Source:http://linkedlifedata.com/resource/pubmed/id/11930938
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2002-4-3
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pubmed:abstractText |
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 factor-like and kringle domains of uPA differentially contribute to activation of p42/p44erk1,2 and p38 MAP-kinases. 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 MAP-kinase pathway and actomyosin by increasing phosphorylation of the critical Ser-19 on the myosin regulatory light chain and MAP-kinase sites of the actin-associated regulatory protein caldesmon. While pharmacological inhibition of p38 MAP-kinase activation did not affect myosin light chain phosphorylation, it blocked the increase in caldesmon phosphorylation and uPA-stimulated migration of hAWSMC on a collagen-coated surface. We conclude that activation of p38 MAP-kinase and downstream phosphorylation of non-muscle caldesmon is essential for urokinase-stimulated smooth muscle cell migration.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Urokinase-Type Plasminogen Activator,
http://linkedlifedata.com/resource/pubmed/chemical/p38 Mitogen-Activated Protein...
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1431-6730
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
383
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
115-26
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11930938-Calmodulin-Binding Proteins,
pubmed-meshheading:11930938-Cell Movement,
pubmed-meshheading:11930938-Humans,
pubmed-meshheading:11930938-Kringles,
pubmed-meshheading:11930938-Mitogen-Activated Protein Kinase 1,
pubmed-meshheading:11930938-Mitogen-Activated Protein Kinase 3,
pubmed-meshheading:11930938-Mitogen-Activated Protein Kinases,
pubmed-meshheading:11930938-Muscle, Smooth, Vascular,
pubmed-meshheading:11930938-Phosphorylation,
pubmed-meshheading:11930938-Protein Structure, Tertiary,
pubmed-meshheading:11930938-Recombinant Proteins,
pubmed-meshheading:11930938-Trachea,
pubmed-meshheading:11930938-Urokinase-Type Plasminogen Activator,
pubmed-meshheading:11930938-p38 Mitogen-Activated Protein Kinases
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pubmed:year |
2002
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pubmed:articleTitle |
Activation of p38 MAP-kinase and caldesmon phosphorylation are essential for urokinase-induced human smooth muscle cell migration.
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pubmed:affiliation |
Laboratory of Cell Motility, Institute of Experimental Cardiology, Russian Cardiology Research Center, Moscow.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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