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      Heat shock protein 70 expression induced by diode laser irradiation on choroid-retinal endothelial cells in vitro

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      Molecular Vision
      Molecular Vision

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          Abstract

          Purpose

          To investigate the biologic effect of an 810 nm diode laser on the induction of heat shock protein 70 (Hsp70) in choroid-retinal endothelial cells in vitro.

          Methods

          Cultured rhesus macaque choroid-retinal endothelial cells (RF/6A) were irradiated using an 810 nm diode laser (spot size, 10 mm; duration, 60 s; power, 400–1,500 mW). Cell viability was assessed by annexin V- fluorescein isothiocyanate (FITC) and propidium iodide flow cytometric assay. Hsp70 expression was determined by western blot at 6, 12, 18, 24, and 48 h following laser exposure. Intracellular distribution of Hsp70 was examined by immunofluorescence staining.

          Results

          The laser-induced cell injury threshold was found to be at a power of 1,100 mW power (fluence, 84.08 J/cm 2), above which there was significant cell death. Under this power, Hsp70 expression elevated obviously and was stronger at 600–1,000 mW power settings (fluences, 45.86–76.43 J/cm 2). The expression of Hsp70 peaked at 12–18 h postirradiation, and returned to baseline by 48 h. Immunofluorescence staining indicated the induced Hsp70 expression in both the cytoplasm and the nucleus.

          Conclusions

          Subthreshold 810 nm diode laser exposure can induce Hsp70 hyperexpression from 12 to 18 h postirradiation in cultured choroid-retinal endothelial cells without obvious cell death. The results could be useful for investigating and designing more effective laser therapies.

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          Most cited references25

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          Heat shock proteins as emerging therapeutic targets.

          Chaperones (stress proteins) are essential proteins to help the formation and maintenance of the proper conformation of other proteins and to promote cell survival after a large variety of environmental stresses. Therefore, normal chaperone function is a key factor for endogenous stress adaptation of several tissues. However, altered chaperone function has been associated with the development of several diseases; therefore, modulators of chaperone activities became a new and emerging field of drug development. Inhibition of the 90 kDa heat shock protein (Hsp)90 recently emerged as a very promising tool to combat various forms of cancer. On the other hand, the induction of the 70 kDa Hsp70 has been proved to be an efficient help in the recovery from a large number of diseases, such as, for example, ischemic heart disease, diabetes and neurodegeneration. Development of membrane-interacting drugs to modify specific membrane domains, thereby modulating heat shock response, may be of considerable therapeutic benefit as well. In this review, we give an overview of the therapeutic approaches and list some of the key questions of drug development in this novel and promising therapeutic approach.
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            Antiapoptotic and anti-inflammatory mechanisms of heat-shock protein protection.

            We and others have previously shown that heat-shock proteins (HSPs) are involved in protecting the brain from a variety of insults including stroke, epilepsy, and other related insults. While the mechanism of this protection has largely been thought to be due to their chaperone functions (i.e., preventing abnormal protein folding or aggregation), recent work has shown that HSPs may also directly interfere with other cell death pathways such as apoptosis and inflammation. Using models of cerebral ischemic and ischemia-like injury, we overexpressed the 70-kDa heat-shock protein (HSP70) using gene transfer or by studying a transgenic mouse model. HSP70 protected neurons and astrocytes from experimental stroke and stroke-like insults. HSP70 transgenic mice also had better neurological scores following experimental stroke compared to their wild-type littermates. Overexpressing HSP70 was associated with less apoptotic cell death and increased expression of the antiapoptotic protein, Bcl-2. Furthermore, HSP70 suppressed microglial/monocyte activation following experimental stroke. HSP70 overexpression also led to the reduction of matrix metalloproteinases. We suggest that HSPs are capable of protecting brain cells from lethal insults through a variety of mechanisms and should be explored as a potential therapy against stroke and other neurodegenerative diseases.
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              The role of heat shock proteins Hsp70 and Hsp27 in cellular protection of the central nervous system.

              Heat shock proteins (Hsps) are highly conserved and under physiological conditions act as molecular chaperones and/or have anti-apoptotic activities. Expression in the brain of two heat shock proteins, the70 kDa Hsp (Hsp70) and the 27 kDa Hsp (Hsp27), is notable because both proteins are highly inducible in glial cells and neurons following a wide range of noxious stimuli including ischemia, epileptic seizure and hyperthermia. In the central nervous system, constitutive expression of Hsp27 is limited to many (but not all) sensory and motor neurons of the brain stem and spinal cord, while there is little or no constitutive expression of Hsp70. However, inducible expression of both Hsp70 and Hsp27 is present in many areas of the brain and retina and is associated with cellular resistance to a variety of insults. The potential for manipulating the expression levels of Hsps for therapeutic advantage in neurodegenerative diseases such as Alzheimer's disease, stroke and glaucoma will be explored.
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                Author and article information

                Journal
                Mol Vis
                Mol. Vis
                MV
                Molecular Vision
                Molecular Vision
                1090-0535
                2012
                21 September 2012
                : 18
                : 2380-2387
                Affiliations
                [1]Department of Ophthalmology, Ruijin Hospital, School of Medicine, Shanghai Jiaotong University, Shanghai, China
                Author notes
                Correspondence to: Ling Wang, Department of Ophthalmology, Ruijin Hospital, School of Medicine, Shanghai Jiaotong University, 197 2nd Ruijin Road, Shanghai, China 200025; Phone: 8613817230313; FAX: 86 21 64374104; email: lwang@ 123456rjeye.com
                Article
                251 2012MOLVIS0130
                3462596
                23049238
                de1078b6-cc82-4d02-8d9e-323d9983b1c5
                Copyright © 2012 Molecular Vision.

                This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                : 14 March 2012
                : 19 September 2012
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                Vision sciences
                Vision sciences

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