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• W2098494251 startingPage "078002" @default.
• W2098494251 abstract "Induction of heat shock protein (Hsp) expression correlates with cytoprotection, reduced tissue damage, and accelerated healing in animal models. Since Hsps are transcriptionally activated in response to stress, they can act as stress indicators in burn injury or surgical procedures that produce heat and thermal change. A fast in vivo readout for induction of Hsp transcription in tissues would allow for the study of these proteins as therapeutic effect mediators and reporters of thermal stress/damage. We used a transgenic reporter mouse in which a luciferase expression is controlled by the regulatory region of the inducible 70 kilodalton (kDa) Hsp as a rapid readout of cellular responses to laser-mediated thermal stress/injury in mouse skin. We assessed the pulse duration dependence of the Hsp70 expression after irradiation with a CO2 laser at 10.6 μm in wavelength over a range of 1000 to 1 ms. Hsp70 induction varied with changes in laser pulse durations and radiant exposures, which defined the ranges at which thermal activation of Hsp70 can be used to protect cells from subsequent stress, and reveals the window of thermal stress that tissues can endure." @default.
• W2098494251 created "2016-06-24" @default.
• W2098494251 creator A5067599166 @default.
• W2098494251 creator A5081671050 @default.
• W2098494251 date "2011-01-01" @default.
• W2098494251 modified "2023-10-18" @default.
• W2098494251 title "Pulse duration determines levels of Hsp70 induction in tissues following laser irradiation" @default.
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• W2098494251 doi "https://doi.org/10.1117/1.3600013" @default.
• W2098494251 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21806294" @default.
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