Reference : Activation of rat peritoneal mast cells by substance P and mastoparan
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/10993/5740
Activation of rat peritoneal mast cells by substance P and mastoparan
English
Mousli, M. [> >]
Bronner, C. [> >]
Bueb, Jean-Luc mailto [University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Life Science Research Unit >]
Tschirhart, Eric mailto [University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Life Science Research Unit >]
Gies, J. P. [> >]
Landry, Y. [> >]
1989
Journal of Pharmacology and Experimental Therapeutics
American Society for Pharmacology and Experimental Therapeutics
250
1
329-35
Yes (verified by ORBilu)
0022-3565
1521-0103
Bethesda
MD
[en] physiology ; Neuraminidase ; Mast Cells ; Male ; Kinetics ; Inositol Phosphates ; Histamine Release ; Calcium Chloride ; Bee Venoms ; Peptides ; Pertussis Toxin ; Rats ; metabolism ; drug effects ; pharmacology ; p-Methoxy-N-methylphenethylamine ; Wasp Venoms ; Virulence Factors, Bordetella ; Substance P ; Rats, Inbred Strains ; Animals
[en] Incubation of rat peritoneal mast cells with substance P resulted in the transient stimulation of phosphoinositol breakdown and histamine secretion through an exocytotic process. These effects were inhibited markedly by a prior 2-hr exposure of the cells to pertussis toxin. Pertussis toxin also inhibited exocytosis induced by substance P, mastoparan and compound 48/80, but did not modify the secretory effect of the ionophore A23187. The transfer of rat peritoneal mast cells from balanced salt solution to calcium-free buffer led to a similar time-dependent decrease in their response to substance P and mastoparan. The concomitant absence of potassium from the calcium-free buffer enabled the mast cells to retain their secretory response. These data demonstrate identical dependency for calcium and monovalent ions of the secretory process elicited by substance P, mastoparan and compound 48/80. Pretreatment of mast cells with neuraminidase decreased the secretagogic effect of substance P, mastoparan and compound 48/80 without modifying the efficiency of the ionophore A23187. Thus, sialic acid residues might be involved in the initial binding of peptides and compound 48/80 to mast cells, which activate a pertussis toxin-sensitive G-protein and allows the increase in phospholipase C activity to induce exocytosis. This sequence of events might characterize the physiological pathway of mast cell activation by peptides, without necessarily requiring selective membrane receptors.
http://hdl.handle.net/10993/5740

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