Inhibition of .beta.-bungarotoxin binding to brain membranes by mast cell degranulating peptide, toxin I, and ethylene glycol bis(.beta.-aminoethyl ether)-N,N,N',N'-tetraacetic acid

Biochemistry ◽  
1988 ◽  
Vol 27 (3) ◽  
pp. 963-967 ◽  
Author(s):  
Ralf R. Schmidt ◽  
Heinrich Betz ◽  
Hubert Rehm
Keyword(s):  
Mast Cell ◽  
Ethylene Glycol ◽  
Tetraacetic Acid ◽  
Brain Membranes ◽  
Peptide Toxin ◽  
Mast Cell Degranulating

ADP-ribosylation of rho proteins is inhibited by melittin, mast cell degranulating peptide and compound 48/80

1992 ◽  
Vol 226 (1) ◽  
pp. 87-91 ◽  
Author(s):  
Gertrud Koch ◽  
Barbara Habermann ◽  
Christiane Mohr ◽  
Ingo Just ◽  
Klaus Aktories
Keyword(s):  
Mast Cell ◽  
Rho Proteins ◽  
Adp Ribosylation ◽  
Mast Cell Degranulating

Synthetic analogs of mast cell degranulating (MCD) peptide

Peptides 1990 ◽  
1991 ◽  
pp. 746-747
Author(s):  
Angeliki Buku ◽  
Christian Birr ◽  
Diana Gazis
Keyword(s):  
Mast Cell ◽  
Synthetic Analogs ◽  
Mast Cell Degranulating

Phospholipase A2 activation in human neutrophils requires influx of extracellular Ca2+ and leukotriene B4

1995 ◽  
Vol 268 (1) ◽  
pp. C138-C146 ◽  
Author(s):  
S. Reddy ◽  
R. Bose ◽  
G. H. Rao ◽  
M. Murthy
Keyword(s):  
Ethylene Glycol ◽  
Phospholipase A2 ◽  
Platelet Activating Factor ◽  
Leukotriene B4 ◽  
Lipid Mediators ◽  
Oxidation Products ◽  
Human Neutrophils ◽  
Tetraacetic Acid ◽  
A 23187 ◽  
Transient Elevation

We have demonstrated that phospolipase A2 (PLA2) activation in human neutrophils requires both the influx of extracellular Ca2+ and leukotriene B4 (LTB4). Surprisingly, the eicosanoids (LTB4 and its omega-oxidation products) formed were quantitatively very similar in both thapsigargin (Thap)- and A-23187-stimulated neutrophils. In contrast, Thap had very little effect on the activation of PLA2 when 5-lipoxygenase (5-LO) was blocked by BW755C or MK-886, whereas A-23187 caused a substantial activation. The lack of PLA2 activation in Thap-stimulated neutrophils results from the inhibition of LTB4 formation in the presence of 5-LO inhibitors. It appears that A-23187 activates both LTB4-dependent and -independent PLA2, whereas Thap activates LTB4-dependent PLA2. Experiments with ethylene glycol-bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid demonstrated that activation of Thap-sensitive PLA2 and 5-LO requires the influx of Ca2+. Neither the transient elevation of cytosolic Ca2+ from intracellular stores nor the sustained Ca2+ influx alone without LTB4 appears sufficient to cause the activation of LTB4-dependent PLA2. We suggest that the activation of LTB4-dependent PLA2 involves 1) a sustained elevation of cytosolic Ca2+ coupled to the influx of extracellular Ca2+ and 2) a coupling between LTB4 and its receptor. We conclude that LTB4-dependent PLA2 plays an important role in the poststimulatory formation of lipid mediators such as prostaglandins, leukotrienes, and platelet-activating factor.

Mast cell degranulating (MCD) peptide analogs with reduced ring structure

1992 ◽  
Vol 11 (3) ◽  
pp. 275-280 ◽  
Author(s):  
A. Buku ◽  
J. Reibman ◽  
A. Pistelli ◽  
P. Blandina ◽  
D. Gazis
Keyword(s):  
Mast Cell ◽  
Ring Structure ◽  
Peptide Analogs ◽  
Reduced Ring ◽  
Mast Cell Degranulating
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