Document Detail

Inhibition of insulin-like growth factor-I mitogenic action by zinc chelation is associated with a decreased mitogen-activated protein kinase activation in RAT-1 fibroblasts.
MedLine Citation:
PMID:  10338149     Owner:  NLM     Status:  MEDLINE    
The mechanisms responsible for the resistance to the anabolic actions of IGF-I induced by zinc deficiency are not understood. We showed that zinc chelation by DTPA (diethylenetriaminepenta-acetic acid) inhibits [3H]thymidine incorporation stimulated by IGF-I in Rat-1 fibroblasts. This inhibition was specific of zinc chelation since it was prevented by the addition of zinc to DTPA. The stimulation of MAPK, which is crucial for the [3H]thymidine incorporation induced by IGF-I in Rat-1 cells, was partially blunted by DTPA. Therefore, the inhibition of the mitogenic action of IGF-I in Rat-1 fibroblasts by DTPA is potentially caused by decreased MAPK activation by IGF-I.
D Lefebvre; C M Boney; J M Ketelslegers; J P Thissen
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  FEBS letters     Volume:  449     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  1999 Apr 
Date Detail:
Created Date:  1999-06-15     Completed Date:  1999-06-15     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  284-8     Citation Subset:  IM    
Diabetes and Nutrition Unit, Université Catholique de Louvain, Brussels, Belgium.
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MeSH Terms
Calcium-Calmodulin-Dependent Protein Kinases / metabolism*
Cell Division
Cell Line
Chelating Agents / pharmacology
Enzyme Activation
Fibroblasts / drug effects,  metabolism
Insulin-Like Growth Factor I / antagonists & inhibitors,  metabolism*
Isotope Labeling
Pentetic Acid / pharmacology
Zinc / metabolism*
Reg. No./Substance:
0/Chelating Agents; 10028-17-8/Tritium; 67-43-6/Pentetic Acid; 67763-96-6/Insulin-Like Growth Factor I; 7440-66-6/Zinc; EC Protein Kinases

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

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