Stress protein expression kinetics.
In all organisms there is an elevated synthesis of a select family of "stress proteins" in response to a broad array of environmentally driven stress vectors including elevated or depressed temperature, changes in pH, treatment with many classes of chemicals, ischemia, desiccation, and UV irradiation. The presence of stress proteins, often termed heat shock proteins (HSPs), has been recognized for more than four decades, and there is an extensive literature that addresses the structure and properties of HSPs, their function in normal and injured cells and tissues, and the molecular mechanisms of HSP expression in response to stress. Owing to this substantial aggregate of research, there is a growing appreciation of the potential for manipulating the magnitude and timing of elevated HSP expression to achieve targeted therapeutic objectives. The successful realization of this potential requires an understanding of the kinetics of the HSP expression process in response to sublethal stress regimens along with the ability to model the governing events in the process to design practical protocols that could be applied in therapeutic settings. Significant progress has been made in recent years in defining and developing capabilities in these two areas.
Diller
Kenneth R
KR
Department of Biomedical Engineering, University of Texas at Austin, Austin, Texas 78712-1084, USA. kdiller@mail.utexas.edu
D000222:Adaptation, Physiological / Q000502:physiology*; D000818:Animals; D005786:Gene Expression Regulation / Q000502:physiology*; D006360:Heat-Shock Proteins / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D008657:Metabolic Clearance Rate; D008954:Models, Biological; D018384:Oxidative Stress / Q000502:physiology*
D006360:Heat-Shock Proteins