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Neutrophil Membrane Sulfhydryl Groups Are Involved in Stimulated Neutrophil Adherence to Endothelium
Author(s) -
Schwartz Barbara R.,
Harlan John M.
Publication year - 1989
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1002/jlb.45.3.177
Subject(s) - degranulation , neutrophile , endothelium , phorbol , granulocyte , hydrogen peroxide , biochemistry , microbiology and biotechnology , ionophore , biology , chemistry , immunology , in vitro , membrane , enzyme , protein kinase c , endocrinology , receptor
We investigated the role of membrane sulfhydryl groups in adherence of stimulated polymorphonuclear neutrophils to cultured endothelial cells. Treatment of neutrophils with p‐chloromercuriphenyl sulfonate (PCMPS), a slowly penetrating sulfhydryl reagent, inhibited phorbol myristate acetate (PMA)‐ or calcium ionophore A23187‐stimulated adherence to cultured human or bovine endothelial cells. At concentrations which completely blocked PMA‐stimulated adherence, PCMPS did not cause release of lactic dehydrogenase, inhibit PMA‐mediated degranulation or hydrogen peroxide production, or prevent the PMA‐induced increased surface expression of CD11b/CD 18 (Mac‐1). Coincubation with a competing reduced sulfhydryl compound protected neutrophils from inhibition of PMA‐stimulated adherence by PCMPS, whereas coincubation with an oxidized sulfhydryl compound did not. Monobromotrimethylammoniobimane, a nonpenetrating sulfhydryl reagent that is structurally unrelated to PCMPS, also inhibited stimulated neutrophil adherence to endothelium cultures. We conclude that stimulated neutrophil adherence to endothelium involves neutrophil membrane protein sulfhydryl groups.