Effects of chronic administration of doxorubicin on myocardial alpha-adrenergic receptors, histamine, cyclic nucleotides, calcium, norepinephrine, calmodulin, and guanylate cyclase activity, and plasma catecholamines in rats

1987 ◽  
Vol 54 (1) ◽  
pp. 182-189 ◽  
Author(s):  
Timothy W. Robison ◽  
Shri N. Giri
Keyword(s):  
Guanylate Cyclase ◽  
Cyclic Nucleotides ◽  
Adrenergic Receptors ◽  
Plasma Catecholamines ◽  
Chronic Administration ◽  
Cyclase Activity ◽  
Guanylate Cyclase Activity ◽  
Alpha Adrenergic Receptors

scholarly journals The metabolism of cyclic nucleotides in the guinea-pig pancreas. Adenylate cyclase and guanylate cyclase

1980 ◽  
Vol 186 (2) ◽  
pp. 499-505 ◽  
Author(s):  
M Lemon ◽  
P Methven ◽  
K Bhoola
Keyword(s):  
Adenylate Cyclase ◽  
Guinea Pig ◽  
Guanylate Cyclase ◽  
Cyclic Nucleotides ◽  
Cyclase Activity ◽  
Dependent Manner ◽  
Guanylate Cyclase Activity ◽  
Triton X ◽  
Dose Dependent ◽  
Significant Activation

Adenylate cyclase from the guinea-pig pancreas was activated in a dose-dependent manner by both secretin and cholecystokinin-pancreozymin, but in contrast with results in other species the hormones were approximately equipotent. All other hormones and transmitter substances tested were without any effect on adenylate cyclase activity. Guanylate cyclase activity was shown to have both particulate and supernatant components in the guinea-pig pancreas. The particulate enzyme, but not the supernatant enzyme, was markedly activated by Triton X-100, and most of the induced activity was released into the supernatant. The supernatant enzyme was specifically Mn2+-dependent, but, even though Mn2+ was maximally effective at a concentration of 3 mM, activity could be raised further by increasing Ca2+ concentration. The particulate enzyme, by contrast, was relatively Mn2+-independent. Activity of the particulate guanylate cyclase was enhanced by phosphatidylserine. The supernatant enzyme displayed classical Michaelis-Menten kinetics, but the particulate enzyme deviated markedly from such kinetics. Under none of the conditions used was any significant activation of guanylate cyclase observed with any of the secretogen hormones or transmitter substances.

Guanylate Cyclase Activity in Normal and Neoplastic Squamous Epithelia from the Upper Aero-Digestive Tract

ORL ◽  
1986 ◽  
Vol 48 (5) ◽  
pp. 265-269
Author(s):  
E.L. Rydell ◽  
K.L. Axelsson ◽  
J. Olofsson ◽  
J.E.S. Wikberg
Keyword(s):  
Digestive Tract ◽  
Guanylate Cyclase ◽  
Cyclase Activity ◽  
Guanylate Cyclase Activity ◽  
Squamous Epithelia

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

scholarly journals Histochemistry of guanylate cyclase activity.

1995 ◽  
Vol 43 (12) ◽  
pp. 1235-1240 ◽  
Author(s):  
S Mehdizadeh ◽  
A O'Farrell ◽  
L Bitensky ◽  
J Weisz ◽  
J Alaghband-Zadeh ◽  
...  
Keyword(s):  
Guanylate Cyclase ◽  
Cyclase Activity ◽  
Lead Ions ◽  
Ammonium Citrate ◽  
Considerable Proportion ◽  
Guanosine Triphosphate ◽  
Guanylate Cyclase Activity ◽  
Metal Capture ◽  
Cryostat Sections ◽  
Sufficient Concentration

Guanylate cyclase liberates pyrophosphate from guanosine triphosphate (GTP). In studies published previously, this phosphate is trapped by lead ions even though it is known that free lead ions inactivate a considerable proportion of this enzymatic activity. To overcome the damaging effects of fixation, this study used fresh cryostat sections stabilized with a sufficient concentration of a collagen-derived polypeptide to ensure no measurable loss of guanylate cyclase activity. To avoid the damaging influence of free lead ions, we used a hidden metal capture reagent, i.e., a complex of lead ammonium citrate/acetate that does not react with GTP but which rapidly forms a precipitate with the pyrophosphate liberated by the enzyme. The lead precipitate is then converted into the colored sulfide which is measured in individual cells by microdensitometry. This system was used to measure guanylate cyclase activity in individual cells in unfixed sections of rat liver.

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