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PDGF-BB-mediated activation of p42MAPK is independent of PDGF b-receptor tyrosine phosphorylation


, : PDGF-BB-mediated activation of p42MAPK is independent of PDGF b-receptor tyrosine phosphorylation. American Journal of Physiology 281(4): 86-L798

Cartel, Nicholas J., Jason Liu, Jinxia Wang, and Martin Post. PDGF-BB-mediated activation of p42MAPK is independent of PDGF b-receptor tyrosine phosphorylation. Am J Physiol Lung Cell Mol Physiol 281: L786-L798, 2001.--Herein, we investigated the activity of mitogen-activated protein kinase (MAPK), a key component of downstream signaling events, which is activated subsequent to platelet-derived growth factor (PDGF)-BB stimulation. Specifically, p42MAPK activity peaked 60 min after addition of PDGF-BB, declined thereafter, and was determined not to be a direct or necessary component of glycosaminoglycan (GAG) synthesis. PDGF-BB also activated MAPK kinase 2 (MAPKK2) but had no effect on MAPKK1 and Raf-1 activity. Chemical inhibition of Janus kinase, phosphatidylinositol 3-kinase, Src kinase, or tyrosine phosphorylation inhibition of the PDGF b-receptor (PDGFR-b) did not abrogate PDGF-BB-induced p42MAPK activation or its threonine or tyrosine phosphorylation. A dominant negative cytoplasmic receptor for hyaluronan-mediated motility variant 4 (RHAMMv4), a regulator of MAPKK-MAPK interaction and activation, did not inhibit PDGF-BB-induced p42MAPK activation nor did a construct expressing PDGFR-b with cytoplasmic tyrosines mutated to phenylalanine. However, overexpression of a dominant negative PDGFR-b lacking the cytoplasmic signaling domain abrogated p42MAPK activity. These results suggest that PDGF-BB-mediated activation of p42MAPK requires the PDGFR-b but is independent of its tyrosine phosphorylation. Reprinted by permission of the publisher.

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