Share Email Print

Proceedings Paper

HSP70 inhibits Bax translocation during Photofrin-PDT apoptosis
Format Member Price Non-Member Price
PDF $14.40 $18.00
cover GOOD NEWS! Your organization subscribes to the SPIE Digital Library. You may be able to download this paper for free. Check Access

Paper 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.

Paper Details

Date Published: 12 February 2009
PDF: 8 pages
Proc. SPIE 7178, Biophotonics and Immune Responses IV, 71780D (12 February 2009); doi: 10.1117/12.808111
Show Author Affiliations
Feifan Zhou, South China Normal Univ. (China)
Wei R. Chen, South China Normal Univ. (China)
Univ. of Central Oklahoma (United States)
Sheng Song, South China Normal Univ. (China)

Published in SPIE Proceedings Vol. 7178:
Biophotonics and Immune Responses IV
Wei R. Chen, Editor(s)

© SPIE. Terms of Use
Back to Top