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Articles in PresS, published online ahead of print October 31, 2001
Am J Physiol Cell Physiol, 10.1152/ajpcell.00240.2001
Submitted on May 31, 2001
Accepted on October 19, 2001
1 Medicine, UCLA School of Medicine, Los Angeles, CA, USA
* To whom correspondence should be addressed. E-mail: erozengurt{at}mednet.ucla.edu.
The role of G-protein coupled receptors and their ligands in intestinal epithelial cell signaling and proliferation is poorly understood. Here, we demonstrate that arginine vasopressin (AVP) induces multiple intracellular signal transduction pathways in rat intestinal epithelial IEC-18 cells via a V1A receptor. Addition of AVP to these cells induces a rapid and transient increase in cytosolic Ca2+ concentration and promotes protein kinase D (PKD) activation through a PKC-dependent pathway as revealed by in vitro kinase assays and immunoblotting with an antibody that recognizes autophosphorylated PKD at Ser 916. AVP also stimulates the tyrosine phosphorylation of the non-receptor tyrosine kinase Pyk2 and promotes Src-family kinase phosphorylation at Tyr 418, indicative of Src activation. AVP induces ERK-1 (p44mapk) and ERK-2 (p42mapk) activation, a response prevented by treatment with MEK inhibitors (PD 98059 and U0126), specific PKC inhibitors (GF-I and Ro 31-8220), depletion of Ca2+ (EGTA and thapsigargin), selective EGFR tyrosine kinase inhibitors (tyrphostin AG1478, compound 56), or the selective Src-family kinase inhibitor PP-2. Furthermore, AVP acts as a potent growth factor for IEC-18 cells inducing DNA synthesis and cell proliferation through ERK-, Ca2+, PKC, EGFR tyrosine kinase- and Src-dependent pathways.
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