TY - JOUR
T1 - Persistent stimulation of adenylate cyclase and urea transport by an AVP photolabel
AU - Eggena, P.
AU - Ma, C. L.
AU - Fahrenholz, F.
AU - Schwartz, I. L.
PY - 1985
Y1 - 1985
N2 - The effects of a photoaffinity label for arginine vasopressin receptors, [Phe2,Phe(p-N3)3]AVP (N3-AVP), on urea permeability and adenylate cyclase activity have been investigated in the toad urinary bladder. This compound, when activated by ultraviolet light, induced a maximal and persistent increase in the urea permeability of the intact bladder and a persistent increase in the adenylate cyclase activity of toad bladder epithelial cell homogenates. Covalent attachment of the analogue to target tissue during photolysis was equivalent at 4 and 20°C. Bladders exposed to N3-AVP in the presence of AVP during photolysis were substantially less permeable to urea than controls that had been exposed to N3-AVP alone. These findings constitute further evidence in support of our previous suggestion that N3-AVP binds covalently to AVP receptors and, in addition, demonstrates that N3-AVP evokes a persistent increase in adenylate cyclase activity which, in turn, triggers a persistent increase in bladder permeability to urea.
AB - The effects of a photoaffinity label for arginine vasopressin receptors, [Phe2,Phe(p-N3)3]AVP (N3-AVP), on urea permeability and adenylate cyclase activity have been investigated in the toad urinary bladder. This compound, when activated by ultraviolet light, induced a maximal and persistent increase in the urea permeability of the intact bladder and a persistent increase in the adenylate cyclase activity of toad bladder epithelial cell homogenates. Covalent attachment of the analogue to target tissue during photolysis was equivalent at 4 and 20°C. Bladders exposed to N3-AVP in the presence of AVP during photolysis were substantially less permeable to urea than controls that had been exposed to N3-AVP alone. These findings constitute further evidence in support of our previous suggestion that N3-AVP binds covalently to AVP receptors and, in addition, demonstrates that N3-AVP evokes a persistent increase in adenylate cyclase activity which, in turn, triggers a persistent increase in bladder permeability to urea.
UR - http://www.scopus.com/inward/record.url?scp=0022102194&partnerID=8YFLogxK
U2 - 10.1152/ajpcell.1985.249.1.c84
DO - 10.1152/ajpcell.1985.249.1.c84
M3 - Article
C2 - 3160246
AN - SCOPUS:0022102194
SN - 0363-6143
VL - 18
SP - C84-C88
JO - American Journal of Physiology - Cell Physiology
JF - American Journal of Physiology - Cell Physiology
IS - 1
ER -