Variations in Functional Activity of the Hormone-Sensitive Adenylate Cyclase System in Tissues of Gastropod Mollusks with Streptozotocin-Induced Diabetes

2008 ◽  
Vol 146 (4) ◽  
pp. 424-428 ◽  
Author(s):  
A. O. Shpakov ◽  
L. A. Kuznetsova ◽  
S. A. Plesneva ◽  
M. N. Pertseva
Keyword(s):  
Adenylate Cyclase ◽  
Functional Activity ◽  
Adenylate Cyclase System ◽  
Gastropod Mollusks ◽  
Streptozotocin Induced Diabetes ◽  
Hormone Sensitive

Effects of benzyl alcohol on PTH receptor-adenylate cyclase system of canine kidney

1985 ◽  
Vol 248 (1) ◽  
pp. E31-E35
Author(s):  
K. J. Martin ◽  
C. L. McConkey ◽  
T. J. Stokes
Keyword(s):  
Enzyme Activity ◽  
Adenylate Cyclase ◽  
Benzyl Alcohol ◽  
Membrane Fluidity ◽  
Phospholipid Composition ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Adenylate Cyclase System ◽  
Hormone Sensitive ◽  
Canine Kidney

In many systems, perturbations of membrane architecture by changes of lipid and phospholipid composition have been shown to alter the activity of membrane-bound enzymes. The present studies examined the effect of benzyl alcohol, an agent that has been shown to increase membrane fluidity, on the parathyroid hormone (PTH)-sensitive adenylate cyclase system of canine kidney. Benzyl alcohol progressively increased basal adenylate cyclase activity up to fourfold and maximal enzyme activity in the presence of PTH, GTP, guanylimidodiphosphate, and sodium fluoride by four- to sixfold. In the presence of 20 mM Mn2+ (no Mg2+), conditions under which enzyme activity is devoid of influence of guanine nucleotides or hormones, benzyl alcohol was without effect. PTH binding was increased by 25% in the presence of benzyl alcohol without a change in binding affinity. Fluorescent polarization studies using diphenylhexatriene showed a decrease in fluorescence anisotropy in the presence of benzyl alcohol. The results suggest that benzyl alcohol facilitates the interaction of the components of the adenylate cyclase system, presumably by increasing membrane fluidity. Alterations of membrane fluidity may be a potent means of regulating hormone sensitive adenylate cyclase activity.

Acetylcholine and norepinephrine interactions on cardiac lipids and hemodynamics

1975 ◽  
Vol 228 (6) ◽  
pp. 1678-1684 ◽  
Author(s):  
VV Glaviano ◽  
J Goldberg ◽  
MT Pindok
Keyword(s):  
Cyclic Amp ◽  
Adenylate Cyclase ◽  
Lipolytic Activity ◽  
Cardiac Metabolism ◽  
Left Ventricular ◽  
Extraction Ratio ◽  
Adenylate Cyclase System ◽  
Sodium Pentobarbital ◽  
Myocardial Uptake ◽  
Hormone Sensitive

In open-chest dogs anesthized with sodium pentobarbital, acetylcholine (ACh, 5 times 10'-5M) infused into the left circumflex coronary artery caused an increase in coronary flow and a decrease in myocardial O'2 extraction ratio (P less than .01) anduptake (P less than .05). Heart rate and mean arterial pressure were not altered,although left ventricular dP/dt declined from 2,037 plus or minus 205 to 1,873 plus or minus 194 mmHg/s (P less than .02). Intracoronary administration of norepinephrine (NE, 2.4 times 10'-6M) caused an increase in myocardial O'2 uptake (P less than .02); simultaneous infusion of both NE and ACh caused a decline in O'2 extraction ratio (P less than .01) and uptake (P less than 0.5). Myocardial adenylatecyclase activity in response to ACh was not altered significantly from a control levelof 188 plus or minus 22 pmol of '14C-labeled cyclic AMP/mg protein per 10 min. Norepinephrine alone elevated adenylate cyclase activity to 401 plus or minus 45 pmol ['14C]cyclic AMP/mg protein per 10 min (P less than .01). However, with simultaneous infusion of both NE and ACh, adenylate cyclase returned to control levels. Although ACh alone did not alter myocardial hormone-sensitive lipaseactivity, NE elevated lipolytic activity from 8.1 plus or minus .7 to 13.2 plus or minus 1.8 mueq free fatty acid (FTA)/g per 30 min (P less than .05). The administration of both ACh and NE returned lipase activity to nearly control levels. Myocardial uptake of FFA increased significantly during ACh infusion alone (P less than 0.5) and during NE infusion alone (P less than 905). However, when NE and AChwere administered together, a decline in FFA uptake was observed (P less than .02).These data indicate that the effects of ACh on cardiac metabolism are minimal, withthe decline in myocardial O'2 uptake of ACh primarily reflecting the decrease in contractility. On the other hand, antagonism of ACh on NE-stimulated myocardial lipid metabolism appears to involve activity of the adenylate cyclase system.

