Heat shock protein 70 is a potent activator of the human complement system.
Cell Stress Chaperones
; 7(1): 17-22, 2002 Jan.
Article
em En
| MEDLINE
| ID: mdl-11892984
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 a chaperone and cytokine, inducing potent proinflammatory response in human monocytes, provided support for the hypothesis that extracellular Hsp is a messenger of stress. Our previous work focused on the complement-activating ability of human Hsp60. We demonstrated that Hsp60 complexed with specific antibodies induces a strong classical pathway (CP) activation. Here, we show that another chaperone molecule also possesses complement-activating ability. Solid-phase enzyme-linked immunosorbent assay was applied for the experiments. Human Hsp70 activated the CP independently of antibodies. No complement activation was found in the case of human Hsp90. Our data further support the hypothesis that chaperones may messenger stress to other cells. Complement-like molecules and primitive immune cells appeared together early in evolution. A joint action of these arms of innate immunity in response to free chaperones, the most abundant cellular proteins displaying a stress signal, may further strengthen the effectiveness of immune reactions.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Proteínas do Sistema Complemento
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Via Clássica do Complemento
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Proteínas de Choque Térmico HSP70
Limite:
Female
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Humans
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Male
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Middle aged
Idioma:
En
Ano de publicação:
2002
Tipo de documento:
Article