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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Morgan, T. E. Lockerbie, R. O. Browning, M. D. Bamburg, J. R. Minamide, L. S. |
| Description | Author Affiliation: Morgan TE ( Department of Biochemistry, Colorado State University, Fort Collins 80523.) |
| Abstract | Actin depolymerizing factor (ADF) is an 18.5-kD protein with pH- dependent reciprocal F-actin binding and severing/depolymerizing activities. We previously showed developing muscle down-regulates ADF (J. R. Bamburg and D. Bray. 1987. J. Cell Biol. 105: 2817-2825). To further study this process, we examined ADF expression in chick myocytes cultured in vitro. Surprisingly, ADF immunoreactivity increases during the first 7-10 d in culture. This increase is due to the presence of a new ADF species with higher relative molecular weight which reacts identically to brain ADF with antisera raised against either brain ADF or recombinant ADF. We have purified both ADF isoforms from myocytes and have shown by peptide mapping and partial sequence analysis that the new isoform is structurally related to ADF. Immunoprecipitation of both isoforms from extracts of cells prelabeled with [32P]orthophosphate showed that the new isoform is radiolabeled, predominantly on a serine residue, and hence is called pADF. pADF can be converted into a form which comigrates with ADF on 1-D and 2-D gels by treatment with alkaline phosphatase. pADF has been quantified in a number of cells and tissues where it is present from approximately 18% to 150% of the amount of unphosphorylated ADF. pADF, unlike ADF, does not bind to G-actin, or affect the rate or extent of actin assembly. Four ubiquitous protein kinases failed to phosphorylate ADF in vitro suggesting that ADF phosphorylation in vivo is catalyzed by a more specific kinase. We conclude that the ability to regulate ADF activity is important to muscle development since myocytes have both pre- and posttranslational mechanisms for regulating ADF activity. The latter mechanism is apparently a general one for cell regulation of ADF activity. |
| ISSN | 00219525 |
| e-ISSN | 15408140 |
| Journal | The Journal of Cell Biology |
| Issue Number | 3 |
| Volume Number | 122 |
| Language | English |
| Publisher | Rockefeller University Press (United States) |
| Publisher Date | 1993-08-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Actins Metabolism Microfilament Proteins Isolation & Purification Muscles Actin Depolymerizing Factors Alkaline Phosphatase Amino Acid Sequence Animals Cell Line Cells, Cultured Chick Embryo Destrin Electrophoresis, Polyacrylamide Gel Epitopes Chemistry Immunology Molecular Sequence Data Cytology Peptide Mapping Phosphorylation Phosphoserine Protein Kinases 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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