Reference : G protein activation: a receptor-independent mode of action for cationic amphiphilic ...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/10993/5737
G protein activation: a receptor-independent mode of action for cationic amphiphilic neuropeptides and venom peptides
English
Mousli, M. [> >]
Bueb, Jean-Luc mailto [University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Life Science Research Unit >]
Bronner, C. [> >]
Rouot, B. [> >]
Landry, Y. [> >]
1990
Trends in Pharmacological Sciences
Elsevier
11
9
358-62
Yes (verified by ORBilu)
0165-6147
1873-3735
Cambridge
United Kingdom
[en] pharmacology ; Animals ; Biotransformation ; GTP-Binding Proteins ; Humans ; Molecular Sequence Data ; Neuropeptides ; Peptides ; Wasp Venoms ; metabolism ; chemistry ; Amino Acid Sequence
[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.
http://hdl.handle.net/10993/5737

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