Stimulation of Membrane-Bound Guanylate Cyclase Activity by 17-β Estradiol

1998 ◽  
Vol 252 (3) ◽  
pp. 639-642 ◽  
Author(s):  
Zi-Jiang Chen ◽  
Linda Yu ◽  
Chung-Ho Chang
Keyword(s):  
Guanylate Cyclase ◽  
Cyclase Activity ◽  
Guanylate Cyclase Activity ◽  
Membrane Bound ◽  
Stimulation Of

scholarly journals Methylprednisolone stimulation of guanylate cyclase activity in rat ileal mucosa

1978 ◽  
Vol 74 (5) ◽  
pp. 1062 ◽  
Author(s):  
W.G. Marnane ◽  
A.N. Charney ◽  
E.C. Boedeker ◽  
M. Donowitz
Keyword(s):  
Guanylate Cyclase ◽  
Cyclase Activity ◽  
Ileal Mucosa ◽  
Guanylate Cyclase Activity ◽  
Stimulation Of

Human and rat growth hormones enhance guanylate cyclase activity

1981 ◽  
Vol 240 (2) ◽  
pp. E79-E82
Author(s):  
D. L. Vesely
Keyword(s):  
Growth Hormone ◽  
Guanylate Cyclase ◽  
Soluble Guanylate Cyclase ◽  
Human Growth ◽  
Growth Hormones ◽  
Cyclase Activity ◽  
Kidney Cortex ◽  
Guanylate Cyclase Activity ◽  
Rat Growth ◽  
Stimulation Of

The objective of this investigation was to determine whether physiological levels of growth hormone have part of their mechanism of action through stimulation of guanylate cyclase (EC 4.6.1.2.). Rat and human growth hormones enhanced the activity of soluble guanylate cyclase two- to fourfold in rat gracilis anticus skeletal muscle, liver, lung, heart, pancreas, and kidney cortex at a concentration of 10 nM. Dose-response relationships revealed that more than half-maximal stimulation of guanylate cyclase activity was seen at a concentration as low as 10 nM and nonstimulation of guanylate cyclase activity was seen when the concentration was decreased to 1 nM. Maximal enhancement was seen at 100 nM of growth hormone, and there was no further enhancement when the concentration was increased to the micromolar or millimolar range. Thus, the data in this investigation indicate that at concentrations at which growth hormone is known to cause its growth-promoting effects, growth hormone does cause an enhancement of the activity of the guanylate cyclase-cyclic GMP system.

Forskolin perturbs cGMP as well as cAMP levels in human thyroid cells

1984 ◽  
Vol 107 (2) ◽  
pp. 225-229 ◽  
Author(s):  
Maria Luisa Brandi ◽  
Carlo M. Rotella ◽  
Andrea Lopponi ◽  
Leonard D. Kohn ◽  
Salvatore M. Aloj ◽  
...  
Keyword(s):  
Guanylate Cyclase ◽  
Cyclase Activity ◽  
Human Thyroid ◽  
Thyroid Cell ◽  
Camp Production ◽  
Thyroid Cells ◽  
Guanylate Cyclase Activity ◽  
Low Concentrations ◽  
Camp Levels ◽  
Stimulation Of

Abstract. Forskolin, at 10−11 m, stimulates guanylate cyclase activity in primary human thyroid cell cultures, but does not modify cAMP accumulation. At a 10-fold higher concentration it still stimulates guanylate cyclase activity and becomes an inhibitor of cAMP production. Above 10−9 m, forskolin stimulation of cGMP decreases, while it also becomes a stimulator of cAMP production. There is an additive effect of TSH and forskolin on cAMP production at concentrations of the diterpene which are stimulatory. Concentrations of forskolin which are inhibitory for cAMP, but stimulatory for cGMP, are inhibitory for TSH stimulation of cAMP. The addition of 8-bromo-cGMP duplicates the forskolin effect at low concentrations.

scholarly journals Guanylate cyclase activity and cyclic nucleotide concentrations during liver regeneration after experimental injury

1977 ◽  
Vol 164 (1) ◽  
pp. 33-39 ◽  
Author(s):  
Christo Goridis ◽  
Jean Zwiller ◽  
Werner Reutter
Keyword(s):  
Dna Synthesis ◽  
Guanylate Cyclase ◽  
Cyclic Gmp ◽  
Cyclic Nucleotide ◽  
Cyclase Activity ◽  
Tissue Concentrations ◽  
Guanylate Cyclase Activity ◽  
Time Period ◽  
Membrane Bound ◽  
Experimental Injury

