scholarly journals The Insulin-Like Growth Factor Receptor I Promotes Motility and Invasion of Bladder Cancer Cells through Akt- and Mitogen-Activated Protein Kinase-Dependent Activation of Paxillin

2010 ◽  
Vol 176 (6) ◽  
pp. 2997-3006 ◽  
Author(s):  
David Metalli ◽  
Francesca Lovat ◽  
Farida Tripodi ◽  
Marco Genua ◽  
Shi-Qiong Xu ◽  
...  
Keyword(s):  
Bladder Cancer ◽  
Growth Factor ◽  
Protein Kinase ◽  
Cancer Cells ◽  
Growth Factor Receptor ◽  
Mitogen Activated Protein Kinase ◽  
Insulin Like Growth Factor ◽  
Bladder Cancer Cells ◽  
Mitogen Activated Protein

scholarly journals Multiple Signaling Pathways of the Insulin-Like Growth Factor 1 Receptor in Protection from Apoptosis

1999 ◽  
Vol 19 (10) ◽  
pp. 7203-7215 ◽  
Author(s):  
Francesca Peruzzi ◽  
Marco Prisco ◽  
Michael Dews ◽  
Paolo Salomoni ◽  
Emanuela Grassilli ◽  
...  
Keyword(s):  
Growth Factor ◽  
Protein Kinase ◽  
Growth Factor Receptor ◽  
Cell Types ◽  
Mitogen Activated Protein Kinase ◽  
Insulin Like Growth Factor ◽  
Phosphatidylinositol 3 Kinase ◽  
Alternative Pathways ◽  
C Terminus ◽  
Mitogen Activated Protein

ABSTRACT The type 1 insulin-like growth factor receptor (IGF-1R), activated by its ligands, protects several cell types from a variety of apoptotic injuries. The main signaling pathway for IGF-1R-mediated protection from apoptosis has been previously elucidated and rests on the activation of phosphatidylinositol 3-kinase, Akt/protein kinase B, and the phosphorylation and inactivation of BAD, a member of the Bcl-2 family of proteins. In 32D cells (a murine hemopoietic cell line devoid of insulin receptor substrate 1 [IRS-1]), the IGF-1R activates alternative pathways for protection from apoptosis induced by withdrawal of interleukin-3. One of these pathways leads to the activation of mitogen-activated protein kinase, while a third pathway results in the mitochondrial translocation of Raf and depends on the integrity of a group of serines in the C terminus of the receptor that are known to interact with 14.3.3 proteins. All three pathways, however, result in BAD phosphorylation. The presence of multiple antiapoptotic pathways may explain the remarkable efficacy of the IGF-1R in protecting cells from apoptosis.

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