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Mast cell degranulating (MCD) peptide and its optical isomer activate GTP binding protein in rat mast cells
Author(s) -
Fujimoto Ichiro,
Ikenaka Kazuhiro,
Kondo Tetsuro,
Aimoto Saburo,
Kuno Miyuki,
Mikoshiba Katsuhiko
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80005-n
Subject(s) - degranulation , peptide , calcium , pertussis toxin , chemistry , mast cell , mastoparan , biophysics , g protein , microbiology and biotechnology , biochemistry , receptor , biology , immunology , organic chemistry
The MCD peptide in bee venom induces degranulation in mast cells. The internal calcium concentration of mast cells increased and remained high following MCD stimulation. This calcium increase was blocked by pertussis toxin (Ptx) treatment, suggesting that MCD peptide activates Ptx‐sensitive G‐protein. Even in the absence of external calcium in the incubation medium, the calcium concentration increased by MCD treatment. but soon returned to the original level. D‐MCD, the optical isomer of the MCD peptide, also increased the internal calcium concentration through a Ptx‐sensitive pathway. We suggest that cationic clusters at one side of the surface are more important in activating the G‐protein than the α‐helix conformation.