Cyclic nucleotide concentrations and guanylate cyclase activity were measured in regenerating rat liver. Previous work has shown that in livers of partially hepatectomized rats the activity of a membrane-bound guanylate cyclase increases considerably during the early replicative phase [Kimura & Murad (1975) Proc. Natl. Acad. Sci. U.S.A.72, 1965–1969; Goridis & Reutter (1975) Nature (London) 257, 698–700]. Over the same time period after partial hepatectomy, increased tissue concentrations of cyclic GMP were found when the rats were killed under pentobarbital anaesthesia, but not when anaesthesia was omitted. The results obtained on hepatectomized livers were compared with the changes in guanylate cyclase activity and cyclic nucleotide concentrations during the response to galactosamine treatment. Here, a peak of guanylate cyclase activity and of cyclic GMP concentrations occurred at 8h, that is before the beginning of the proliferative response. Both parameters were normal at the time of increased DNA synthesis. There does not, therefore, seem to be a consistent correlation between changes in guanylate cyclase activity or concentrations of cyclic GMP and an increase in liver DNA synthesis. A modest rise in cyclic AMP concentrations was found, however, in livers of galactosamine-treated rats, which was coincident with the time of DNA synthesis.

scholarly journals Guanylate cyclase in Dictyostelium discoideum with the topology of mammalian adenylate cyclase

2001 ◽  
Vol 354 (3) ◽  
pp. 697-706 ◽  
Author(s):  
Jeroen ROELOFS ◽  
Helena SNIPPE ◽  
Reinhard G. KLEINEIDAM ◽  
Peter J.M. Van HAASTERT
Keyword(s):  
Adenylate Cyclase ◽  
G Proteins ◽  
Guanylate Cyclase ◽  
Cyclase Activity ◽  
Knock Out ◽  
Guanylate Cyclase Activity ◽  
Cyclase Domain ◽  
Cellular Slime ◽  
Membrane Bound ◽  
Camp Receptor

The core of adenylate and guanylate cyclases is formed by an intramolecular or intermolecular dimer of two cyclase domains arranged in an antiparallel fashion. Metazoan membrane-bound adenylate cyclases are composed of 12 transmembrane spanning regions, and two cyclase domains which function as a heterodimer and are activated by G-proteins. In contrast, membrane-bound guanylate cyclases have only one transmembrane spanning region and one cyclase domain, and are activated by extracellular ligands to form a homodimer. In the cellular slime mould, Dictyosteliumdiscoideum, membrane-bound guanylate cyclase activity is induced after cAMP stimulation; a G-protein-coupled cAMP receptor and G-proteins are essential for this activation. We have cloned a Dictyostelium gene, DdGCA, encoding a protein with 12 transmembrane spanning regions and two cyclase domains. Sequence alignment demonstrates that the two cyclase domains are transposed, relative to these domains in adenylate cyclases. DdGCA expressed in Dictyostelium exhibits high guanylate cyclase activity and no detectable adenylate cyclase activity. Deletion of the gene indicates that DdGCA is not essential for chemotaxis or osmo-regulation. The knock-out strain still exhibits substantial guanylate cyclase activity, demonstrating that Dictyostelium contains at least one other guanylate cyclase.

Cation-dependent vitamin D activation of human renal cortical guanylate cyclase

1984 ◽  
Vol 246 (1) ◽  
pp. E115-E120 ◽  
Author(s):  
D. L. Vesely ◽  
D. Juan
Keyword(s):  
Vitamin D ◽  
Guanylate Cyclase ◽  
Cellular Level ◽  
Cyclase Activity ◽  
Rat Tissues ◽  
Response Curves ◽  
Guanylate Cyclase Activity ◽  
Manganese Ion ◽  
Maximal Stimulation ◽  
Stimulation Of

The objective of this investigation was to determine whether physiological levels of vitamin D and its metabolites have part of their mechanisms of action through stimulation of guanylate cyclase (EC 4.6.1.2). These sterols enhanced both soluble and particulate guanylate cyclase activities as well as cGMP levels two- to threefold in human and rat tissues. At a concentration of 1 nM, 1,25(OH)2D3 greater than 25(OH)D3 greater than vitamin D3 greater than 24,25(OH)2D3 = 25,26(OH)2D3 = vitamin D2. Dose-response curves revealed that maximal stimulation of guanylate cyclase by these sterols was at 1 nM and that there was no augmented guanylate cyclase activity at 0.01 nM. The precursors of vitamin D, cholesterol and 7-dehydrocholesterol, had no effect on guanylate cyclase activity. The activation of guanylate cyclase activity by the vitamin D sterols required the presence of manganese ion. Calcium was not as efficient as manganese in optimizing basal or hormone-stimulated guanylate cyclase activity. Vitamin D and its metabolites failed to stimulate adenylate cyclase (EC 4.6.1.1) activity. The data in this investigation suggest that guanylate cyclase may play a role in the mechanism of action of vitamin D at the cellular level.

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