G protein-dependent activation of mast cell by peptides and basic secretagogues.
Signaling pathways leading to exocytosis and arachidonate release from serosal mast cells by basic secretagogues, including cationic peptides, arise from the involvement of betagamma subunits from G(i2) and G(i3) GTP-binding proteins. The original concept that basic secretagogues directly interact with G proteins implicated the entry of secretagogues into mast cells. This has been demonstrated only for the neuropeptide substance P. Basic secretagogues might share a common mechanism of penetration with the newly described cell-penetrating peptides. The involvement of some membrane transporter or non-selective membrane receptor to basic secretagogues cannot be excluded.
Laboratoire de Neuroimmunopharmacologie, Faculté de Pharmacie, INSERM U425, Université Louis Pasteur-Strasbourg I, bp 24, 67401 Illkirch Cedex, France.
Xavier
X
Ferry
Stephan
S
Brehin
Rehab
R
Kamel
Yves
Y
Landry
D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D019204:GTP-Binding Proteins / Q000378:metabolism*; D006801:Humans; D008407:Mast Cells / Q000378:metabolism*; D009478:Neuropeptide Y / Q000378:metabolism; D009496:Neurotensin / Q000378:metabolism; D010455:Peptides / Q000378:metabolism*; D021381:Protein Transport / Q000502:physiology; D051381:Rats; D013373:Substance P / Q000378:metabolism
D009478:Neuropeptide Y; D010455:Peptides; D013373:Substance P; D009496:Neurotensin; D019204:GTP-Binding Proteins