作者: Zoltán Prohászka , Mahavir Singh , Kálmán Nagy , Emese Kiss , Gabriella Lakos
DOI: 10.1379/1466-1268(2002)007<0017:HSPIAP>2.0.CO;2
关键词: Classical complement pathway 、 Heat shock protein 、 Immune system 、 HSP60 、 Complement system 、 Biology 、 Chaperone (protein) 、 Hsp90 、 Biochemistry 、 Innate immune system 、 Cell biology
摘要: According to new hypotheses, extracellular heat shock proteins (Hsps) may represent an ancestral danger signal of cellular death or lysis-activating innate immunity. Recent studies demonstrating a dual role for Hsp70 as both chaperone and cytokine, inducing potent proinflammatory response in human monocytes, provided support the hypothesis that Hsp is messenger stress. Our previous work focused on complement-activating ability Hsp60. We demonstrated Hsp60 complexed with specific antibodies induces strong classical pathway (CP) activation. Here, we show another molecule also possesses ability. Solid-phase enzyme-linked immunosorbent assay was applied experiments. Human activated CP independently antibodies. No complement activation found case Hsp90. data further chaperones stress other cells. Complement-like molecules primitive immune cells appeared together early evolution. A joint action these arms immunity free chaperones, most abundant displaying signal, strengthen effectiveness reactions.