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13 - Hsp27 as an Anti-inflammatory Protein

Published online by Cambridge University Press:  10 August 2009

By
Krzysztof Laudanski ,
Asit K. De  and
Carol L. Miller-Graziano
Edited by
Brian Henderson  and
A. Graham Pockley
Krzysztof Laudanski
Affiliation:
Immunobiology & Stress Response Laboratories, University of Rochester Medical Center, Department of Surgery, Rochester, New York, U.S.A.
Asit K. De
Affiliation:
Immunobiology & Stress Response Laboratories, University of Rochester Medical Center, Department of Surgery, Rochester, New York, U.S.A.
Carol L. Miller-Graziano
Affiliation:
Immunobiology & Stress Response Laboratories, University of Rochester Medical Center, Department of Surgery, Rochester, New York, U.S.A.
Brian Henderson
Affiliation:
University College London
A. Graham Pockley
Affiliation:
University of Sheffield
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Summary

Introduction

As discussed in other chapters in this volume, heat shock proteins are traditionally viewed as protein chaperones rather than immunomodulators [1–3]. However, recent data suggest that heat shock proteins might also be ancestral danger signals which activate adaptive and innate immune responses [3]. The majority of studies examining the immunomodulatory activities of heat shock proteins have focused on the large heat shock proteins, Hsp60, Hsp70 and gp96, and these proteins have been shown to stimulate the innate immune system via binding to a variety of cellular receptors, particularly on monocytes, and to play an important role in health and disease [1–6].

This chapter focuses on the small heat shock protein, Hsp27, which, although shown to have some role in resistance to chemotherapeutic drugs, cytokine-induced cytotoxicity and to have been described as a prognostic marker in serum of breast cancer patients, has not been well characterised as an immunomodulator [7–13]. Hsp27 has been reported as present in increased amounts in the serum of patients with several human diseases, as well as being necessary for activation of the signal transduction pathway leading to monocyte production of the anti-inflammatory and immunoinhibitory cytokine IL-10 [1–3, 14]. These data led to our interest in investigating the possible immunomodulatory activity of Hsp27 on different human monocyte functions, which are pivotal in both the development of inflammatory responses as well as the triggering of lymphocyte-specific immunity.

Type
Chapter
Information
Molecular Chaperones and Cell Signalling , pp. 220 - 233
Publisher: Cambridge University Press
Print publication year: 2005

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References

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  • Hsp27 as an Anti-inflammatory Protein
    • By Krzysztof Laudanski, Immunobiology & Stress Response Laboratories, University of Rochester Medical Center, Department of Surgery, Rochester, New York, U.S.A., Asit K. De, Immunobiology & Stress Response Laboratories, University of Rochester Medical Center, Department of Surgery, Rochester, New York, U.S.A., Carol L. Miller-Graziano, Immunobiology & Stress Response Laboratories, University of Rochester Medical Center, Department of Surgery, Rochester, New York, U.S.A.
  • Edited by Brian Henderson, University College London, A. Graham Pockley, University of Sheffield
  • Book: Molecular Chaperones and Cell Signalling
  • Online publication: 10 August 2009
  • Chapter DOI: https://doi.org/10.1017/CBO9780511546310.014
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To save content items to your account, please confirm that you agree to abide by our usage policies. If this is the first time you use this feature, you will be asked to authorise Cambridge Core to connect with your account. Find out more about saving content to Dropbox.

  • Hsp27 as an Anti-inflammatory Protein
    • By Krzysztof Laudanski, Immunobiology & Stress Response Laboratories, University of Rochester Medical Center, Department of Surgery, Rochester, New York, U.S.A., Asit K. De, Immunobiology & Stress Response Laboratories, University of Rochester Medical Center, Department of Surgery, Rochester, New York, U.S.A., Carol L. Miller-Graziano, Immunobiology & Stress Response Laboratories, University of Rochester Medical Center, Department of Surgery, Rochester, New York, U.S.A.
  • Edited by Brian Henderson, University College London, A. Graham Pockley, University of Sheffield
  • Book: Molecular Chaperones and Cell Signalling
  • Online publication: 10 August 2009
  • Chapter DOI: https://doi.org/10.1017/CBO9780511546310.014
Available formats
×

Save book to Google Drive

To save content items to your account, please confirm that you agree to abide by our usage policies. If this is the first time you use this feature, you will be asked to authorise Cambridge Core to connect with your account. Find out more about saving content to Google Drive.

  • Hsp27 as an Anti-inflammatory Protein
    • By Krzysztof Laudanski, Immunobiology & Stress Response Laboratories, University of Rochester Medical Center, Department of Surgery, Rochester, New York, U.S.A., Asit K. De, Immunobiology & Stress Response Laboratories, University of Rochester Medical Center, Department of Surgery, Rochester, New York, U.S.A., Carol L. Miller-Graziano, Immunobiology & Stress Response Laboratories, University of Rochester Medical Center, Department of Surgery, Rochester, New York, U.S.A.
  • Edited by Brian Henderson, University College London, A. Graham Pockley, University of Sheffield
  • Book: Molecular Chaperones and Cell Signalling
  • Online publication: 10 August 2009
  • Chapter DOI: https://doi.org/10.1017/CBO9780511546310.014
Available formats
×