Vasopressin-induced activation of protein kinase C in renal epithelial cells
| Autor: | Surasak Kantachuvesiri, Robert F. Reilly, Lawrence J. Macala, John P. Hayslett, Carlos M. Isales, Nawab Ali, Jing Ji, Joan I. Smallwood |
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| Rok vydání: | 1998 |
| Předmět: |
MARCKS
Vasopressin Adenosine Vasopressins Biology Kidney Renal Agents Sodium transport Diglycerides Xenopus laevis chemistry.chemical_compound Animals Insulin Phosphorylation Myristoylated Alanine-Rich C Kinase Substrate Molecular Biology Cells Cultured Protein Kinase C Protein kinase C Diacylglycerol kinase Intracellular Signaling Peptides and Proteins Membrane Proteins Proteins Epithelial Cells Inositol trisphosphate Cell Biology Molecular biology Arginine Vasopressin Enzyme Activation Isoenzymes Cytosol chemistry A6 cell Signal transduction |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1402(2):188-196 |
| ISSN: | 0167-4889 |
| DOI: | 10.1016/s0167-4889(98)00006-8 |
| Popis: | Recent studies indicate that the actions of arginine vasopressin (AVP) and other agonists that stimulate electrogenic sodium transport in renal epithelial A6 cells are linked to a Ca 2+ -mobilizing signal transduction mechanism that involves generation of inositol trisphosphate. Since diacylglycerol is the other product in this pathway, studies were performed to determine the possible role of PKC in the stimulation of sodium transport. AVP induced a biphasic increase in diacylglycerol generation, characterized by an initial rapid rise and then a sustained elevation, and PKC activation, reflected by phosphorylation of a specific 80 kDa myristoylated alanine-rich PKC substrate (MARCKS). To determine the PKC isoform(s) involved in this process, immunoblot analysis was performed using antisera that recognize both classical PKC isoforms, XPKC-I and XPCK-II, cloned from Xenopus oocytes. The transcripts of both isoforms were expressed in the A6 cell. Since protein recognized by antisera was translocated from cytosol to the particulate fraction after exposure to AVP, one or both isoforms were activated in the A6 cell. Further studies showed that cyclohexyladenosine and insulin, additional agonists of sodium transport in A6 cells, also stimulated phosphorylation of MARCKS. These results argue that Ca 2+ -dependent PKC is involved in the action of AVP, and that of other agonists, which stimulate sodium transport. |
| Databáze: | OpenAIRE |
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