Detection and investigation of a protein factor concerned with the stimulation of disulfide reductase activity by cyclic AMP and other effectors

1976 ◽  
Vol 81 (6) ◽  
pp. 819-822
Author(s):  
V. I. Kulinskii ◽  
L. S. Kolesnichenko
Keyword(s):  
Cyclic Amp ◽  
Reductase Activity ◽  
Protein Factor ◽  
Disulfide Reductase ◽  
Stimulation Of

Stimulation of cyclic AMP formation and nerve electrical activity by octopamine in the terminal abdominal ganglion of the female gypsy moth Lymantria dispar

2006 ◽  
Vol 1071 (1) ◽  
pp. 63-74 ◽  
Author(s):  
Maria C. Olianas ◽  
Paolo Solari ◽  
Luciana Garau ◽  
Anna Liscia ◽  
Roberto Crnjar ◽  
...  
Keyword(s):  
Cyclic Amp ◽  
Electrical Activity ◽  
Gypsy Moth ◽  
Lymantria Dispar ◽  
Abdominal Ganglion ◽  
Stimulation Of

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.

scholarly journals Stimulation of Cyclic AMP Formation by Pituitary Adenylate Cyclase-Activating Polypeptide Is Attenuated by Glutamate in Rat Brain Slices

1995 ◽  
Vol 67 (4) ◽  
pp. 399-402
Author(s):  
Kaoru Kondo ◽  
Hitoshi Hashimoto ◽  
Kazuko Sakata ◽  
Hiroshi Saga ◽  
Jun-ichi Kitanaka ◽  
...  
Keyword(s):  
Cyclic Amp ◽  
Adenylate Cyclase ◽  
Rat Brain ◽  
Brain Slices ◽  
Pituitary Adenylate Cyclase ◽  
Stimulation Of

scholarly journals Turnover of protein-bound serine phosphate in respiring slices of guinea-pig cerebral cortex. Effects of putative transmitters, tetrodotoxin and other agents

1973 ◽  
Vol 132 (3) ◽  
pp. 475-482 ◽  
Author(s):  
Martin Reddington ◽  
Richard Rodnight ◽  
Michael Williams
Keyword(s):  
Cerebral Cortex ◽  
Cyclic Amp ◽  
Guinea Pig ◽  
Electrical Pulses ◽  
Phosphorus Turnover ◽  
Serine Phosphate ◽  
Stimulation Of

1. The effect of various agents on the turnover of protein-bound phosphorus in respiring slices of cerebral cortex was studied. 2. Confirming previous work turnover was increased by the application of electrical pulses for 10s to the tissue. 3. Turnover was also increased by exposure of the slices for 10min to noradrenaline (0.5mm), 5-hydroxytryptamine (1μm) and histamine (0.1mm). 4. When slices were stimulated by electrical pulses in the presence of histamine the increase in turnover was the sum of the responses given by each agent above, suggesting that different phosphorylating systems were involved. 5. Tetrodotoxin (0.5μm) blocked the increased turnover due to electrical pulses, but not that due to histamine. Tetrodotoxin also prevented the increase in tissue cyclic AMP content caused by the application of electrical pulses. 6. Phosphoprotein turnover was not affected by adenosine, despite the increase in tissue cyclic AMP content given by this agent. 7. Adenosine blocked the phosphoprotein response to histamine, but did not affect the response to electrical pulses. 8. The results are discussed in relation to the hypothesis that the stimulation of protein phosphorus turnover by electrical pulses is secondary to the release of cyclic AMP in the tissue.

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