title: 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.
authors.affiliation: Department of Biological Sciences, Wayne State University, Detroit, Michigan 48202.
authors.forename: J W
authors.initials: JW
authors.lastname: Francis
authors.forename: R F
authors.initials: RF
authors.lastname: Todd
authors.forename: L A
authors.initials: LA
authors.lastname: Boxer
authors.forename: H R
authors.initials: HR
authors.lastname: Petty
mesh_terms: D002448:Cell Adhesion / Q000187:drug effects*; D015550:Cell Degranulation / Q000187:drug effects; D003176:Complement C3 / Q000378:metabolism; D006632:Histamine / Q000494:pharmacology*; D006801:Humans; D006861:Hydrogen Peroxide / Q000378:metabolism*; D066298:In Vitro Techniques; D016177:Macrophage-1 Antigen / Q000378:metabolism*; D009240:N-Formylmethionine Leucyl-Phenylalanine / Q000494:pharmacology; D009504:Neutrophils / Q000166:cytology / Q000187:drug effects* / Q000502:physiology; D011940:Receptor Aggregation / Q000187:drug effects; D011968:Receptors, Histamine / Q000378:metabolism; D013481:Superoxides / Q000378:metabolism
chemical_list: D003176:Complement C3; D016177:Macrophage-1 Antigen; D011968:Receptors, Histamine; D013481:Superoxides; D009240:N-Formylmethionine Leucyl-Phenylalanine; D006632:Histamine; D006861:Hydrogen Peroxide