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אסיף מאגר המחקר החקלאי
פותח על ידי קלירמאש פתרונות בע"מ -
Multi-signal transduction of the pheromonotropic response by pheromone gland incubations of Helicoverpa armigera
Year:
1995
Authors :
סורוקר, ויקטוריה
;
.
רפאלי, עדה
;
.
Volume :
25
Co-Authors:
Soroker, V., Department of Zoology, Tel Aviv University, Tel Aviv, 69978, Israel
Rafaeli, A., Department of Stored Products, ARO, The Volcani Center, P.O. Box 6, Bet Dagan, Israel
Facilitators :
From page:
1
To page:
9
(
Total pages:
9
)
Abstract:
The transduction of the pheromonotropic response by the pheromone glands of Helicoverpa armigera females was studied using an in vitro bioassay. Pheromonotropic activity was observed in the presence of the phorbol ester, phorbol-12-myristate 13-acetate, ionomycin and adenosine 3′-, 5′-cyclic monophosphathioate suggesting that several transducing systems (phosphatidylinositol breakdown; calcium levels; and adenylate cyclase activity) play a role in the mediation of the pheromonotropic activation due to PBAN. The involvement and interaction of the different messengers was further studied using various inhibitors of protein kinases and calcium-calmodulin. The stimulation of pheromonotropic activity by PBAN was observed to be calcium dependent, however, at high PBAN concentration (20 pmol) there was a calcium-independent pheromonotropic response. Experiments with the phorbol ester, phorbol-12-myristate 13-acetate, indicated that the activation of pheromone production by protein kinase-C is calcium-dependent. Stimulation of the adenylate cyclase pathway by PBAN was also calcium-dependent. The interaction between intracellular cAMP production and calcium levels was tested using a cAMP RIA. Studies concerning the elevation of intracellular cAMP levels as a result of the ionophore, ionomycin, suggested that during the pheromone gland stimulation, calcium activates adenylate cyclase. © 1995.
Note:
Related Files :
Helicoverpa armigera
In vitro
PBAN
Pheromone biosynthesis
Pheromone gland
Second messengers
עוד תגיות
תוכן קשור
More details
DOI :
10.1016/0965-1748(94)00049-N
Article number:
0
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
19574
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:30
You may also be interested in
Scientific Publication
Multi-signal transduction of the pheromonotropic response by pheromone gland incubations of Helicoverpa armigera
25
Soroker, V., Department of Zoology, Tel Aviv University, Tel Aviv, 69978, Israel
Rafaeli, A., Department of Stored Products, ARO, The Volcani Center, P.O. Box 6, Bet Dagan, Israel
Multi-signal transduction of the pheromonotropic response by pheromone gland incubations of Helicoverpa armigera
The transduction of the pheromonotropic response by the pheromone glands of Helicoverpa armigera females was studied using an in vitro bioassay. Pheromonotropic activity was observed in the presence of the phorbol ester, phorbol-12-myristate 13-acetate, ionomycin and adenosine 3′-, 5′-cyclic monophosphathioate suggesting that several transducing systems (phosphatidylinositol breakdown; calcium levels; and adenylate cyclase activity) play a role in the mediation of the pheromonotropic activation due to PBAN. The involvement and interaction of the different messengers was further studied using various inhibitors of protein kinases and calcium-calmodulin. The stimulation of pheromonotropic activity by PBAN was observed to be calcium dependent, however, at high PBAN concentration (20 pmol) there was a calcium-independent pheromonotropic response. Experiments with the phorbol ester, phorbol-12-myristate 13-acetate, indicated that the activation of pheromone production by protein kinase-C is calcium-dependent. Stimulation of the adenylate cyclase pathway by PBAN was also calcium-dependent. The interaction between intracellular cAMP production and calcium levels was tested using a cAMP RIA. Studies concerning the elevation of intracellular cAMP levels as a result of the ionophore, ionomycin, suggested that during the pheromone gland stimulation, calcium activates adenylate cyclase. © 1995.
Scientific Publication
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