Focal Adhesion-associated Proteins p125FAK and Paxillin Are Substrates for Bradykinin-stimulated Tyrosine Phosphorylation in Swiss 3T3 Cells

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Focal Adhesion-associated Proteins p125FAK and Paxillin Are Substrates for Bradykinin-stimulated Tyrosine Phosphorylation in Swiss 3T3 Cells. / Leeb-Lundberg, L. M Fredrik; Song, Xin Hua; Mathis, Sandra A.

In: Journal of Biological Chemistry, Vol. 269, No. 39, 30.09.1994, p. 24328-24334.

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T1 - Focal Adhesion-associated Proteins p125FAK and Paxillin Are Substrates for Bradykinin-stimulated Tyrosine Phosphorylation in Swiss 3T3 Cells

AU - Leeb-Lundberg, L. M Fredrik

AU - Song, Xin Hua

AU - Mathis, Sandra A.

PY - 1994/9/30

Y1 - 1994/9/30

N2 - In this study we examined the involvement of the focal adhesion-associated proteins p125FAK and paxillin as substrates for bradykinin (BK)-stimulated tyrosine phosphorylation in Swiss 3T3 cells and the potential role of protein kinase C and Ca2+ in these events. BK (1 UM) stimulated tyrosine phosphorylation of p125FAK and paxillin. In addition, BK also increased the phosphotyrosine content of the src transformation-associated protein p130. The responses were rapid and transient and peaked at ∼1 min after BK addition. Furthermore, the responses were dose-dependent with half-maximal effects occurring at 1-10 nM BK. The phosphotyrosine content of p125FAK, paxillin, and p130 was also increased following stimulation with phorbol 12-myristate 13-acetate (PMA) (0.1 μM). In contrast, PMA had no effect on the phosphotyrosine content of p125, a Ras-GAP-associated tyrosine phosphoprotein that we recently identified. Long term pretreatment (18 h) of cells with 0.3 μM PMA partially attenuated BK-stimulated phosphorylation of p125FAK but was without effect on phosphorylation of paxillin and Ras-GAP-associated p125. Furthermore, only a small inhibition of BK- and PMA-stimulated phosphorylation of p125FAK was observed following pretreatment with 25 μM BAPTA/AM. In all, these results show that multiple mechanisms are involved in BK-stimulated tyrosine phosphorylation of p125FAK, paxillin, RasGAP-associated p125, and src transformation-associated p130.

AB - In this study we examined the involvement of the focal adhesion-associated proteins p125FAK and paxillin as substrates for bradykinin (BK)-stimulated tyrosine phosphorylation in Swiss 3T3 cells and the potential role of protein kinase C and Ca2+ in these events. BK (1 UM) stimulated tyrosine phosphorylation of p125FAK and paxillin. In addition, BK also increased the phosphotyrosine content of the src transformation-associated protein p130. The responses were rapid and transient and peaked at ∼1 min after BK addition. Furthermore, the responses were dose-dependent with half-maximal effects occurring at 1-10 nM BK. The phosphotyrosine content of p125FAK, paxillin, and p130 was also increased following stimulation with phorbol 12-myristate 13-acetate (PMA) (0.1 μM). In contrast, PMA had no effect on the phosphotyrosine content of p125, a Ras-GAP-associated tyrosine phosphoprotein that we recently identified. Long term pretreatment (18 h) of cells with 0.3 μM PMA partially attenuated BK-stimulated phosphorylation of p125FAK but was without effect on phosphorylation of paxillin and Ras-GAP-associated p125. Furthermore, only a small inhibition of BK- and PMA-stimulated phosphorylation of p125FAK was observed following pretreatment with 25 μM BAPTA/AM. In all, these results show that multiple mechanisms are involved in BK-stimulated tyrosine phosphorylation of p125FAK, paxillin, RasGAP-associated p125, and src transformation-associated p130.

UR - http://www.scopus.com/inward/record.url?scp=0028071784&partnerID=8YFLogxK

M3 - Article

VL - 269

SP - 24328

EP - 24334

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 1083-351X

IS - 39

ER -