Cyclic Monophosphate Formation Research Articles

Effect of Antidiuretic Hormone Upon Urinary Concentrating Ability and Medullary c-AMP Formation in Neonatal Piglets

Summary: In 16 anesthetized piglets, the effects of 1-deamino-8-D-argininc-vasoprcssin (DDAVP) upon urinary flow rate, relative urinary osmolarity (U/Posmol), fractional water excretion (U/PIn), fractional urta excretion (U/Purea/U/PIn), renal adenosine 3′,5′-cyclic monophosphate (c-AMP) formation rate, and medullary c-AMP content were studied during the first 6 days of life. Glomerular filtration rate (GFR) was 0.19 ± 0.09 ml/min/g kidney wt (means ± SD) on day 1 and increased to 0.51 ± 0.11 ml/min/g kidney wt on day 6. It was not affected by the application of 20 μg DDAVP/ kg body wt. On day 1, U/Posmol (1.81 ± 0.29), urinary flow rate (5.36 ± 1.49 μl/min/g kidney wt), U/PIn (31.67 ± 6.10) and U/ Purea/U/PIn (0.84 ± 0.12) were not affected by DDAVP application. From day 2 onward, the reponse of these variables to application of DDAVP increased progressively. On day 6, the following responses were observed: Urinary flow rate decreased from 13.85 ± 7.02 μl/min/g kidney wt before DDAVP to 5.07 ± 2.19 μl/min/ g kidney wt after DDAVP. U/Posmol raised from 1.24 ± 0.27 before DDAVP to 2.64 ± 0.17 after DDAVP. U/PIn increased from 36.85 ± 13.11 before DDAVP to 109.39 ± 22.00 after DDAVP. U/Purea/U/PIn decreased from 0.75 ± 0.05 before DDAVP to 0.55 ± 0.04 after DDAVP. These data indicate that the small solute permeability of the medullary collecting ducts becomes increasingly sensitive to antidiuretic hormone (ADII) during this period. The increase in responsiveness of the urinary concentrating system with age was paralleled by the effect of DDAVP on renal c-AMP formation rate. In the diuretic control state, no correlation between renal c-AMP formation rate and the number of days was observed. However, after the application of DDAVP, the nephrogenic fraction of renal c-AMP excretion rate increased from 10.58 ± 4.49 pmole/min/g kidney wt on day 1 to 21.61 ± 8.10 pmole/ min/g kidney wt on day 6. Similar results were observed with the medullary c-AMP content. In diuretic control animals which had not received DDAVP, the medullary c-AMP content ranged between 636 ± 257 pmole/g wet wt on day 1 and 622 ± 75 pmole/g wet wt on day 6. However, in animals which had been infused with DDAVP, medullary c-AMP content increased from 684 ± 274 pmole/g wet wt on day 1 to 1536 ± 316 pmole/g wet wt on day 6. Speculation: The unresponsiveness of the medullary adenylatecyclase to ADII in the newborn kidney might restrict, in addition to other parameters, the renal concentrating ability during the neonatal period.

Inhibition by calcium ions of adenosine cyclic monophosphate formation in sealed pigeon erythrocyte ‘ghosts’. A study using the photoprotein obelin

1. Sealed pigeon erythrocyte 'ghosts' were prepared containing ATP and the Ca2+-activated photoprotein obelin to investigate the relationship cyclic AMP formation and internal free Ca2+. 2. The 'ghosts' were characterized by (a) morphology (optical and electron microscopy), (b) composition (haemoglobin, K+, Na+, Mg2+, ATP, obelin), (c) permeability to Ca2+, assessed by obelin luminescence and (d) hormone sensitivity (the effect of beta-adrenergic agonists and antagonists on cyclic AMP formation). 3. The effect of osmolarity at haemolysis and ATP at resealing on these parameters was investigated. 4. Sealed 'ghosts', containing approx. 2% of original haemoglobin, 150mM-K+, 0.5MM-ATP, 10(3)--10(4) obelin luminescence counts/10(6) 'ghosts', which were relatively impermeable to Ca2+ and in which cyclic AMP formation was stimulated by beta-adrenergic agonists over a concentration range similar to that for intact cells, could be prepared after haemolysis in 6mM-NaCl3mM-MgCl2/50mM-Tes, pH7, and resealing for 30min at 37 degrees C in the presence of ATP and 150mM-KCl. 5. The initial rate of adrenaline-stimulated cyclic AMP formation in these 'ghosts' was 30--50% of that in intact cells and was inhibited by the addition of extracellular Ca2+. Addition of Ca2+ to the 'ghosts' resulted in a stimulation of obelin luminescence, indicating an increase in internal free Ca2+ under these conditions. 6. The ionophore A23187 increased the rate of obelin luminescence in the 'ghosts' and also inhibited the adrenaline-stimulated increase in cyclic AMP. 7. The effect of ionophore A23187 on obelin luminescence and on cyclic AMP formation in the 'ghosts' was markedly decreased by sealing EGTA inside the 'ghosts'. 8. It was concluded that cyclic AMP formation inside sealed pigeon erythrocyte 'ghosts' could be inhibited by more than 50% by free Ca2+ concentrations in the range 1--10 micrometer.

