The Versatile Stress Protein Mortalin as a Chaperone Therapeutic Agent

Authors: Deocaris, Custer C.; Kaul, Sunil C.; Wadhwa, Renu

Source: Protein and Peptide Letters, Volume 16, Number 5, May 2009 , pp. 517-529(13)

Publisher: Bentham Science Publishers

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Abstract:

Age- and stress-induced modulations in chaperone systems result in “chaperono-deficiency” or “chaperonopulence”. Development of modulators, of chaperone function has therefore, become an emerging field in drug development and discovery. This mini-review summarizes (i) the events leading to identification of an Hsp70 family stress chaperone, mortalin, (ii) experimental evidence to its role in old age diseases and cancer, and (iii) proposes it as a chaperonotherapeutic agent. As post-translational modifications and expression changes in mortalin are being explored as a biomarker for cancer, cardiovascular diseases and neurodegeneration, we discuss here how the current tools used in studying mortalin (e.g. antibodies, peptides, ribozymes, antisense and siRNA, recombinant proteins and small molecules etc.) could be creatively applied in a clinical setting to manage stress and to treat various chaperone-based maladies or “chaperonopathies”.





Keywords: Mortalin; aging; cancer; chaperono-therapeutic agent; stress chaperone; upregulation

Document Type: Research Article

DOI: http://dx.doi.org/10.2174/092986609788167770

Publication date: May 1, 2009

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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