Priming mechanisms and induction of heat shock proteins in human polymorphonuclear granulocytes induced by eicosanoids and cytokines.
Priming of human polymorphonuclear granulocytes (PMNs) with cytokines (IL-3, IL-6, TNF-alpha) followed by a subsequent stimulation (FMLP) led to an enhanced polymerization of actin and GTPase-activity which correlated to a loss of ras immunoreactivity and an increased expression of Rab proteins. Furthermore TNF-alpha and 12-HETE induced the heat shock proteins (hsp 70 family) in PMNs as was demonstrated by metabolic radiolabeling and Western blotting (anti-hsp 72). This activation of the stress response exerted a protective function towards a subsequent lytic attack by a bacterial cytolysin (leukocidin).
König
W
W
Lehrstuhl für Medizinische Mikrobiologie und Immunologie, AG Infektabwehrmechanismen, Ruhr-Universität Bochum, FRG.
Köller
M
M
Brom
J
J
D019377:12-Hydroxy-5,8,10,14-eicosatetraenoic Acid; D000199:Actins / Q000378:metabolism; D015153:Blotting, Western; D016207:Cytokines / Q000494:pharmacology*; D015777:Eicosanoids / Q000494:pharmacology*; D020558:GTP Phosphohydrolases / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000096:biosynthesis*; D006801:Humans; D006893:Hydroxyeicosatetraenoic Acids / Q000494:pharmacology; D007377:Interleukin-3 / Q000494:pharmacology; D015850:Interleukin-6 / Q000494:pharmacology; D009240:N-Formylmethionine Leucyl-Phenylalanine / Q000494:pharmacology; D009504:Neutrophils / Q000187:drug effects / Q000378:metabolism*; D014409:Tumor Necrosis Factor-alpha / Q000494:pharmacology
D000199:Actins; D016207:Cytokines; D015777:Eicosanoids; D006360:Heat-Shock Proteins; D006893:Hydroxyeicosatetraenoic Acids; D007377:Interleukin-3; D015850:Interleukin-6; D014409:Tumor Necrosis Factor-alpha; D009240:N-Formylmethionine Leucyl-Phenylalanine; D019377:12-Hydroxy-5,8,10,14-eicosatetraenoic Acid; D020558:GTP Phosphohydrolases