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PMID: 11907028 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Src-mediated inter-receptor cross-talk between the Na+/K+-ATPase and the epidermal growth factor receptor relays the signal from ouabain to mitogen-activated protein kinases.

The Journal of biological chemistry ·Vol. 277 ·No. 21 ·2002-05-24 ·Pages 18694-702

Haas M, Wang H, Tian J, Xie Z

Abstract

Binding of ouabain to Na(+)/K(+)-ATPase activates tyrosine phosphorylation of the epidermal growth factor receptor (EGFR), Src, and p42/44 mitogen-activated protein kinases (MAPKs) in both cardiac myocytes and A7r5 cells. Here, we explored the roles of Src and the EGFR in the ouabain-invoked pathways that lead to the activation of MAPKs. Exposure of A7r5 and LLC-PK1 cells to ouabain caused a dose-dependent inhibition of Na(+)/K(+)-ATPase activity, which correlated well with ouabain-induced activation of Src and MAPKs in these cells. Immunoprecipitation experiments showed that ouabain stimulated Src binding to Na(+)/K(+)-ATPase in a dose- and time-dependent manner and increased phosphorylation of Src at Tyr(418) but had no effect on Tyr(529) phosphorylation. Ouabain failed to activate MAPKs in A7r5 cells that were pretreated with the Src inhibitor PP2 and in SYF cells in which Src family kinases are knocked out. Preincubation with AG1478, but not AG1295, also blocked the effects of ouabain on p42/44 MAPKs in A7r5 cells. Significantly, both herbimycin A and PP2 abrogated ouabain-induced but not epidermal growth factor-induced Src binding to the EGFR and the subsequent EGFR tyrosine phosphorylation. Ouabain also failed to affect tyrosine phosphorylation of the EGFR in SYF cells. In addition, unlike epidermal growth factor, ouabain did not increase EGFR autophosphorylation at Tyr(1173). These findings clearly indicate that ouabain transactivates the EGFR by activation of Src and stimulation of Src binding to the EGFR. Furthermore, we found that the transactivated EGFR was capable of recruiting and phosphorylating the adaptor protein Shc. This resulted in increased binding of another adaptor protein Grb2 to the Src-EGFR complex and the subsequent activation of Ras and MAPKs. Taken together, these new findings suggest that Src mediates the inter-receptor cross-talk between Na(+)/K(+)-ATPase and the EGFR to transduce the signals from ouabain to the Ras/MAPK cascade.

MeSH Terms
Animals Enzyme Activation Enzyme Inhibitors/pharmacology ErbB Receptors/metabolism LLC-PK1 Cells Mitogen-Activated Protein Kinases/metabolism Ouabain/metabolism Phosphorylation Proto-Oncogene Proteins pp60(c-src)/physiology Rats Receptor Cross-Talk Signal Transduction Sodium-Potassium-Exchanging ATPase/antagonists & inhibitors,metabolism Swine
Chemicals
Enzyme Inhibitors Ouabain ErbB Receptors Proto-Oncogene Proteins pp60(c-src) Mitogen-Activated Protein Kinases Sodium-Potassium-Exchanging ATPase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Haas Michael
Department of Pharmacology, Medical College of Ohio, Toledo, Ohio 43614, USA.
Wang Haojie
Tian Jiang
Xie Zijian
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
2002-05-24
Epub
2002-00-20
Pages
18694-702
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
Grants
NHLBI NIH HHS · HL-36573 · United States
NHLBI NIH HHS · HL-63238 · United States
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