The 70-kDa heat shock protein (HSP70) contains three domains: the ATPase N-domain, which hydrolyses ATP, the substrate domain, which binds proteins, and the C-domain that forms the "lid" for the substrate domain. Because of its three-domain structure, HSP70 forms a unified ATPase cycle coupled with the association and the disassociation of the client protein. The "team" of HSP70 cycle regulators includes: HSP40, which delivers clients to HSP70 and stimulates ATP hydrolysis; Hip, which assists HSP70 in retaining the client; and Bag-1 and HspBP1, which accelerate ADP dissociation and the release of the client protein. Therefore, HSP70 cycle is involved in the most import intracellular processes such as protein folding, protein transportation into organelles, and directing old or incorrectly folded proteins for degradation.
The heat shock response and the structure of HSPs have been highly conserved through evolution. Moreover, the heat shock response is elicited by a wide variety of environmental stresses. These evidences indicate that this response is essential for the survival of organisms. Living cells have various defense and repair systems against genotoxic stresses. On the other hand, the molecular chaperone system is considered to be a defense mechanism against proteotoxic stresses at cellular level. Recent finding indicates that molecular chaperones could assist correct folding not only of wild type proteins but also of some mutant proteins. This beneficial function of molecular chaperones might be applicable for the delay of senescence, increase of life span and the fight of inherited diseases caused by protein misfolding.
The function and application of Acetyl Tetrapeptide-22
Acetyl Tetrapeptide-22 is the reaction product of acetic acid and tetrapeptide-22. It increases heat shock protein (HSP70) levels in the skin, which enhances stress tolerance and prevents damage. Therefore, acetyl tetrapeptide-22, as one of the most effective skin regeneration ingredients, helps skin to be more relaxed with a more vital appearance.
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