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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.
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 . 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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