A novel succinyl dipeptide stimulates directed cell migration by modulating protein kinase C activity
| Autor: | Gabriel F. Eilon, Wayne J. Thompson, Timothy C. Chambers, Mary Ann Gallo, Renato N. Mascardo |
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| Rok vydání: | 1990 |
| Předmět: |
Physiology
Molecular Sequence Data Clinical Biochemistry Biology Cell Line chemistry.chemical_compound medicine Animals Amino Acid Sequence Phosphorylation Protein Kinase C Protein kinase C Chemotactic Factors Chemotaxis fungi Succinates Cell migration Dipeptides Cell Biology Phosphoproteins Cell biology Enzyme Activation N-Formylmethionine Leucyl-Phenylalanine Endothelial stem cell Cytosol Biochemistry Mechanism of action chemistry Cell culture Phorbol Tetradecanoylphorbol Acetate Cattle Endothelium Vascular medicine.symptom |
| Zdroj: | Journal of Cellular Physiology. 142:401-409 |
| ISSN: | 1097-4652 0021-9541 |
| DOI: | 10.1002/jcp.1041420225 |
| Popis: | In determining the mechanism of the chemokinetic action of the thiol protease inhibitor, E-64, in endothelial cell monolayers subjected to wounding, we synthesized succinyl-leucyl-agmatine (SLA), an analogue of E-64 that lacked the epoxy group and protease inhibitory effect. We observed that this analogue retained its chemokinetic effect on wounded endothelial cells. Its stimulatory action on en-dothelial cell polarization response to wounding was rapid and associated with directed cell migration. Furthermore, its effect on cellular polarization was blocked by protein kinase C (PKC) inhibitors and mimicked by pharmacologic agents that stimulated PKC activity. To determine if SLA's chemokinetic action was mediated by protein kinase C activation, we compared the effects of SLA and the tumor promoter phorbol myristate acetato (PMA) on the translocation of PKC activity in endothelial cells. We observed that both SLA and PMA induced the translocation of PKC activity from the cytosolic to the particulate fraction of the cells. We also observed that both SLA and PMA induced the phosphorylation of two proteins (Mr 23.4 and 36.5 kDa) in intact 32P-labeled cells. Thus, SLA stimulates the endothelial cell locomotor response to wounding by stimulating PKC activity. |
| Databáze: | OpenAIRE |
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