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Articles in PresS, published online ahead of print February 6, 2002
Am J Physiol Cell Physiol, 10.1152/ajpcell.00323.2001
Submitted on July 17, 2001
Accepted on February 1, 2002
1 Departments of Pediatrics and Medicine, UCLA School of Medicine, Los Angeles, CA, USA
* To whom correspondence should be addressed. E-mail: erozengurt{at}mednet.ucla.edu.
The G protein-coupled receptor agonists angiotensin II (Ang II) and lysophosphatidic acid (LPA) rapidly induce tyrosine phosphorylation of the cytosolic proline-rich tyrosine kinase 2 (Pyk2) in IEC-18 intestinal epithelial cells. The combined Pyk2 tyrosine phosphorylation induced by phorbol 12,13 dibutyrate, a direct agonist of protein kinase C (PKC), and ionomycin, a Ca2+ ionophore, was equal to that induced by Ang II. Inhibition of either PKC or Ca2+ signaling attenuated the effect of Ang II and LPA, though simultaneous inhibition of both pathways failed to completely abolish Pyk2 tyrosine phosphorylation. Cytochalasin D, which disrupts stress fibers, strongly inhibited the response of Pyk2 to Ang II or LPA. The distinct Rho-associated kinase (ROK) inhibitors HA-1077 and Y-27632, as well as the Rho inhibitor Clostridium botulinum C3 exoenzyme, also significantly attenuated Ang II- and LPA-stimulated Pyk2 tyrosine phosphorylation. Simultaneous inhibition of PKC, Ca2+, and either actin assembly or ROK completely abolished the Pyk2 response. Together these results show that Ang II and LPA rapidly induce Pyk2 tyrosine phosphorylation in intestinal epithelial cells via separate Ca2+-, PKC-, and Rho-mediated pathways.
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