Antagonistic Effects of 25(OH)Vitamin D3 and Peptide Hormones on the Activation of Adenylate Cyclase/Cyclic AMP System in Renal Tissue in Vitro

1980 ◽  
pp. 625-633 ◽  
Author(s):  
Hanna Wald ◽  
Mordecai M. Popovtzer
Keyword(s):  
Cyclic Amp ◽  
Adenylate Cyclase ◽  
Vitamin D3 ◽  
Peptide Hormones ◽  
Renal Tissue ◽  
Antagonistic Effects ◽  
Amp System

Cytochemical Evidence for Presynatic β-Adrenergic Regulation of Secretion in the Developing Rat Submandibular Gland

1977 ◽  
Vol 35 ◽  
pp. 430-431
Author(s):  
L.S. Cutler
Keyword(s):  
Cyclic Amp ◽  
Adenylate Cyclase ◽  
Submandibular Gland ◽  
Neonatal Rat ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Parotid Glands ◽  
Adrenergic Agonist ◽  
Rat Submandibular Gland

Many studies previously have shown that the B-adrenergic agonist isoproterenol and the a-adrenergic agonist norepinephrine will stimulate secretion by the adult rat submandibular (SMG) and parotid glands. Recent data from several laboratories indicates that adrenergic agonists bind to specific receptors on the secretory cell surface and stimulate membrane associated adenylate cyclase activity which generates cyclic AMP. The production of cyclic AMP apparently initiates a cascade of events which culminates in exocytosis. During recent studies in our laboratory it was observed that the adenylate cyclase activity in plasma membrane fractions derived from the prenatal and early neonatal rat submandibular gland was retractile to stimulation by isoproterenol but was stimulated by norepinephrine. In addition, in vitro secretion studies indicated that these prenatal and neonatal glands would not secrete peroxidase in response to isoproterenol but would secrete in response to norepinephrine. In contrast to these in vitro observations, it has been shown that the injection of isoproterenol into the living newborn rat results in secretion of peroxidase by the SMG (1).

scholarly journals Interactions between adenylate cyclase and the yeast GTPase-activating protein IRA1.

1991 ◽  
Vol 11 (9) ◽  
pp. 4591-4598 ◽  
Author(s):  
M R Mitts ◽  
J Bradshaw-Rouse ◽  
W Heideman
Keyword(s):  
Cyclic Amp ◽  
Adenylate Cyclase ◽  
Adenylate Cyclase System ◽  
Gtpase Activating Protein ◽  
Yeast Saccharomyces Cerevisiae ◽  
Strong Candidate ◽  
Sepharose 4B ◽  
Stimulation Of ◽  
Cyclic Amp Synthesis

The adenylate cyclase system of the yeast Saccharomyces cerevisiae contains many proteins, including the CYR1 polypeptide, which is responsible for catalyzing the formation of cyclic AMP from ATP, RAS1 and RAS2 polypeptides, which mediate stimulation of cyclic AMP synthesis by guanine nucleotides, and the yeast GTPase-activating protein analog IRA1. We have previously reported that adenylate cyclase is only peripherally bound to the yeast membrane. We have concluded that IRA1 is a strong candidate for a protein involved in anchoring adenylate cyclase to the membrane. We base this conclusion on the following criteria: (i) a disruption of the IRA1 gene produced a mutant with very low membrane-associated levels of adenylate cyclase activity, (ii) membranes made from these mutants were incapable of binding adenylate cyclase in vitro, (iii) IRA1 antibodies inhibit binding of adenylate cyclase to the membrane, and (iv) IRA1 and adenylate cyclase comigrate on Sepharose 4B.

Cannabinoid effects on adenylate cyclase and phosphodiesterase activities of mouse brain

1977 ◽  
Vol 55 (4) ◽  
pp. 934-942 ◽  
Author(s):  
Thomas W. Dolby ◽  
Lewis J. Kleinsmith
Keyword(s):  
Cyclic Amp ◽  
Adenylate Cyclase ◽  
Mouse Brain ◽  
Biogenic Amine ◽  
Specific Activity ◽  
Intraperitoneal Administration ◽  
The Brain

The experiments presented in this paper examine the mechanisms underlying the ability of cannabinoids to alter the in vivo levels of cyclic adenosine 3′,5′-monophosphate (cyclic AMP) in mouse brain. It was found that changes in cyclic AMP levels are a composite result of direct actions of cannabinoids on adenylate cyclase (EC 4.6.1.1) activity and indirect actions involving the potentiation or inhibition of biogenic amine induced activity of adenylate cyclase. Furthermore, the long-term intraperitoneal administration of 1-(−)-Δ-tetrahydrocannabinol to mice produced a form of phosphodiesterase (EC 3.1.4.17) in the brain whose activity is not stimulated by Ca2+, although its basal specific activity is similar to that of control animals. In vitro, the presence of the cannabinoids caused no significant changes in activity of brain PDE at the concentrations tested. Some correlations are presented which imply that many of the observed behavioral and physiological actions of the cannabinoids in mammalian organisms may be mediated via cyclic AMP mechanisms.

Evidence for interference of 25(OH)vitamin D3 with phosphaturic action of glucagon

1981 ◽  
Vol 240 (4) ◽  
pp. F269-F275 ◽  
Author(s):  
M. M. Popovtzer ◽  
H. Wald
Keyword(s):  
Adenylate Cyclase ◽  
Vitamin D3 ◽  
Fractional Excretion ◽  
Camp Level ◽  
Kidney Slices ◽  
Group 3 ◽  
Camp System ◽  
Group 2 ◽  
Group 1

The effect of 25(OH)vitamin D3 [25(OH)D3] on the phosphaturic action of glucagon was studied using clearance techniques in the following groups of rats: group 1, parathyroidectomized (PTX) glucagon-infused rats receiving intravenous 25(OH)D3; group 2, PTX 25(OH)D3-pretreated rats receiving intravenous glucagon; and group 3, the thyroparathyroidectomized glucagon-infused rats receiving intravenous 25(OH)D3. The effect of 25(OH)D3 on glucagon-induced increase of cAMP in kidney slices and glucagon-activated adenylate cyclase (AC) in kidney membrane fractions was studied in vitro. In group 1, 25(OH)D3 suppressed the glucagon-induced phosphaturia by reducing fractional excretion of phosphorus (CP/CIn) from 0.175 +/- 0.02 (mean +/- SE) to 0.112 +/- 0.12 (P less than 0.05); this was associated with a reduction of urinary cAMP from 1,830 +/- 230 to 660 +/- 120 pmol/min (P less than 0.01). In group 2, pretreatment with 25(OH)D3 reduced CP/CIn from 0.221 +/- 0.025 to 0.108 +/- 0.012 (P less than 0.005). In group 3, 25(OH)D3 reduced CP/CIn from 0.165 +/- 0.012 to 0.075 +/- 0.011 (P less than 0.005). In vitro, 25(OH)D3 blunted the glucagon-induced activation of the AC/cAMP system by reducing AC from 570 +/- 30 to 325 +/- 28 pmol cAMP.mg protein-1.h-1 (P less than 0.01) and the cAMP level from 11.2 +/- 0.9 to 8.5 +/- 0.7 pmol cAMP/g wet tissue (P less than 0.05). These results show that 25(OH)D3 blunts the phosphaturic action of glucagon and suggest that this response may be mediated through suppression of the AC/cAMP system.

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