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G protein activation: a receptor-independent mode of action for cationic amphiphilic neuropeptides and venom peptides
Mousli, M.; Bueb, Jean-Luc; Bronner, C. et al.
1990In Trends in Pharmacological Sciences, 11 (9), p. 358-62
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Keywords :
pharmacology; Animals; Biotransformation; GTP-Binding Proteins; Humans; Molecular Sequence Data; Neuropeptides; Peptides; Wasp Venoms; metabolism; chemistry; Amino Acid Sequence
Abstract :
[en] The neuropeptide substance P, the venom peptide mastoparan and the synthetic polyamine compound 48/80 activate rat peritoneal mast cells, leading to rapid histamine release by exocytosis. Although these effects are inhibited by pertussis toxin and involve a transient increase in IP3, no selective membrane receptors have been identified. However, it has recently been shown that these compounds activate G proteins in vitro. Here Yves Landry and colleagues discuss the proposal that direct activation of G protein is the physiological mechanism of action of substance P on rat peritoneal mast cells, this mechanism being mimicked by mastoparan and 48/80, and possibly by other cationic amphiphilic peptides such as kinins. These compounds might be of help in defining the interaction between membrane receptors and G proteins.
Disciplines :
Biochemistry, biophysics & molecular biology
Identifiers :
UNILU:UL-ARTICLE-2008-205
Author, co-author :
Mousli, M.
Bueb, Jean-Luc ;  University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Life Science Research Unit
Bronner, C.
Rouot, B.
Landry, Y.
Language :
English
Title :
G protein activation: a receptor-independent mode of action for cationic amphiphilic neuropeptides and venom peptides
Publication date :
1990
Journal title :
Trends in Pharmacological Sciences
ISSN :
1873-3735
Publisher :
Elsevier, Cambridge, United Kingdom
Volume :
11
Issue :
9
Pages :
358-62
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBilu :
since 09 September 2013

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