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A survey and analysis of the role of molecular chaperone proteins and imidazole-containing dipeptide-based compounds as molecular escorts into the skin during stress, injury, water structuring and other types of cutaneous pathophysiology

, : A survey and analysis of the role of molecular chaperone proteins and imidazole-containing dipeptide-based compounds as molecular escorts into the skin during stress, injury, water structuring and other types of cutaneous pathophysiology. International Journal of Cosmetic Science 33(1): 1-16

Molecular chaperone, heat shock proteins (HSPs), stabilizes intracellular processes of cells under stress. Little is known about the role of molecular chaperone proteins in the skin pathology, rejuvenation and wound healing, or whether their expression is altered by environmental and physiological stress to the skin or systemic disease. The focus of this study was to examine the role of molecular chaperone proteins in the skin's local response to wounding, skin ageing and a range of skin diseases. Free radicals, one form of insult, induce or contribute to adverse effects on the skin, including erythema, oedema, wrinkling, photoaging, inflammation, autoimmune reactions, hypersensitivity, keratinization abnormalities, preneoplastic lesions and skin cancer. A unified view of the molecular and cellular pathogenesis of the skin age-related pathology conditions has led to the search for molecular and chemical chaperones that can slow, arrest or revert disease progression. Specific alpha-crystallin domains and pharmacological imidazole-containing dipeptide chaperone molecules are now emerging that link our biophysical insights with developed skin therapeutic techniques. In this article, we discuss the molecular nature of the stress signals, the mechanisms that underlie activation of the heat shock response, the role of molecular chaperone proteins as skin protective molecules, and strategies for pharmacologically active chaperone molecules and their imidazole-containing dipeptide inducers as regulators of the skin stress response. We discuss how impairment in protein hydration may cause ultrastructural, mechanical and biochemical changes in structural proteins in the aged skin. We have pioneered the molecular chaperone protein activated therapeutic or cosmetic platform to enable simultaneous analysis of water-binding and structuring characteristics for biology of skin ageing and skin disease-related pathways. This cutting-edge technology has improved the way that proteins hydrate in photoaged skin. The mechanisms of skin diseases, ageing, cellular, and signalling pathways mediated by targeting with molecular chaperone protein(s) in patented formulations with imidazole containing dipeptide (N-acetylcarnosine, carcinine, carnosine) are also discussed within this review.


PMID: 20546050

DOI: 10.1111/j.1468-2494.2010.00601.x

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