THE PROPERTIES OF ADENYLATE CYCLASE SYSTEM IN EMBRYONIC SKELETAL MUSCLES

1981 ◽  
Vol 9 (2) ◽  
pp. 208P-208P
Author(s):  
M. N. Pertseva ◽  
T. I. Mazina ◽  
L. A. Kuznetzova ◽  
S. A. Plesneva
Keyword(s):  
Adenylate Cyclase ◽  
Skeletal Muscles ◽  
Adenylate Cyclase System

Changes in skeletal muscle glycogenolysis after prolonged cold exposure and repeated injections with isoproterenol

1979 ◽  
Vol 57 (9) ◽  
pp. 938-943 ◽  
Author(s):  
M. C. Thibault ◽  
C. Côté ◽  
J. Vallières
Keyword(s):  
Adenylate Cyclase ◽  
Cold Stress ◽  
Tibialis Anterior ◽  
Skeletal Muscles ◽  
Glycogen Phosphorylase ◽  
Phosphorylase Kinase ◽  
Adenylate Cyclase System ◽  
Great Capacity ◽  
Contracting Muscle

Wistar rats were either given daily injections of isoproterenol (ISO) (15 μg/100 g per day) or exposed to 6 °C for 4 or 12 weeks (cold acclimated (CA)). After a 4-week exposure to cold and to ISO, acute cold stress (4 h at –18 °C) produced a 48% depletion of glycogen in the tibialis anterior of control rats while it did not significantly affect the levels in ISO-treated and CA animals. ISO treatment enhanced the in vivo response of phosphorylase kinase and glycogen phosphorylase to epinephrine (EPI) in the tibialis anterior, a fast contracting muscle. In the soleus, a slow contracting muscle known to be more sensitive to catecholamines, chronic treatment with ISO also resulted in increased basal and EPI-stimulated adenylate cyclase activity. No evidence could be found for an alteration of the glycogenolytic pathway (adenylate cyclase system, phosphorylase kinase, and glycogen phosphorylase) in fast contracting skeletal muscles of CA rats. It is concluded that ISO-treated and CA rats, which have a great capacity for nonshivering thermogenesis, do not rely on their muscle carbohydrate reserves during cold stress. It might be suggested that plasma levels of catecholamines higher than those produced by exposure to 6 °C are required to alter glycogenolytic mechanisms in fast contracting rat skeletal muscles.

scholarly journals Adenylate cyclase system of bovine adrenal plasma membranes.

1975 ◽  
Vol 250 (4) ◽  
pp. 1186-1192
Author(s):  
F M Finn ◽  
J A Montibeller ◽  
Y Ushijima ◽  
K Hofmann
Keyword(s):  
Adenylate Cyclase ◽  
Plasma Membranes ◽  
Adenylate Cyclase System

scholarly journals The Glucagon-sensitive Adenylate Cyclase System in Plasma Membranes of Rat Liver

1972 ◽  
Vol 247 (7) ◽  
pp. 2038-2043 ◽  
Author(s):  
Lutz Birnbaumer ◽  
Stephen L. Pohl ◽  
Martin Rodbell ◽  
Finn Sundby
Keyword(s):  
Adenylate Cyclase ◽  
Rat Liver ◽  
Plasma Membranes ◽  
Adenylate Cyclase System

scholarly journals Independent mechanisms of adenosine activation and inhibition of the turkey erythrocyte adenylate cyclase system.

1980 ◽  
Vol 255 (22) ◽  
pp. 10841-10846 ◽  
Author(s):  
P.M. Lad ◽  
T.B. Nielsen ◽  
C. Londos ◽  
M.S. Preston ◽  
M. Rodbell
Keyword(s):  
Adenylate Cyclase ◽  
Adenylate Cyclase System

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.

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