scholarly journals Further studies on histamine release from rat mast cells in vitro induced by peptides. Characteristics of a synthetic intermediate with potent releasing activity

1980 ◽  
Vol 191 (1) ◽  
pp. 233-237 ◽  
Author(s):  
P D Roy ◽  
D M Moran ◽  
V Bryant ◽  
R Stevenson ◽  
D R Stanworth
Keyword(s):  
Mast Cells ◽  
Histamine Release ◽  
Synthetic Peptide ◽  
Structural Basis ◽  
Optical Isomers ◽  
Compound I ◽  
Synthetic Intermediate ◽  
Rat Mast Cells ◽  
Release Processes

Previous studies on histamine release by corticotropin peptides and melittin peptides were extended, leading to the identification of a synthetic peptide intermediate, Lys(Z)-Arg(NO2)-Arg(NO2)OMe, (I) as an active non-cytolytic histamine releaser from rat mast cells. However, significant differences in the releasing capacity of optical isomers of this compound, and of Lys-Lys-Arg-ArgOMe [methyl ester of corticotropin-(15-18)-tetrapeptide; ‘basic core’] were observed, with the L-forms being markedly more active. A study of various analogues of the tripeptide compound (I) indicated that the structural basis for mast-cell triggering by such peptidic agents was highly specific. The relevance of these observations to the immunologically induced histamine-release processes is discussed.

scholarly journals Further studies on the structural requirements for polypeptide-mediated histamine release from rat mast cells

1979 ◽  
Vol 181 (3) ◽  
pp. 623-632 ◽  
Author(s):  
B Jasani ◽  
G Kreil ◽  
B F Mackler ◽  
D R Stanworth
Keyword(s):  
Amino Acids ◽  
Mast Cells ◽  
Histamine Release ◽  
Immunoglobulin E ◽  
Polymyxin B ◽  
Carboxyl Group ◽  
Peritoneal Mast Cells ◽  
Normal Rat ◽  
Rat Mast Cells

Structure-activity studies have been performed on a series of naturally occurring and ‘tailor-made’ polypeptides, by measurement of ability to induce selective histamine release from normal rat peritoneal mast cells in vitro. Compounds investigated include corticotropin and melittin derivatives, mast-cell-degranulating peptide from bee venom, polymyxin B, bradykinin and various synthetic poly(amino acids) and short-chain peptides. It was confirmed that a cluster of four basic residues (lysine or arginine) was optimal for histamine release by corticotropin and melittin polypeptides, provided that the C-terminal carboxyl group was substituted (by, for instance, amidation). In contrast, the presence of a free C-terminal carboxyl group or nearby dicarboxylic acid residues led to a considerable diminution in histamine-releasing activity. Likewise, polypeptides comprised essentially of acidic amino acids were inactive. On the basis of these observations it has been possible to predict that synthetic peptides comprising a particular sequence within the Fc region of human immunoglobulin E, the immunoglobulin class particularly involved in mediation of allergic reactions of the immediate type, would possess potent histamine-releasing activity when similarly made to react with normal rat mast cells. The further study of such a structure should throw new light on the molecular basis of allergen-antibody triggering of mast cells.

Immunological Histamine Release from Rat Mast Cells in vitro: Effect of Age of Cell Donor

1965 ◽  
Vol 120 (2) ◽  
pp. 542-546 ◽  
Author(s):  
K. F. Austen ◽  
K. J. Bloch ◽  
A. R. Baker ◽  
B. G. Arnason
Keyword(s):  
Mast Cells ◽  
Histamine Release ◽  
Cell Donor ◽  
Vitro Effect ◽  
Effect Of Age ◽  
Rat Mast Cells
Sign in / Sign up

Export Citation Format

Share Document