scholarly journals 3,3′,5-Triiodothyronine Administration In Vivo Modulates the Hormone-sensitive Adenylate Cyclase System of Rat Hepatocytes

1982 ◽  
Vol 69 (2) ◽  
pp. 414-426 ◽  
Author(s):  
Craig C. Malbon ◽  
Michael L. Greenberg
Keyword(s):  
Adenylate Cyclase ◽  
Rat Hepatocytes ◽  
Adenylate Cyclase System ◽  
Hormone Sensitive

The Parathyroid Hormone-Sensitive Adenylate Cyclase System in Plasma Membranes of Rat Liver research-article*

Endocrinology ◽  
1980 ◽  
Vol 107 (6) ◽  
pp. 2082-2087 ◽  
Author(s):  
WILLIAM NEUMAN ◽  
NANCY SCHNEIDER
Keyword(s):  
Parathyroid Hormone ◽  
Adenylate Cyclase ◽  
Rat Liver ◽  
Plasma Membranes ◽  
Adenylate Cyclase System ◽  
Research Article ◽  
Hormone Sensitive

scholarly journals Effects of litter removal on the lipolytic response and the regulatory components of the adenylate cyclase in adipocytes isolated from lactating rats

1992 ◽  
Vol 281 (2) ◽  
pp. 333-337 ◽  
Author(s):  
M Ros ◽  
G Alonso ◽  
F J Moreno
Keyword(s):  
Adipose Tissue ◽  
Adenylate Cyclase ◽  
Pertussis Toxin ◽  
Adrenergic Receptors ◽  
Plasma Membranes ◽  
Adenylate Cyclase System ◽  
Litter Removal ◽  
The Status ◽  
Hormone Sensitive ◽  
A1 Adenosine Receptors

The effects of litter removal on the status of different components of the hormone-sensitive adenylate cyclase system were analysed in plasma membranes of rat adipocytes. These effects were correlated with the decreased lipolytic response of adipose tissue. No changes in total number of A1 adenosine receptors or their affinity were detected in response to litter removal. In contrast, beta-adrenergic receptors showed a decrease (35%) in total number of receptors, without any significant change in their affinity. The status of alpha-GS and alpha-Gi, the alpha-subunits of G proteins which mediate stimulation and inhibition respectively of adenylate cyclase, were probed by cholera- and pertussis-toxin-catalysed ADP-ribosylation respectively and by immunoblot. Associated with litter removal, decreases of 63% and 62% in the incorporation of [alpha 32P]ADP-ribose catalysed by cholera toxin and pertussis toxin into alpha-Gs and alpha-Gi respectively were detected. Immunoblotting using RM/1 (anti-alpha-Gs) and AS/7 (anti-alpha-Gi) antisera also showed decreases in the levels of alpha-Gs (52%) and alpha-Gi (55%) in adipocyte membranes from litter-removed rats compared with lactating rats. Alterations in the status of hormone-sensitive adenylate cyclase components, such as those described herein, may be biochemical mechanism(s) by which adipose tissue shows a decreased lipolytic response during recovery from lactation.

Phorbol ester regulates stimulatory and inhibitory pathways of the hormone-sensitive adenylate cyclase system in rat reticulocytes

1988 ◽  
Vol 151 (2) ◽  
pp. 167-175 ◽  
Author(s):  
Atsushi Yamashita ◽  
Tomonori Kurokawa ◽  
Yasutomo Une ◽  
Sadahiko Ishibashi
Keyword(s):  
Adenylate Cyclase ◽  
Phorbol Ester ◽  
Adenylate Cyclase System ◽  
Inhibitory Pathways ◽  
Hormone Sensitive ◽  
Rat Reticulocytes
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