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PDGF‐BB AND IGF‐I USE DIFFERENT SIGNALING PATHWAYS TO INDUCE NaK‐ATPase SUBUNITS IN CULTURED RAT THORACIC AORTIC SMOOTH MUSCLE CELLS
Author(s) -
Lo Chu S.
Publication year - 1999
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1006/cbir.1999.0345
Subject(s) - genistein , protein subunit , nak , microbiology and biotechnology , growth factor , platelet derived growth factor receptor , phosphorylation , atpase , g alpha subunit , signal transduction , biology , biochemistry , chemistry , medicine , endocrinology , enzyme , receptor , telecommunications link , computer network , computer science , gene
(Na + +K + )‐adenosine triphosphatase (NaK‐ATPase), an ubiquitous membrane transport protein consisting of α and β subunits, regulates Na + /K + fluxes and maintains many vital physiological functions, including cell growth. Results have indicated that platelet‐derived growth factor (PDGF) and insulin‐like growth factor‐I (IGF‐I) both enhance NaK‐ATPase subunits. Genistein, an inhibitor of tyrosine phosphorylation, inhibits serum‐ and PDGF‐BB‐induced NaK‐ATPase α 1 subunit protein levels without inhibiting IGF‐I‐induced NaK‐ATPase α 1 subunit protein levels. These results indicate that PDGF‐BB and IGF‐I utilize separate signaling pathways to induce the synthesis of NaK‐ATPase α 1 subunits. In addition, genistein failed to inhibit PDGF‐BB‐stimulated NaK‐ATPase β 1 subunit levels, suggesting that two separate pathways are involved to induce the synthesis of the NaK‐ATPase α 1 and β 1 subunits, respectively.