Focal Adhesion-associated Proteins p125FAK and Paxillin Are Substrates for Bradykinin-stimulated Tyrosine Phosphorylation in Swiss 3T3 Cells
(1994) In Journal of Biological Chemistry 269(39). p.24328-24334- Abstract
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... (More)
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.
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- author
- Leeb-Lundberg, L. M Fredrik LU ; Song, Xin Hua and Mathis, Sandra A.
- publishing date
- 1994-09-30
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 269
- issue
- 39
- pages
- 24328 - 24334
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- pmid:7929090
- scopus:0028071784
- ISSN
- 0021-9258
- language
- English
- LU publication?
- no
- id
- 67e8e285-8096-4064-8f4d-da59c9630333
- alternative location
- http://www.jbc.org/content/269/39/24328.abstract
- date added to LUP
- 2019-06-12 11:42:06
- date last changed
- 2024-01-01 09:52:49
@article{67e8e285-8096-4064-8f4d-da59c9630333, abstract = {{<p>In this study we examined the involvement of the focal adhesion-associated proteins p125<sup>FAK</sup> and paxillin as substrates for bradykinin (BK)-stimulated tyrosine phosphorylation in Swiss 3T3 cells and the potential role of protein kinase C and Ca<sup>2+</sup> in these events. BK (1 UM) stimulated tyrosine phosphorylation of p125<sup>FAK</sup> 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 p125<sup>FAK</sup>, 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 p125<sup>FAK</sup> 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 p125<sup>FAK</sup> 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 p125<sup>FAK</sup>, paxillin, RasGAP-associated p125, and src transformation-associated p130.</p>}}, author = {{Leeb-Lundberg, L. M Fredrik and Song, Xin Hua and Mathis, Sandra A.}}, issn = {{0021-9258}}, language = {{eng}}, month = {{09}}, number = {{39}}, pages = {{24328--24334}}, publisher = {{American Society for Biochemistry and Molecular Biology}}, series = {{Journal of Biological Chemistry}}, title = {{Focal Adhesion-associated Proteins p125FAK and Paxillin Are Substrates for Bradykinin-stimulated Tyrosine Phosphorylation in Swiss 3T3 Cells}}, url = {{http://www.jbc.org/content/269/39/24328.abstract}}, volume = {{269}}, year = {{1994}}, }