TY - JOUR
T1 - Vasopressin-induced activation of protein kinase C in renal epithelial cells
AU - Ali, Nawab
AU - Kantachuvesiri, Surasak
AU - Smallwood, Joan I.
AU - Macala, Lawrence J.
AU - Isales, Carlos
AU - Ji, Jing
AU - Reilly, Robert
AU - Hayslett, John P.
N1 - Funding Information:
This study was supported by the National Institutes of Health Grant DK19813, the Juvenile Diabetes Foundation, a Merit Award from the Veterans Administration and Ramathibodi Hospital, Mahidol University, Bangkok, Thailand (Dr. Kantachuvesiri).
PY - 1998/3/27
Y1 - 1998/3/27
N2 - 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 Ca2+-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 Ca2+-dependent PKC is involved in the action of AVP, and that of other agonists, which stimulate sodium transport.
AB - 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 Ca2+-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 Ca2+-dependent PKC is involved in the action of AVP, and that of other agonists, which stimulate sodium transport.
KW - A6 cell
KW - MARCKS
KW - Protein kinase C
KW - Sodium transport
KW - Vasopressin
UR - http://www.scopus.com/inward/record.url?scp=0032571549&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0032571549&partnerID=8YFLogxK
U2 - 10.1016/S0167-4889(98)00006-8
DO - 10.1016/S0167-4889(98)00006-8
M3 - Article
C2 - 9561804
AN - SCOPUS:0032571549
SN - 0167-4889
VL - 1402
SP - 188
EP - 196
JO - Biochimica et Biophysica Acta - Molecular Cell Research
JF - Biochimica et Biophysica Acta - Molecular Cell Research
IS - 2
ER -