Stimulation by prostaglandin E 1 of adenosine 3′:5′-cyclic monophosphate formation in neuroblastoma cells in the presence of phosphodiesterase inhibitors

FEBS LettersVolume 34, Issue 1 p. 85-89 Full-length articleFree Access Stimulation by prostaglandin E1 of adenosine 3′:5′-cyclic monophosphate formation in neuroblastoma cells in the presence of phosphodiesterase inhibitors Bernd Hamprecht, Bernd Hamprecht Max-Planck-Institut für Biochemie, 8033 Martinsried bei München, Germany Institut für Toxikologie der Universität, 7400 Tübingen, GermanySearch for more papers by this author Bernd Hamprecht, Bernd Hamprecht Max-Planck-Institut für Biochemie, 8033 Martinsried bei München, Germany Institut für Toxikologie der Universität, 7400 Tübingen, GermanySearch for more papers by this author First published: August 01, 1973 https://doi.org/10.1016/0014-5793(73)80709-4Citations: 42AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL References 1 G. Augusti-Tocco, G. Sato, Proc. Natl. Acad. Sci. U.S., 64, (1969), 311– 2 D. Schubert, S. Humphreys, C. Baroni, M. Cohn, Proc. Natl. Acad. Sci. U.S., 64, (1969), 316– 3 N.W. Seeds, A.G. Gilman, T. Amano, M. Nirenberg, Proc. Natl. Acad. Sci. U.S., 66, (1970), 160– 4 T. Amano, E. Richelson, M. Nirenberg, Proc. Natl. Acad. Sci. U.S., 69, (1972), 258– 5 R.N. Rosenberg, L. Vandeventer, Francesco L. de, M.E. Friedkin, Proc. Natl. Acad. Sci. U.S., 68, (1971), 1435– 6 A.J. Harris, M.J. Dennis, Science, 167, (1970), 1253– 7 P. Nelson, W. Ruffner, M. Nirenberg, Proc. Natl. Acad. Sci. U.S., 64, (1969), 1004– 8 P.G. Nelson, J.H. Peacock, T. Amano, J. Minna, J. Cell. Physiol., 77, (1971), 337– 9 P.G. Nelson, J.H. Peacock, T. Amano, J. Cell. Physiol., 77, (1971), 1353– 10 A.G. Gilman, M. Nirenberg, Nature, 234, (1971), 356– 11 U. Rufeger, B. Tellheim, M. Frimmer, Naunyn-Schmiedebergs Arch. Pharmak., 270, (1971), 428– 12 J. Schultz, B. Hamprecht, J.W. Daly, Proc. Natl. Acad. Sci. U.S., 69, (1972), 1266– 13 J.A. Beavo, N.L. Rogers, O.B. Crofford, J.G. Hardman, E.W. Sutherland, E.V. Newman, Mol. Pharmacol., 6, (1970), 597– 14 Amano, T., Hamprecht, B. and Kemper, W., submitted for publication. 15 J. Minna, D. Glazer, M. Nirenberg, Nature New Biol., 235, (1972), 225– 16 A. Blume, F. Gilbert, S. Wilson, J. Farber, R. Rosenberg, M. Nirenberg, Proc. Natl. Acad. Sci. U.S., 67, (1970), 786– 17 J. Schultz, B. Hamprecht, Naunyn-Schmiedebergs Arch. Pharmak., (1973), in press 18 A. Gilman, Proc. Natl. Acad. Sci. U.S., 67, (1970), 305– 19 J. Schultz, J.W. Daly, J. Biol. Chem., 248, (1973), 843– 20 G. Beisenherz, H.J. Bolte, Th. Bücher, R. Czok, K.H. Garbade, E. Meyer-Arendt, G. Pfleiderer, Z. Naturforsch., 8b, (1953), 555– 21 E.E. Jacobs, M. Jacobs, D.R. Samadi, L.B. Bradley, J. Biol. Chem., 223, (1956), 147– 22 K.N. Prasad, A.W. Hsie, Nature New Biol., 233, (1971), 141– 23 K.N. Prasad, Nature New Biol., 236, (1972), 49– 24 K.N. Prasad, J.R. Sheppard, Exptl. Cell Res., 73, (1972), 436– 25 E. Monn, R.O. Christiansen, Science, 173, (1971), 540– 26 P. Uzonov, H.M. Shein, B. Weiss, Fifth Intern. Congress on Pharmacology, San Francisco, (1972), Abstr. 1431 Citing Literature Volume34, Issue1August 01, 1973Pages 85-89 ReferencesRelatedInformation

Stimulation by dopamine of adenylate cyclase in retinal homogenates and of adenosine-3':5'-cyclic monophosphate formation in intact retina.

A catecholamine-sensitive adenylate cyclase system is present in homogenates of both calf and rat retinas. Dopamine is a more potent activator of the bovine enzyme than is norepinephrine or epinephrine. Cyclic AMP concentrations in intact bovine retina are increased by dopamine, as well as by other catecholamines, and by depolarizing agents. Studies with adrenergic blocking agents suggest that the stimulation of retinal adenylate cyclase by catecholamines cannot be clearly defined in terms of the characteristics of alpha or beta adrenergic receptors. Bovine retina also contains a protein kinase that is stimulated 20-fold by cyclic AMP. It is proposed that dopamine is the major activator of a retinal adenylate cyclase, and that this activation is related to its role as a neurotransmitter.

Adenyl cyclase activity in the rabbit ovary.

An assay for adenyl cyclase activity in homogenates of ovarian interstitial tissue from pseudopregnant rabbits is described and evaluated. The assay is based on the estimation of [14C] adenosine-3′,5′-(cyclic) monophosphate ([UC] 3′,5′-AMP) formation from 8-[14C] ATP. 3′,5′-AMP phosphodiesterase activity is estimated simultaneously by the loss of [3H] 3′,5′-AMP from the incubation mixture. Ovine LH and HCG added in vitro stimulated the adenyl cyclase activity, whereas ovine FSH and porcine ACTH were ineffective. LH had no effect on phosphodiesterase activity. (Endocrinology 84: 989, 1969)