Document Detail


The small GTPase Rac suppresses apoptosis caused by serum deprivation in fibroblasts.
MedLine Citation:
PMID:  11474575     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
BACKGROUND: The small GTPase Rac1 is a key signaling protein that mediates a number of important physiologic functions including the organization of the actin cytoskeleton, lipid metabolism, and gene transcription. Rac1 has also been implicated in oncogenic transformation. Expression of constitutively active Rac1 in Rat1 fibroblasts elicits serum- and anchorage-independent growth and causes tumorigenicity in nude mice. The signaling pathways that mediate the role of Rac in cell transformation remain to be identified. Here, we study the role of Rac in cell survival in the absence of serum. MATERIALS AND METHODS: The cell lines used in this study are Ratl fibroblasts that express constitutively active or dominant negative mutants of Rac1. We used long-term video time-lapse microscopy to analyze the effects of these Rac1 mutants on mitogenicity and apoptosis. RESULTS: We show that the increase in viability, which is stimulated by Rac1 in the absence of serum, is predominantly caused by an inhibition of apoptosis, with a minor increase in cell division. We also show that Rac1-stimulated cell viability in serum-starved cells is inhibited by chemical inhibition of phosphatidylinositol 3-kinase. CONCLUSIONS: Our observations indicate a role for Rac1 in survival signaling, possibly via activation of phosphatidylinositol 3-kinase. We propose that Rac1-stimulated cell survival may contribute to the role of Rac1 in serum-independent growth and cell transformation.
Authors:
R Ruggieri; Y Y Chuang; M Symons
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Molecular medicine (Cambridge, Mass.)     Volume:  7     ISSN:  1076-1551     ISO Abbreviation:  Mol. Med.     Publication Date:  2001 May 
Date Detail:
Created Date:  2001-07-27     Completed Date:  2001-12-05     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  9501023     Medline TA:  Mol Med     Country:  United States    
Other Details:
Languages:  eng     Pagination:  293-300     Citation Subset:  IM    
Affiliation:
Onyx Pharmaceuticals, Richmond, CA, USA. mruggieri@picower.edu
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MeSH Terms
Descriptor/Qualifier:
1-Phosphatidylinositol 3-Kinase / antagonists & inhibitors,  metabolism*
Animals
Apoptosis / physiology*
Cell Division / physiology
Cell Survival / physiology
Cells, Cultured
Culture Media, Serum-Free / metabolism
Enzyme-Linked Immunosorbent Assay
Fibroblasts / cytology,  enzymology*
GTPase-Activating Proteins / antagonists & inhibitors*
Genes, Reporter
Immune Sera
In Situ Nick-End Labeling
JNK Mitogen-Activated Protein Kinases*
MAP Kinase Kinase 4
Microscopy, Video
Mitogen-Activated Protein Kinase Kinases / physiology
Mutation
Phosphorylation
Protein Binding
Rats
Signal Transduction
rac1 GTP-Binding Protein / antagonists & inhibitors,  physiology*
Chemical
Reg. No./Substance:
0/Culture Media, Serum-Free; 0/GTPase-Activating Proteins; 0/Immune Sera; EC 2.7.1.137/1-Phosphatidylinositol 3-Kinase; EC 2.7.11.24/JNK Mitogen-Activated Protein Kinases; EC 2.7.12.2/MAP Kinase Kinase 4; EC 2.7.12.2/Mitogen-Activated Protein Kinase Kinases; EC 3.6.5.2/rac1 GTP-Binding Protein

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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