Book contents
- Frontmatter
- Contents
- Contributors
- Preface
- SECTION 1 MOLECULAR CHAPERONES AND THE CELL STRESS RESPONSE
- SECTION 2 CHANGING PARADIGMS OF PROTEIN TRAFFICKING AND PROTEIN FUNCTION
- SECTION 3 EXTRACELLULAR BIOLOGY OF MOLECULAR CHAPERONES: MOLECULAR CHAPERONES AS CELL REGULATORS
- SECTION 4 EXTRACELLULAR BIOLOGY OF MOLECULAR CHAPERONES: PHYSIOLOGICAL AND PATHOPHYSIOLOGICAL SIGNALS
- 12 Heat Shock Protein Release and Naturally Occurring Exogenous Heat Shock Proteins
- 13 Hsp27 as an Anti-inflammatory Protein
- 14 BiP, a Negative Regulator Involved in Rheumatoid Arthritis
- SECTION 5 EXTRACELLULAR BIOLOGY OF MOLECULAR CHAPERONES: MOLECULAR CHAPERONES AS THERAPEUTICS
- SECTION 6 EXTRACELLULAR BIOLOGY OF MOLECULAR CHAPERONES: WHAT DOES THE FUTURE HOLD?
- Index
- References
13 - Hsp27 as an Anti-inflammatory Protein
Published online by Cambridge University Press: 10 August 2009
- Frontmatter
- Contents
- Contributors
- Preface
- SECTION 1 MOLECULAR CHAPERONES AND THE CELL STRESS RESPONSE
- SECTION 2 CHANGING PARADIGMS OF PROTEIN TRAFFICKING AND PROTEIN FUNCTION
- SECTION 3 EXTRACELLULAR BIOLOGY OF MOLECULAR CHAPERONES: MOLECULAR CHAPERONES AS CELL REGULATORS
- SECTION 4 EXTRACELLULAR BIOLOGY OF MOLECULAR CHAPERONES: PHYSIOLOGICAL AND PATHOPHYSIOLOGICAL SIGNALS
- 12 Heat Shock Protein Release and Naturally Occurring Exogenous Heat Shock Proteins
- 13 Hsp27 as an Anti-inflammatory Protein
- 14 BiP, a Negative Regulator Involved in Rheumatoid Arthritis
- SECTION 5 EXTRACELLULAR BIOLOGY OF MOLECULAR CHAPERONES: MOLECULAR CHAPERONES AS THERAPEUTICS
- SECTION 6 EXTRACELLULAR BIOLOGY OF MOLECULAR CHAPERONES: WHAT DOES THE FUTURE HOLD?
- Index
- References
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.
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- Chapter
- Information
- Molecular Chaperones and Cell Signalling , pp. 220 - 233Publisher: Cambridge University PressPrint publication year: 2005
References
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