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Induction of vascular smooth muscle α-isoactin expression in BC3H1 cells
Journal article   Open access   Peer reviewed

Induction of vascular smooth muscle α-isoactin expression in BC3H1 cells

Arthur R Strauch and Peter A Rubenstein
The Journal of biological chemistry, Vol.259(5), pp.3152-3159
1984
DOI: 10.1016/S0021-9258(17)43274-1
PMID: 6699010
url
https://doi.org/10.1016/S0021-9258(17)43274-1View
Published (Version of record) Open Access

Abstract

An isoactin analysis was performed on L-[35S]cysteine labeled BC3H1 cells to determine if these smooth muscle-like cells synthesize vascular smooth muscle actin. Three different NH2-terminal peptides were identified on thin layer electrophoretograms of DNase I-purified and trypsin-digested BC3H1 cell actin. Results obtained from secondary digestion with thermolysin or Staphylococcus aureus V8 protease showed that the most acidic NH2-terminal peptide was derived from vascular smooth muscle alpha-isoactin. Treatment of cell monolayers with serum-free medium caused a 3-fold increase in the level of alpha-isoactin expression and a concomitant decrease in the level of non-muscle beta- and gamma-isoactin. Cell-cell contact was required for induction of alpha-isoactin, and the effects of serum depletion on isoactin expression and cell growth were reversible. The intensity of about 11 out of 500 polypeptide spots on two-dimensional gels of BC3H1 cell polypeptides also was influenced by the culture conditions. The finding that smooth muscle isoactin expression was coupled to cell growth conditions indicate the potential usefulness of BC3H1 cells in studies of isoactin expression and utilization during vascular smooth muscle development.
 Biotechnology Genetic Engineering Fundamental and applied biological sciences. Psychology Biological and medical sciences Methods. Procedures. Technologies Genetic technics

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