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Involvement of the Tyrosine Phosphorylation on GSH Transport in NIH3T3 Fibroblasts
Author(s) -
Iantomasi Teresa,
Favilli Fabio,
Catarzi Serena,
Giani Elisa,
Biagioni Chiara,
Vincenzini Maria
Publication year - 2003
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/1521654031000116040
Subject(s) - vanadate , protein tyrosine phosphatase , phosphorylation , tyrosine phosphorylation , glutathione , phosphatase , platelet derived growth factor receptor , microbiology and biotechnology , receptor tyrosine kinase , tyrosine , mutant , chemistry , biochemistry , tyrosine kinase , growth factor , biology , receptor , enzyme , gene
This study demonstrates the involvement of phosphotyrosine phosphatases on the activity and regulation of GSH ATP‐dependent transport system that we have previously identified in NIH3T3 fibroblasts. This is shown by the fact that increases of the initial rate of GSH uptake were measured in NIH3T3 overexpressing a synthetic gene coding for a low‐Mr‐phosphotyrosine protein phosphatase (LMW‐PTP), while decreases were obtained in NIH3T3 overexpressing the phosphatase inactive mutant (LMW‐C12SPTP), with respect to NIH3T3neo. Moreover, these results have been confirmed by experiments performed in the same cells by vanadate, and H2O2 treatment on both GSH transport and mediated passive transport of glucose. A possible regulation of this transport system by platelet‐derived growth factor receptor (PDGFr) with tyrosine kinase activity is also demonstrated. Moreover, these data show a relationship among GSH, PDGFr and phosphotyrosine phosphatase activity, and suggest a role of GSH transport systems on the cell proliferation process. IUBMB Life, 55: 159‐165, 2003