Histamine inhibits cell spreading and C3bi receptor clustering and diminishes hydrogen peroxide production by adherent human neutrophils

Abstract

Cell adherence plays a central role in many host defense mechanisms. Human peripheral blood neutrophils possess cell surface receptors that contribute to cell adherence or detachment. Receptors specific for the C3bi cleavage fragment of the third component of complement (CR3) promote adhesion, whereas histamine receptors promote detachment. In the present study, we tested the ability of histamine to down-regulate the physiological effects of CR3 receptors. Histamine decreased the binding of 51Cr-labeled neutrophils to complement-coated surfaces (C3-coated surfaces) in a dose-dependent fashion. Scanning electron microscopic and optical microscopic observations of neutrophils on C3-coated surfaces revealed polarized or spherical cell morphologies in the absence or presence of histamine, respectively. Histamine inhibited the ability of CR3 to cluster on plasma membranes of neutrophils adherent to C3-coated surfaces as shown by fluorescence microscopy. In addition, histamine diminished but did not abolish the FMLP-stimulated increase in plasma membrane CR3 expression as measured by fluorometry. Histamine did not inhibit the release of marker proteins from specific or gelatinase containing granules by neutrophils in suspension. Histamine also diminished the FMLP-stimulated production of respiratory burst oxidants from cells in suspension or cells allowed to adhere to fibrinogen substrates. We suggest that histamine may modulate selective changes in neutrophil function by diminishing adherence and preventing changes in cell shape following cell activation.

High concentrations of histamine stimulate equine polymorphonuclear neutrophils to produce reactive oxygen species

“…Our results are in agreement with previously reported observations on alveolar macrophages, eosinophils and neutrophils isolated from histamine-rich blood [9][10][11][12][13], but are in opposition with most of the previously published results obtained with human, bovine and equine neutrophils [3][4][5][6][7][8]11]. A possible explanation to this opposition can be found in an assay specific discrepancy of histamine on the release of superoxide radicals, and in the high histamine concentrations used in our assays.…”

“…Intradermic injections of 2 ¥10 -3 M histamine led to the development of local oedema with circular lesions, that could be treated by administration of an antagonist drug of H1 receptors to histamine [2]. In neutrophils stimulated by N-formyl-methionyl-leucyl-phenylalanine (FMLP), phorbol 12-myristate 13-acetate (PMA) or calcium ionophore, histamine has very often been reported to be either inhibitor of the production of superoxide anion (O 2 • -) or without effect [3][4][5][6][7][8]. It was also reported that histamine alone was unable to stimulate neutrophils [3,5,8].…”

Convergence of the adhesive and fibrinolytic systems: recognition of urokinase by integrin αMβ2 as well as by the urokinase receptor regulates cell adhesion and migration

“…Although our model considers only the trimolecular complex of uPA, ␣ M ␤ 2 , and uPAR, we do not exclude additional regulatory roles of still higher order multimers induced by uPAR dimerization, 52 ␣ M ␤ 2 clustering, 53 or uPA-mediated bridging of ␣ M ␤ 2 to uPAR on adjacent cells.…”

Critical Role of L-Selectin and Histamine H4 Receptor in Zymosan-Induced Neutrophil Recruitment from the Bone Marrow: Comparison with Carrageenan

“…histamine-induced bone marrow efflux, it would seem that inhibition of Mac-1 promoted the efflux. It has been shown that histamine prevents complement fragment (C3bi)-induced Mac-1 clustering and chemoattractant-induced up-regulation and cell spreading in vitro, the suggestion being that histamine is negatively regulating cell adhesion (Francis et al, 1991). If a similar scenario occurs in vivo in the bone marrow whereby histamine inhibits Mac-1 function, explaining the result using anti-Mac-1 antibody becomes difficult.…”