scholarly journals Synthetic peptides comprising sequences of the human immunoglobulin E heavy chain capable of releasing histamine

1979 ◽  
Vol 180 (3) ◽  
pp. 665-668 ◽  
Author(s):  
D R Stanworth ◽  
M Kings ◽  
P D Roy ◽  
J M Moran ◽  
D M Moran
Keyword(s):  
Mast Cells ◽  
Immunoglobulin E ◽  
Structure Activity ◽  
Peritoneal Mast Cells ◽  
Normal Rat ◽  
Antigen Interaction ◽  
A Site ◽  
Relationship Of ◽  
Histamine Liberators ◽  
Induce Histamine Release

On the basis of previous studies on the structure-activity relationship of model polypeptide histamine liberators, a site within the Fc region of immunoglobulin E antibody molecules has been proposed as that responsible for the direct triggering of target mast cells after antigen challenge. Peptides comprising this region of the epsilon-chain have now been synthesized and shown to induce histamine release from normal rat peritoneal mast cells in a selective manner essentially similar to that mediated by anaphylactic antibody-antigen interaction.

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.

scholarly journals Evidence for a role of phosphatidylinositol turnover in stimulus–secretion coupling. Studies with rat peritoneal mast cells

1979 ◽  
Vol 178 (3) ◽  
pp. 681-687 ◽  
Author(s):  
Shamshad Cockcroft ◽  
Bastien D. Gomperts
Keyword(s):  
Mast Cells ◽  
Concanavalin A ◽  
Immunoglobulin E ◽  
Histamine Secretion ◽  
Phosphatidylinositol Turnover ◽  
Phosphatidylinositol Response ◽  
Peritoneal Mast Cells ◽  
Stimulus Secretion Coupling ◽  
Rat Peritoneal Mast Cells

Histamine secretion and phosphatidylinositol turnover were compared in antigen-sensitized rat peritoneal mast cells stimulated with a number of different ligands. A small and variable increase in the incorporation of [32P]Pi and of [3H]inositol into phosphatidylinositol was observed when the cells were treated with immunoglobulin E-directed ligands (antigens and concanavalin A), and this was accompanied by a low amount of secretion (<10% of total cell histamine). In the presence of added phosphatidylserine, the addition of immunoglobulin E-directed ligands invariably led to an enhanced rate (approx. 4-fold) of labelling of phosphatidylinositol and, in the presence of Ca2+, this was accompanied by the secretion of histamine. The labelling of phosphatidylinositol and histamine secretion were also stimulated by chymotrypsin and compound 48/80. Whereas the phosphatidylinositol response did not require the presence of extracellular Ca2+, the secretion of histamine was either enhanced or dependent on extracellular Ca2+ (depending on the ligand used). The dependence on ligand concentration for the phosphatidylinositol response and histamine secretion were similar. The increased isotopic incorporation into phosphatidylinositol continued for about 1h although histamine secretion (elicited with concanavalin A) stopped within 2min. These results support the proposition that metabolic events involving phosphatidylinositol play a necessary intermediate role in the regulation of Ca2+ channels by ligand-activated receptors.

Effects of Siegesbeckia pubescens on Immediate Hypersensitivity Reaction

1997 ◽  
Vol 25 (02) ◽  
pp. 163-167 ◽  
Author(s):  
Hyung Min Kim
Keyword(s):  
Mast Cells ◽  
Hypersensitivity Reaction ◽  
Histamine Release ◽  
Immunoglobulin E ◽  
Immediate Hypersensitivity ◽  
Antiallergic Activity ◽  
Peritoneal Mast Cells ◽  
Ige Mediated ◽  
Rat Peritoneal Mast Cells ◽  
Siegesbeckia Pubescens

This study was carried out to examine the effect of an aqueous extract from Siegesbeckia pubescens (Compositae) (SPAE) on immunoglobulin E (IgE)-mediated immediate hypersensitivity reaction. Forty-eight hours passive cutaneous anaphylaxis in rats was significantly inhibited by oral administration of SPAE (100 μg/g). It also inhibited histamine release from rat peritoneal mast cells induced by anti-dinitrophenyl (DNP)-IgE and DNP-human serum albumin. The data indicate that SPAE has antiallergic activity, and that its action may be due to inhibition of histamine release from mast cells.

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