-δK376R is probably an important mechanism underlying the PKC-δK376R-mediated inhibition of cell transformation by NM1 and IGF-IR.

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