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Am J Physiol Cell Physiol (September 4, 2002). doi:10.1152/ajpcell.00233.2002
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Articles in PresS, published online ahead of print September 4, 2002
Am J Physiol Cell Physiol, 10.1152/ajpcell.00233.2002
Submitted on May 21, 2002
Accepted on September 3, 2002

DEVELOPMENTALLY REGULATED EXPRESSION OF CALPONIN ISOFORMS AND THE EFFECT OF H2-CALPONIN ON CELL PROLIFERATION

Moazzem Hossain1, Daw-Yang Hwang1, Qi-Quan Huang1, Yasuharu Sasaki2, and Jian-Ping Jin1*

1 Physiology and Biophysics, Case Western Reserve University, Cleveland, Ohio, USA
2 Pharmacology, Kitasato University, Minatoku, Japan

* To whom correspondence should be addressed. E-mail: jxj12{at}po.cwru.edu.

H2-calponin is found in both smooth muscle and non-muscle cells and its function remains to be established. Western blots using specific monoclonal antibodies detected significant expression of h2-calponin in the growing embryonic stomach and urinary bladder and the early pregnant uterus. While the expression of h1-calponin is up-regulated 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 to the antisense cDNA-transfected or non-transfected cells. Immunofluorescence microscopy showed that the force-expressed h2-calponin was associated with actin-tropomyosin microfilaments. The number of bi-nuclear 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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