Related Experiment Video
Updated: May 10, 2026

Intracellular Refolding Assay
Published on: January 24, 2012
Extracellular heat shock proteins: a new location, a new function.
Antonio De Maio1, Daniel Vazquez
1*Center for Investigations of Health and Education Disparities; †Division of Trauma, Surgical Critical Care and Burns, Department of Surgery; and ‡Department of Neurosciences, School of Medicine University of California San Diego, La Jolla, California; and §Department of Surgery, South Florida University, Tampa, Florida.
Heat shock proteins (HSPs) are crucial for cellular repair and stress tolerance. Extracellular HSPs act as alarm signals, particularly for the immune system, to manage cellular stress and damage.
Area of Science:
- Cellular Biology
- Stress Response
- Immunology
Background:
- Heat shock proteins (HSPs) are vital for cellular repair and stress tolerance.
- Traditionally, HSPs were believed to function solely within cells.
- Emerging evidence shows HSPs also function extracellularly.
Purpose of the Study:
- To review the release mechanisms of extracellular heat shock proteins (HSPs).
- To explore the diverse roles and relevance of extracellular HSPs.
- To understand the non-chaperone functions of HSPs outside the cell.
Main Methods:
- Review of existing literature on HSPs.
- Analysis of proposed mechanisms for HSP export.
- Discussion of experimental findings on extracellular HSP functions.
Main Results:
- HSPs are exported via non-classical secretory pathways.
- Extracellular HSPs act as alarm signals, especially for immune cells.
- HSPs exist in various extracellular forms (membrane-bound and free).
Conclusions:
- Extracellular HSPs play critical roles beyond intracellular chaperoning.
- HSPs released from cells can prime the immune system to stress.
- Understanding extracellular HSPs is key to managing cellular stress and inflammation.
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