The stimulation of dopa decarboxylase activity by ecdysone and its enhancement by cyclic AMP in adult mosquitoes

1973 ◽  
Vol 54 (2) ◽  
pp. 784-789 ◽  
Author(s):  
Morton S. Fuchs ◽  
Dorothy A. Schlaeger
Keyword(s):  
Cyclic Amp ◽  
Dopa Decarboxylase ◽  
Decarboxylase Activity ◽  
Stimulation Of

scholarly journals ECDYSONE-MEDIATED STIMULATION OF DOPA DECARBOXYLASE ACTIVITY AND ITS RELATIONSHIP TO OVARIAN DEVELOPMENT IN AEDES AEGYPTI

1974 ◽  
Vol 61 (2) ◽  
pp. 454-465 ◽  
Author(s):  
Dorothy A. Schlaeger ◽  
Morton S. Fuchs ◽  
Suk-Hee Kang
Keyword(s):  
Aedes Aegypti ◽  
Blood Meal ◽  
Ovarian Development ◽  
Blood Feeding ◽  
Dopa Decarboxylase ◽  
Decarboxylase Activity ◽  
Molting Hormone ◽  
Radioimmune Assay ◽  
Juvenile Hormone Mimic ◽  
Stimulation Of

Very little dopa decarboxylase activity is detectable in adult female mosquitoes Aedes aegypti which have not been allowed to engorge blood. However, when such females are injected with the molting hormone ß-ecdysone a marked stimulation of this enzyme's activity is observable. No stimulation is observed in males similarly injected, nor in females injected with cholesterol or a juvenile hormone mimic. In addition, ecdysone injection initiates ovarian development in these anautogenous non-blood-fed mosquitoes. The extent of stimulation in both cases is dependent upon the amount of ß-ecdysone administered. These results suggested that ecdysone may play a role in ovarian development in Aedes and led us to hypothesize that a normal blood meal may trigger the synthesis, activation, or release of this hormone endogenously. Using the radioimmune assay for ecdysone developed by Borst and O'Connor (Science [Wash. D. C.] 178:4–18.), we found that the titer of an antigenic-positive material, presumably ecdysone or a closely related analogue, substantially increased 24 h after blood feeding, thereby supporting our postulation.

scholarly journals Cell-type differences in the serum and cyclic AMP-dependent regulation of ornithine decarboxylase activity in two cultured fibroblast types

1982 ◽  
Vol 204 (1) ◽  
pp. 357-360 ◽  
Author(s):  
R J Boucek ◽  
J Weiss ◽  
K J Lembach
Keyword(s):  
Cyclic Amp ◽  
Ornithine Decarboxylase ◽  
Decarboxylase Activity ◽  
Cell Type ◽  
Dibutyryl Cyclic Amp ◽  
Cultured Fibroblasts ◽  
Ornithine Decarboxylase Activity ◽  
Serum Stimulation ◽  
3T3 Fibroblasts ◽  
Stimulation Of

Serum re-feeding stimulated ornithine decarboxylase (ODC) activity 8 to 10-fold in FS fibroblasts and 5 to 8-fold in 3T3 fibroblasts. Addition of dibutyryl cyclic AMP or 3-isobutyl-1-methylxanthine at the time of serum re-feeding further stimulated ODC activity in 3T3 fibroblasts but inhibited the serum stimulation of ODC activity in FS fibroblasts. It is suggested that serum and cyclic AMP independently regulate ODC activity in cultured fibroblasts.

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.

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