title: The functional role of 55- and 75-kDa tumour necrosis factor receptors in human polymorphonuclear cells in vitro.
abstract: The expression and biological role of 55- and 75-kDa tumour necrosis factor-receptors (TNF-RI and TNF-RII) in human polymorphonuclear cells (PMN) in vitro were studied using agonistic rabbit polyclonal anti-TNF-R antibodies. PMN express TNF-RII predominantly, and release the superoxide anion on stimulation by human recombinant lymphotoxin (LT) in vitro. Anti-TNF-RI but not anti-TNF-RII antibody stimulated the superoxide release mimicking LT. Release of the elastase from azurophilic granule of PMN was augmented by LT in vitro. Anti-TNF-RI but not anti-TNF-RII antibody augmented the elastase release. Release of the lactoferrin from the specific granules of PMN was enhanced by LT in vitro. Anti-TNF-RI but not anti-TNF-RII antibody augmented the elastase release. Release of the lactoferrin from the specific granules of PMN was enhanced by LT in vitro. Anti-TNF-RI but not anti-TNF-RII antibody enhanced the lactoferrin release. These antibodies failed to co-stimulate these PMN functions. The adhesiveness of PMN to a plastic plate and the expression of Mac-1 on PMN were upregulated by LT in vitro. Anti-TNF-RI but not anti-TNF-RII antibody upregulated the adhesiveness and Mac-1 expression of PMN mimicking LT. Though anti-TNF-RII antibody by itself did not alter the adhesiveness and marginally suppressed Mac-1 expression, it maintained the adhesiveness and adhesion molecule expression in the presence of anti-TNF-RI antibody. In summary, PMN predominantly express TNF-RII, the signalling of LT (and TNF) in PMN is mediated mainly by TNF-RI, and the adhesion function can be modulated also by TNF-RII when TNF-RI is stimulated.
authors.affiliation: Second Department of Surgery, Ehime University School of Medicine, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Abe
authors.forename: Y
authors.initials: Y
authors.lastname: Osuka
authors.forename: T
authors.initials: T
authors.lastname: Nakata
authors.forename: Y
authors.initials: Y
authors.lastname: Kashu
authors.forename: S
authors.initials: S
authors.lastname: Kimura
mesh_terms: D000906:Antibodies / Q000494:pharmacology; D015703:Antigens, CD / Q000096:biosynthesis / Q000737:chemistry / Q000276:immunology / Q000502:physiology*; D002448:Cell Adhesion / Q000187:drug effects; D002478:Cells, Cultured; D003594:Cytoplasmic Granules / Q000378:metabolism; D006801:Humans; D007781:Lactoferrin / Q000378:metabolism; D019272:Leukocyte Elastase; D008233:Lymphotoxin-alpha / Q000378:metabolism / Q000494:pharmacology; D016177:Macrophage-1 Antigen / Q000096:biosynthesis; D009504:Neutrophils / Q000502:physiology*; D010196:Pancreatic Elastase / Q000378:metabolism; D010969:Plastics; D018124:Receptors, Tumor Necrosis Factor / Q000737:chemistry / Q000276:immunology / Q000502:physiology*; D047888:Receptors, Tumor Necrosis Factor, Type I; D047889:Receptors, Tumor Necrosis Factor, Type II; D011994:Recombinant Proteins / Q000494:pharmacology; D013481:Superoxides / Q000378:metabolism
chemical_list: D000906:Antibodies; D015703:Antigens, CD; D008233:Lymphotoxin-alpha; D016177:Macrophage-1 Antigen; D010969:Plastics; D018124:Receptors, Tumor Necrosis Factor; D047888:Receptors, Tumor Necrosis Factor, Type I; D047889:Receptors, Tumor Necrosis Factor, Type II; D011994:Recombinant Proteins; D013481:Superoxides; D007781:Lactoferrin; D010196:Pancreatic Elastase; D019272:Leukocyte Elastase