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אסיף מאגר המחקר החקלאי
פותח על ידי קלירמאש פתרונות בע"מ -
PBAN selective antagonists: Inhibition of PBAN induced cuticular melanization and sex pheromone biosynthesis in moths
Year:
2005
Source of publication :
Journal of Insect Physiology
Authors :
אלטשטיין, מרים
;
.
בן-עזיז, אורנה
;
.
זלצר, אירנה
;
.
Volume :
51
Co-Authors:
Ben-Aziz, O., Department of Entomology, Volcani Center, Bet Dagan 50250, Israel
Zeltser, I., Department of Entomology, Volcani Center, Bet Dagan 50250, Israel
Altstein, M., Department of Entomology, Volcani Center, Bet Dagan 50250, Israel
Facilitators :
From page:
305
To page:
314
(
Total pages:
10
)
Abstract:
A D-Phe scan (sequential D-Phe replacement) library of linear peptides, synthesized on the basis of a slightly modified active sequence of PBAN (YFSPRL-amide) was employed to detect potential inhibitors of cuticular melanization in Spodoptera littoralis larvae and to compare their stimulatory and inhibitory melanization activity with their pheromonotropic agonistic and antagonistic activities. A quantitative melanotropic assay was used to monitor the extent of cuticular melanization elicited by Hez-PBAN1-33NH2 in S. littoralis larvae in the presence and absence of the D-Phe peptides. The data revealed the presence of two partial melanotropic antagonists, and disclosed the presence of selective pure melanotropic agonists and pure pheromonotropic antagonists indicating differences in the inhibitory and stimulatory patterns of the library with respect to both activities. The differences between the pheromonotropic and melanotropic inhibitory patterns of the peptides hints at the possibility that sex pheromone biosynthesis in the pheromone gland of Heliothis peltigera females and induction of cuticular melanization in S. littoralis may be mediated by different receptors (that may result either from presence of different receptor sub-types or may reflect species differences in receptor structure and/or properties) despite the fact that they are induced by the same peptide (PBAN1-33NH2). © 2004 Elsevier Ltd. All rights reserved.
Note:
Related Files :
Animal
Animals
biosynthesis
Lepidoptera
metabolism
neuropeptide
Peltigera
peptides
עוד תגיות
תוכן קשור
More details
DOI :
10.1016/j.jinsphys.2004.11.017
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
20686
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:38
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Scientific Publication
PBAN selective antagonists: Inhibition of PBAN induced cuticular melanization and sex pheromone biosynthesis in moths
51
Ben-Aziz, O., Department of Entomology, Volcani Center, Bet Dagan 50250, Israel
Zeltser, I., Department of Entomology, Volcani Center, Bet Dagan 50250, Israel
Altstein, M., Department of Entomology, Volcani Center, Bet Dagan 50250, Israel
PBAN selective antagonists: Inhibition of PBAN induced cuticular melanization and sex pheromone biosynthesis in moths
A D-Phe scan (sequential D-Phe replacement) library of linear peptides, synthesized on the basis of a slightly modified active sequence of PBAN (YFSPRL-amide) was employed to detect potential inhibitors of cuticular melanization in Spodoptera littoralis larvae and to compare their stimulatory and inhibitory melanization activity with their pheromonotropic agonistic and antagonistic activities. A quantitative melanotropic assay was used to monitor the extent of cuticular melanization elicited by Hez-PBAN1-33NH2 in S. littoralis larvae in the presence and absence of the D-Phe peptides. The data revealed the presence of two partial melanotropic antagonists, and disclosed the presence of selective pure melanotropic agonists and pure pheromonotropic antagonists indicating differences in the inhibitory and stimulatory patterns of the library with respect to both activities. The differences between the pheromonotropic and melanotropic inhibitory patterns of the peptides hints at the possibility that sex pheromone biosynthesis in the pheromone gland of Heliothis peltigera females and induction of cuticular melanization in S. littoralis may be mediated by different receptors (that may result either from presence of different receptor sub-types or may reflect species differences in receptor structure and/or properties) despite the fact that they are induced by the same peptide (PBAN1-33NH2). © 2004 Elsevier Ltd. All rights reserved.
Scientific Publication
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