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      Heat Shock Proteins in the Human Eye

      review-article
      Author(s): , *
      Publication date (Electronic):
      Journal: International Journal of Proteomics
      Publisher: Hindawi Publishing Corporation

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          Abstract

          Heat shock proteins (Hsps) are believed to primarily protect and maintain cell viability under stressful conditions such as those occurring during thermal and oxidative challenges chiefly by refolding and stabilizing proteins. Hsps are found throughout the various tissues of the eye where they are thought to confer protection from disease states such as cataract, glaucoma, and cancer. This minireview summarizes the placement, properties, and roles of Hsps in the eye and aims to provide a better comprehension of their function and involvement in ocular disease pathogenesis.

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          Regulation of aging and age-related disease by DAF-16 and heat-shock factor.

          A.-L. Hsu (2003)
          The Caenorhabditis elegans transcription factor HSF-1, which regulates the heat-shock response, also influences aging. Reducing hsf-1 activity accelerates tissue aging and shortens life-span, and we show that hsf-1 overexpression extends lifespan. We find that HSF-1, like the transcription factor DAF-16, is required for daf-2-insulin/IGF-1 receptor mutations to extend life-span. Our findings suggest this is because HSF-1 and DAF-16 together activate expression of specific genes, including genes encoding small heat-shock proteins, which in turn promote longevity. The small heat-shock proteins also delay the onset of polyglutamine-expansion protein aggregation, suggesting that these proteins couple the normal aging process to this type of age-related disease.
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            Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications.

            Daniel Ciocca, Stuart K. Calderwood (2005)
            Heat shock proteins (Hsps) are overexpressed in a wide range of human cancers and are implicated in tumor cell proliferation, differentiation, invasion, metastasis, death, and recognition by the immune system. We review the current status of the role of Hsp expression in cancer with special emphasis on the clinical setting. Although Hsp levels are not informative at the diagnostic level, they are useful biomarkers for carcinogenesis in some tissues and signal the degree of differentiation and the aggressiveness of some cancers. In addition, the circulating levels of Hsp and anti-Hsp antibodies in cancer patients may be useful in tumor diagnosis. Furthermore, several Hsp are implicated with the prognosis of specific cancers, most notably Hsp27, whose expression is associated with poor prognosis in gastric, liver, and prostate carcinoma, and osteosarcomas, and Hsp70, which is correlated with poor prognosis in breast, endometrial, uterine cervical, and bladder carcinomas. Increased Hsp expression may also predict the response to some anticancer treatments. For example, Hsp27 and Hsp70 are implicated in resistance to chemotherapy in breast cancer, Hsp27 predicts a poor response to chemotherapy in leukemia patients, whereas Hsp70 expression predicts a better response to chemotherapy in osteosarcomas. Implication of Hsp in tumor progression and response to therapy has led to its successful targeting in therapy by 2 main strategies, including: (1) pharmacological modification of Hsp expression or molecular chaperone activity and (2) use of Hsps in anticancer vaccines, exploiting their ability to act as immunological adjuvants. In conclusion, the present times are of importance for the field of Hsps in cancer, with great contributions to both basic and clinical cancer research.
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              Heat shock transcription factors: structure and regulation.

              C. Wu (1995)
              Organisms respond to elevated temperatures and to chemical and physiological stresses by an increase in the synthesis of heat shock proteins. The regulation of heat shock gene expression in eukaryotes is mediated by the conserved heat shock transcription factor (HSF). HSF is present in a latent state under normal conditions; it is activated upon heat stress by induction of trimerization and high-affinity binding to DNA and by exposure of domains for transcriptional activity. Analysis of HSF cDNA clones from many species has defined structural and regulatory regions responsible for the inducible activities. The heat stress signal is thought to be transduced to HSF by changes in the physical environment, in the activity of HSF-modifying enzymes, or by changes in the intracellular level of heat shock proteins.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Int J Proteomics
                Journal ID (publisher-id): IJPRO
                Title: International Journal of Proteomics
                Publisher: Hindawi Publishing Corporation
                ISSN (Print): 2090-2166
                ISSN (Electronic): 2090-2174
                Publication date (Print): 2010
                Publication date (Electronic): 2 March 2011
                Volume: 2010
                Electronic Location Identifier: 479571
                Affiliations
                Department of Ophthalmology, Aalborg Hospital, Aarhus University Hospital, Hobrovej 18-22, 9100 Aalborg, Denmark
                Author notes
                *Henrik Vorum: hv@ 123456dadlnet.dk

                Academic Editor: Jen-Fu Chiu

                Article
                DOI: 10.1155/2010/479571
                PMC ID: 3200129
                PubMed ID: 22084677
                SO-VID: 8b1e191b-ecab-4be5-8232-86b8c00c5641
                Copyright © Copyright © 2010 L. Urbak and H. Vorum.
                License:

                This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                Date received : 1 July 2010
                Date revision received : 11 November 2010
                Date accepted : 17 December 2010
                Categories
                Subject: Review Article

                ScienceOpen disciplines: Molecular biology
                Data availability:
                ScienceOpen disciplines: Molecular biology

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