12 February 2009 HSP70 inhibits Bax translocation during Photofrin-PDT apoptosis
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Abstract
Apoptosis is an important cellular event that plays a key role in therapy of many diseases. The mechanisms of the initiation and regulation of photodynamic therapy (PDT) -induced apoptosis is complex. Some PDT-associated apoptosis pathways involved plasma membrane death receptors, mitochondria, lysosomes and endoplasmic reticulum (ER). Our previous study found that Photofrin were localized primarily in mitochondria, the primary targets of Photofrin-PDT. The key role of Bax in the mitochondrion-mediated apoptosis has been demonstrated in many systems. In order to determine the role of Bax in the mitochondrion-mediated apoptosis induced by Photofrin-PDT, we used the CFP/GFP-Bax plasmid to monitor the dynamics of Bax activation and translocation after PDT treatment. With laser scanning confocal microscopy, we found that PDT induced Bax translocation from the cytosol to mitochondria; however, with cells over-expressing YFP-HSP70 plasmids, Bax translocation was not detected. Thus, for Photofrin-PDT, Bax activation and translocation were inhibited by HSP70, not influence the cell death.
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Feifan Zhou, Wei R. Chen, Sheng Song, "HSP70 inhibits Bax translocation during Photofrin-PDT apoptosis", Proc. SPIE 7178, Biophotonics and Immune Responses IV, 71780D (12 February 2009); doi: 10.1117/12.808111; https://doi.org/10.1117/12.808111
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