Source:http://linkedlifedata.com/resource/pubmed/id/12388067
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2002-12-11
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pubmed:abstractText |
h2-calponin is found in both smooth muscle and nonmuscle cells, and its function remains to be established. Western blots with specific monoclonal antibodies detected significant expression of h2-calponin in the growing embryonic stomach and urinary bladder and the early pregnant uterus. Although the expression of h1-calponin is upregulated in the stomach and bladder during postnatal development, the expression of h2-calponin is decreased to low levels in quiescent smooth muscle cells. To investigate a hypothesis that h2-calponin regulates the function of the actin cytoskeleton during cytokinesis, a smooth muscle-originated cell line (SM3) lacking calponin was transfected to express either sense or antisense h2-calponin cDNA and the effects on the rates of cell proliferation were examined. Both stable and transient sense cDNA-transfected cells had a significantly decreased proliferation rate compared with the antisense cDNA-transfected or nontransfected cells. Immunofluorescence microscopy showed that the force-expressed h2-calponin was associated with actin-tropomyosin microfilaments. The number of binuclear cells was significantly greater in the sense cDNA-transfected culture, in which h2-calponin was concentrated in a nuclear ring structure formed by actin filaments. The results suggest that h2-calponin may regulate cytokinesis by inhibiting the activity of the actin cytoskeleton.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Growth Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/calponin
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0363-6143
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
284
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
C156-67
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12388067-Animals,
pubmed-meshheading:12388067-Calcium-Binding Proteins,
pubmed-meshheading:12388067-Cell Division,
pubmed-meshheading:12388067-Cell Line, Transformed,
pubmed-meshheading:12388067-Female,
pubmed-meshheading:12388067-Gene Expression Regulation, Developmental,
pubmed-meshheading:12388067-Growth Inhibitors,
pubmed-meshheading:12388067-Mice,
pubmed-meshheading:12388067-Mice, Inbred C57BL,
pubmed-meshheading:12388067-Microfilament Proteins,
pubmed-meshheading:12388067-Muscle, Smooth,
pubmed-meshheading:12388067-Pregnancy,
pubmed-meshheading:12388067-Protein Isoforms,
pubmed-meshheading:12388067-Rabbits,
pubmed-meshheading:12388067-Stomach,
pubmed-meshheading:12388067-Transfection,
pubmed-meshheading:12388067-Uterus
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pubmed:year |
2003
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pubmed:articleTitle |
Developmentally regulated expression of calponin isoforms and the effect of h2-calponin on cell proliferation.
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pubmed:affiliation |
Department of Physiology and Biophysics, Case Western Reserve University School of Medicine, 10900 Euclid Avenue, Cleveland, OH 44106-4970, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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