PMID- 833541 OWN - NLM STAT- MEDLINE DCOM- 19770331 LR - 20190709 IS - 0022-0795 (Print) IS - 0022-0795 (Linking) VI - 72 IP - 1 DP - 1977 Jan TI - States of activation of chick kidney adenylate cyclase induced by parathyroid hormone and guanyl nucleotides. PG - 69-79 AB - Several aspects of the activation of adenylate cyclase by guanosine 5'-triphosphate (GTP), 5'-guanylylimidodiphosphate (Gpp(NH)p) and bovine parathyroid hormone (bPTH) have been studied in chick kidney plasma membrane preparations. GTP (10(-4) mol/l), Gpp(NH)p (10(-4) mol/l) and bPTH (10 i.u./ml) activated adenylate cyclase without any significant time lag. However a 2 min delay was observed before the activity of the enzyme increased after the addition of bPTH (-6 leads to +34) to incubations. The early (0-3 min) effects of GTP and Gpp(NH)p upon chick kidney adenylate cyclase activity were antagonized by the addition of the alternative guanyl nucleotide. After 5 min of incubation with kidney plasma membranes, Gpp(NH)p induced a stable state of activation of adenylate cyclase which was not reversible by subsequent addition of GTP. GTP did not induce an irreversible state of enzyme activation. In pre-incubation studies, GTP did not produce a persistent enzyme activation and did not modify the effect of Gpp(NH)p added subsequently at the incubation stage. Gpp(NH)p produced a stable state of activation of adenylate cyclase which was not inhibited by addition of GTP at the incubation stage. Bovine PTH (2-34) inhibited the effect of bPTH upon adenylate cyclase activity when the native hormone (10 i.u./ml) had been incubated with plasma membranes for up to 8 min before addition of the analogue (5 mug/ml). Incubation of plasma membranes with bPTH (2-34) for as little as 10 s prevented activation of adenylate cyclase by subsequent addition of bPTH. This pattern was confirmed in pre-incubation studies. After pre-incubation of kidney membranes with bPTH and bPTH (2-34), followed by washing, an acid extract of the membranes contained immunoreactive bPTH. Gpp(NH)p produced a greater increase in adenylate cyclase activity in membranes pre-incubated with bPTH or bPTH (2-34) than in membranes pre-incubated with buffer alone, suggesting that the hormone and analogue facilitated the interaction of Gpp(NH)p with adenylate cyclase. FAU - Michalangeli, V P AU - Michalangeli VP FAU - Hunt, N H AU - Hunt NH FAU - Martin, T J AU - Martin TJ LA - eng PT - Journal Article PL - England TA - J Endocrinol JT - The Journal of endocrinology JID - 0375363 RN - 0 (Guanine Nucleotides) RN - 0 (Hormones) RN - 0 (Parathyroid Hormone) RN - 86-01-1 (Guanosine Triphosphate) RN - EC 4.6.1.1 (Adenylyl Cyclases) SB - IM MH - Adenylyl Cyclases/*biosynthesis MH - Animals MH - Cell Membrane/drug effects/enzymology MH - Chick Embryo MH - Enzyme Induction MH - Guanine Nucleotides/*pharmacology MH - Guanosine Triphosphate/*pharmacology MH - Hormones/pharmacology MH - Kidney/drug effects/*enzymology MH - Parathyroid Hormone/*pharmacology EDAT- 1977/01/01 00:00 MHDA- 1977/01/01 00:01 CRDT- 1977/01/01 00:00 PHST- 1977/01/01 00:00 [pubmed] PHST- 1977/01/01 00:01 [medline] PHST- 1977/01/01 00:00 [entrez] AID - 10.1677/joe.0.0720069 [doi] PST - ppublish SO - J Endocrinol. 1977 Jan;72(1):69-79. doi: 10.1677/joe.0.0720069.