Modulation of Rat Guanylate Cyclase Activity in vitro by Chemical Carcinogens

Enzyme ◽  
1978 ◽  
Vol 23 (5) ◽  
pp. 356-360 ◽  
Author(s):  
David L. Vesely ◽  
Denis C. Lehotay ◽  
Gerald S. Levey
Keyword(s):  
Guanylate Cyclase ◽  
Cyclase Activity ◽  
Chemical Carcinogens ◽  
Guanylate Cyclase Activity

scholarly journals Identification of a novel Arabidopsis thaliana nitric oxide-binding molecule with guanylate cyclase activity in vitro

FEBS Letters ◽  
2011 ◽  
Vol 585 (17) ◽  
pp. 2693-2697 ◽  
Author(s):  
Takalani Mulaudzi ◽  
Ndiko Ludidi ◽  
Oziniel Ruzvidzo ◽  
Monique Morse ◽  
Nicolette Hendricks ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Arabidopsis Thaliana ◽  
Guanylate Cyclase ◽  
Cyclase Activity ◽  
Guanylate Cyclase Activity

Phosphorylation of the dimeric cytoplasmic domain of the phytosulfokine receptor, PSKR1

2016 ◽  
Vol 473 (19) ◽  
pp. 3081-3098 ◽  
Author(s):  
Victor Muleya ◽  
Claudius Marondedze ◽  
Janet I. Wheeler ◽  
Ludivine Thomas ◽  
Yee-Fong Mok ◽  
...  
Keyword(s):  
Guanylate Cyclase ◽  
Kinase Activity ◽  
Analytical Ultracentrifugation ◽  
Domain Architecture ◽  
Defense Responses ◽  
Cytoplasmic Domain ◽  
Size Exclusion ◽  
Cyclase Activity ◽  
Guanylate Cyclase Activity

Phytosulfokines (PSKs) are plant peptide hormones that co-regulate plant growth, differentiation and defense responses. PSKs signal through a plasma membrane localized leucine-rich repeat receptor-like kinase (phytosulfokine receptor 1, PSKR1) that also contains a functional cytosolic guanylate cyclase with its cyclase catalytic center embedded within the kinase domain. To functionally characterize this novel type of overlapping dual catalytic function, we investigated the phosphorylation of PSKR1 in vitro. Tandem mass spectrometry of the cytoplasmic domain of PSKR1 (PSKR1cd) revealed at least 11 phosphorylation sites (8 serines, 2 threonines and 1 tyrosine) within the PSKR1cd. Phosphomimetic mutations of three serine residues (Ser686, Ser696 and Ser698) in tandem at the juxta-membrane position resulted in enhanced kinase activity in the on-mutant that was suppressed in the off-mutant, but both mutations reduced guanylate cyclase activity. Both the on and off phosphomimetic mutations of the phosphotyrosine (Tyr888) residue in the activation loop suppressed kinase activity, while neither mutation affected guanylate cyclase activity. Size exclusion and analytical ultracentrifugation analysis of the PSKR1cd suggest that it is reversibly dimeric in solution, which was further confirmed by biflourescence complementation. Taken together, these data suggest that in this novel type of receptor domain architecture, specific phosphorylation and dimerization are possibly essential mechanisms for ligand-mediated catalysis and signaling.

Effects of methylprednisolone on electrolyte transport by in vitro rat ileum

1981 ◽  
Vol 240 (5) ◽  
pp. G365-G370 ◽  
Author(s):  
Y. H. Tai ◽  
R. A. Decker ◽  
W. G. Marnane ◽  
A. N. Charney ◽  
M. Donowitz
Keyword(s):  
Atpase Activity ◽  
Guanylate Cyclase ◽  
Short Circuit ◽  
Electrical Potential ◽  
Cyclase Activity ◽  
Secretory Process ◽  
Electrical Potential Difference ◽  
Guanylate Cyclase Activity ◽  
Cl Secretion

Administration of the glucocorticoid methylprednisolone (MP) (30 mg/kg body wt for 3 days) to rats increased intestinal mucosal guanylate cyclase and Na-K-ATPase activities, short-circuit current (Isc), electrical potential difference (PD), net Na absorption, and net Cl secretion and reversed HCO3 transport from secretion to absorption. In the MP-treated animals, removal of HCO3 from both the mucosal and serosal bathing solutions increased Cl secretion but did not alter the Isc, PD, and net Na flux. Removal of Cl abolished the MP-induced increase in Isc but did not affect the MP-induced changes in net Na and HCO3 fluxes. At 6 h, after a single dose of MP, stimulation of guanylate cyclase activity was already maximal, whereas Na-K-ATPase activity was not detectably altered. The changes in intestinal transport properties present 6 h after MP treatment and associated with the increased guanylate cyclase activity were an increase in Isc and PD and a reversal of net Cl absorption to net secretion. These results suggest that an initial response to MP administration is a persistent increase in intestinal guanylate cyclase activity that mediates an electrogenic Cl secretory process, then is followed by a superimposed effect of increased Na-K-ATPase activity that mediates an increase in net Na absorption.

Adenylate and guanylate cyclase activity in the penis and aorta of the diabetic rat: an in vitro study

1994 ◽  
Vol 74 (1) ◽  
pp. 106-111 ◽  
Author(s):  
M.A.W. MILLER ◽  
R.J. MORGAN ◽  
C.S. THOMPSON ◽  
D.P. MIKHAILIDIS ◽  
J.Y. JEREMY
Keyword(s):  
Guanylate Cyclase ◽  
In Vitro Study ◽  
Vitro Study ◽  
Cyclase Activity ◽  
Diabetic Rat ◽  
Guanylate Cyclase Activity
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