APPENDIX 1T Heat-Shock Proteins

  1. Zihai Li,
  2. Pramod Srivastava

Published Online: 1 FEB 2004

DOI: 10.1002/0471142735.ima01ts58

Current Protocols in Immunology

Current Protocols in Immunology

How to Cite

Li, Z. and Srivastava, P. 2004. Heat-Shock Proteins. Current Protocols in Immunology. 58:1T:A.1T.1–A.1T.6.

Author Information

  1. University of Connecticut School of Medicine, Farmington, Connecticut

Publication History

  1. Published Online: 1 FEB 2004
  2. Published Print: DEC 2003


Heat-shock proteins (HSPs), or stress proteins, are highly conserved and present in all organisms and in all cells of all organisms. Selected HSPs, also known as chaperones, play crucial roles in folding/unfolding of proteins, assembly of multiprotein complexes, transport/sorting of proteins into correct subcellular compartments, cell-cycle control and signaling, and protection of cells against stress/apoptosis. More recently, HSPs have been implicated in antigen presentation with the role of chaperoning and transferring antigenic peptides to the class I and class II molecules of the major histocompatibility complexes. In addition, extracellular HSPs can stimulate professional antigen-presenting cells of the immune system, such as macrophages and dendritic cells. HSPs constitute a large family of proteins that are often classified based on their molecular weight: hsp10, hsp40, hsp60, hsp70, hsp90, etc. This unit contains a table that lists common HSPs and summarizes their characteristics including (a) name, (b) subcellular localization, (c) known function, (d) chromosome assignment, (e) brief comments, and (f) references.