Source:http://linkedlifedata.com/resource/pubmed/id/20506308
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2010-9-27
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pubmed:abstractText |
Both rat derived vascular smooth muscle cells (SMC) and human myofibroblasts contain ? smooth muscle actin (SMA), but they utilize different mechanisms to contract populated collagen lattices (PCLs). The difference is in how the cells generate the force that contracts the lattices. Human dermal fibroblasts transform into myofibroblasts, expressing ?-SMA within stress fibers, when cultured in lattices that remain attached to the surface of a tissue culture dish. When attached lattices are populated with rat derived vascular SMC, the cells retain their vascular SMC phenotype. Comparing the contraction of attached PCLs when they are released from the culture dish on day 4 shows that lattices populated with rat vascular SMC contract less than those populated with human myofibroblast. PCL contraction was evaluated in the presence of vanadate and genistein, which modify protein tyrosine phosphorylation, and ML-7 and Y-27632, which modify myosin ATPase activity. Genistein and ML-7 had no affect upon either myofibroblast or vascular SMC-PCL contraction, demonstrating that neither protein tyrosine kinase nor myosin light chain kinase was involved. Vanadate inhibited myofibroblast-PCL contraction, consistent with a role for protein tyrosine phosphatase activity with myofibroblast-generated forces. Y-27632 inhibited both SMC and myofibroblast PCL contraction, consistent with a central role of myosin light chain phosphatase.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1097-4644
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pubmed:author | |
pubmed:copyrightInfo |
© 2010 Wiley-Liss, Inc.
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
111
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
362-9
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pubmed:meshHeading |
pubmed-meshheading:20506308-Animals,
pubmed-meshheading:20506308-Biomechanics,
pubmed-meshheading:20506308-Cells, Cultured,
pubmed-meshheading:20506308-Collagen,
pubmed-meshheading:20506308-Humans,
pubmed-meshheading:20506308-Muscle Contraction,
pubmed-meshheading:20506308-Myocytes, Smooth Muscle,
pubmed-meshheading:20506308-Myofibroblasts,
pubmed-meshheading:20506308-Myosin-Light-Chain Phosphatase,
pubmed-meshheading:20506308-Protein Tyrosine Phosphatases,
pubmed-meshheading:20506308-Rats,
pubmed-meshheading:20506308-Species Specificity
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pubmed:year |
2010
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pubmed:articleTitle |
Differences in the mechanism of collagen lattice contraction by myofibroblasts and smooth muscle cells.
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pubmed:affiliation |
Department of Mathematics, Brigham Young University, Provo, Utah 84602-6539, USA. dallon@math.byu.edu
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, N.I.H., Extramural
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