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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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Volume 383, Issue 1


Activation of p38 MAP-Kinase and Caldesmon Phosphorylation Are Essential for Urokinase-Induced Human Smooth Muscle Cell Migration

Elena A. Goncharova / Alexander V. Vorotnikov / Elena O. Gracheva / C.-L. Albert Wang / Reynold A. Panettieri Jr. / Victoria V. Stepanova / Vsevolod A. Tkachuk
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/BC.2002.012


We have explored intracellular pathways involved in the urokinase type plasminogen activator (urokinase or uPA)stimulated migration of human airway smooth muscle cells (hAWSMC). Using a set of uPA mutants we found that protease activity, growth factorlike and kringle domains of uPA differentially contribute to activation of p42/p44erk1,2 and p38 MAPkinases. Consistent with our earlier data [Mukhina et al., J. Biol. Chem. 275 (2000), 16450 16458], the kringle domain of uPA was sufficient and required to stimulate cell motility. Here we report that uPA mutants containing the kringle domain specifically activate the p38 MAPkinase pathway and actomyosin by increasing phosphorylation of the critical Ser-19 on the myosin regulatory light chain and MAPkinase sites of the actinassociated regulatory protein caldesmon. While pharmacological inhibition of p38 MAPkinase activation did not affect myosin light chain phosphorylation, it blocked the increase in caldesmon phosphorylation and uPAstimulated migration of hAWSMC on a collagencoated surface. We conclude that activation of p38 MAPkinase and downstream phosphorylation of nonmuscle caldesmon is essential for urokinasestimulated smooth muscle cell migration.

About the article

Published Online: 2005-06-01

Published in Print: 2002-01-23

Citation Information: Biological Chemistry, Volume 383, Issue 1, Pages 115–126, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2002.012.

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