Histamine release from isolated guinea pig mast cells by anaphylatoxin.
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Biomedical subjects
Publications and source records attributed to F L Pearce.
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Antisera were raised against nerve growth factors isolated from mouse salivary gland and five venoms representative of the three main families of poisonous snakes. Immunochemical cross-reactivity was assessed from the ability of the antisera to inhibit the biological activities of the heterologous antigens. The high and low molecular weight forms of the salivary gland factors were found to be immunologically identical but distinct from the snake venom factors. The snake venom factors, on the other hand, were immunologically closely related to each other but not identical.
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Human mast cell heterogeneity was assessed by histochemical and detailed functional criteria using mast cells isolated from foreskin, uterine myometrium and lung parenchyma. The skin mast cells were histochemically distinct from their counterparts in the other two tissues by being predominantly insensitive to blockage of dye-binding following formalin fixation (ca. 80%). Functionally, a wide range of structurally diverse polycationic compounds induced selective histamine release from the skin mast cells (ca. 10% at top concentrations) although these cells were less responsive to immunological ligands and calcium ionophores when compared with the uterine and lung cells. The basic compounds, polyarginine and histone, proved to be more generalised histamine liberators as compared with their structural analogues, polylysine and protamine sulphate, probably by virtue of their high content of arginine residues and hydrophobic nature (histone). Studies with the anaphylatoxin, C3a, and its analogues 21R and C3ades Arg on skin mast cells emphasized the importance of basic amino acids for histamine-liberating peptides. Skin mast cells also proved more susceptible than their uterine counterparts to lysis by the detergents, Triton X-100 and Tween 20, suggesting that fundamental differences in membrane structure and/or fluidity might account for functional heterogeneity within the human mast cell population.
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