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Cytokine function of heat shock proteins
1Research Service, Veterans Affairs Medical Center, Washington, DC 20422, USA. min-fu.tsan2@med.va.gov
American Journal of Physiology. Cell Physiology
|March 6, 2004
Summary
Heat shock proteins (HSPs) were thought to activate the innate immune system. However, recent evidence suggests contaminants like lipopolysaccharide (LPS) may cause these effects, necessitating further investigation.
Area of Science:
- Immunology
- Molecular Biology
Background:
- Heat shock proteins (HSPs) like Hsp60, Hsp70, Hsp90, and gp96 have been implicated as potent activators of the innate immune system.
- These proteins were reported to induce proinflammatory cytokine production and dendritic cell maturation, mimicking effects of lipopolysaccharide (LPS).
Purpose of the Study:
- To critically evaluate whether the reported cytokine-inducing effects of HSPs are intrinsic to the proteins or due to contaminating molecules.
- To determine the necessity of using highly purified HSP preparations for accurate research.
Main Methods:
- Review of recent evidence suggesting contamination in HSP preparations.
- Analysis of potential reasons for previous misattribution of cytokine effects to HSPs, including inadequate purification and heat sensitivity of LPS.
- Emphasis on the need for rigorous assessment of HSP purity.
Main Results:
- Recent evidence challenges the direct cytokine-inducing role of HSPs.
- Contaminating lipopolysaccharide (LPS) and associated molecules are proposed as the actual cause of previously observed immune responses.
- Failure to use highly purified HSPs and account for LPS heat sensitivity contributed to misinterpretation.
Conclusions:
- The purported cytokine-activating effects of HSPs may be attributable to LPS contamination.
- Further research must utilize highly purified HSPs to definitively ascertain their role in innate immunity.
- Clarifying this distinction is crucial before exploring therapeutic applications of HSPs.