Phorbol ester-induced down-regulation of the 80-kDa myristoylated alanine-rich C-kinase substrate-related protein in Swiss 3T3 fibroblasts. Inhibition by staurosporine
| Autor: | Friedrich Marks, Dieter Lindner, Michael Gschwendt |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
Blotting
Western Down-Regulation Biology Biochemistry Mice Alkaloids medicine Animals Staurosporine Phosphorylation MARCKS Myristoylated Alanine-Rich C Kinase Substrate Protein kinase A Molecular Biology Peptide sequence Protein Kinase C Protein kinase C Antiserum Oligopeptide Intracellular Signaling Peptides and Proteins Membrane Proteins Proteins 3T3 Cells Cell Biology Molecular biology Tetradecanoylphorbol Acetate Electrophoresis Polyacrylamide Gel medicine.drug |
| Zdroj: | Journal of Biological Chemistry. 267:24-26 |
| ISSN: | 0021-9258 |
| DOI: | 10.1016/s0021-9258(18)48450-5 |
| Popis: | A polyclonal antiserum raised against an oligopeptide with an amino acid sequence corresponding to a sequence of the myristoylated alanine-rich C-kinase substrate (MARCKS) from mouse macrophages and rat brain recognizes the 80-kDa C-kinase substrate from Swiss 3T3 fibroblasts. Using this antiserum for quantitative determination of the 80-kDa MARCKS-related protein, we found that the phorbol ester 12-O-tetradecanoylphorbol-13-acetate (TPA) induces a rapid down-regulation of this protein in the fibroblasts. In accordance with earlier reports, TPA causes phosphorylation of the 80-kDa protein which can be inhibited by staurosporine. Staurosporine also suppresses the TPA-induced down-regulation, possibly indicating that the down-regulation of the MARCKS-related protein is dependent on its phosphorylation by protein kinase C. |
| Databáze: | OpenAIRE |
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