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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Lin, J. L. Warren, K. S. Lin, J. J. Wamboldt, D. D. |
| Description | Author Affiliation: Warren KS ( Department of Biological Sciences, University of Iowa, Iowa City 52242-1324.) |
| Abstract | Fibroblast caldesmon is a protein postulated to participate in the modulation of the actin cytoskeleton and the regulation of actin-based motility. The cDNAs encoding the NH2-terminal (aa.1-243, CaD40) and COOH-terminal (aa.244-538, CaD39) fragments of human caldesmon were subcloned into expression vectors and we previously reported that bacterially produced CaD39 protein retains its actin-binding properties as well as its ability to enhance low M(r) tropomyosin (TM) binding to actin and to inhibit TM-actin-activated HMM ATPase activity in vitro (Novy, R. E., J. R. Sellers, L.-F. Liu, and J. J.-C. Lin. 1993. Cell Motil. Cytoskeleton. 26:248-261). Bacterially produced CaD40 does not bind actin. To study the in vivo effects of CaD39 expression on the stability of actin filaments in CHO cells, we isolated and characterized stable CHO transfectants which express varying amounts of CaD39. We found that expression of CaD39 in CHO cells stabilized microfilament bundles as well as endogenous TM. CaD39-expressing clones displayed an increased resistance to cytochalasin B and Triton X-100 treatments and yielded increased amounts of TM-containing actin filaments in microfilament isolation procedures. In addition, analysis of these clones with immunoblotting and indirect immunofluorescence microscopy with anti-TM antibody revealed that stabilized endogenous TM and enhanced TM-containing microfilament bundles parallel increased amounts of CaD39 expression. The increased TM observed corresponded to a decrease in TM turnover rate and did not appear to be due to increased synthesis of endogenous TM. Additionally, the phenomenon of stabilized TM did not occur in stable CHO clones expressing CaD40. Therefore, it is likely that CaD39 can enhance TM's binding to F-actin in vivo, thus reducing TM's rate of turnover and stabilizing actin microfilament bundles. |
| ISSN | 00219525 |
| e-ISSN | 15408140 |
| Journal | The Journal of Cell Biology |
| Issue Number | 2 |
| Volume Number | 125 |
| Language | English |
| Publisher | Rockefeller University Press (United States) |
| Publisher Date | 1994-04-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Actin Cytoskeleton Metabolism Actins Calcium Calmodulin-Binding Proteins Calmodulin Tropomyosin Animals Binding Sites Blotting, Western CHO Cells Genetics Cloning, Molecular Cricetinae Cytochalasin B Pharmacology Drug Resistance Fibroblasts Cytology Drug Effects Fluorescent Antibody Technique Peptide Fragments Transfection Research Support, U.S. Gov't, P.H.S. Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Medicine |
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