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Proceedings Paper

Targeting cytochrome C oxidase in mitochondria with Pt(II)-porphyrins for photodynamic therapy
Author(s): Michael Börsch
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Paper Abstract

Mitochondria are the power house of living cells, where the synthesis of the chemical "energy currency" adenosine triphosphate (ATP) occurs. Oxidative phosphorylation by a series of membrane protein complexes I to IV, that is, the electron transport chain, is the source of the electrochemical potential difference or proton motive force (PMF) of protons across the inner mitochondrial membrane. The PMF is required for ATP production by complex V of the electron transport chain, i.e. by FoF1-ATP synthase. Destroying cytochrome C oxidase (COX; complex IV) in Photodynamic Therapy (PDT) is achieved by the cationic photosensitizer Pt(II)-TMPyP. Electron microscopy revealed the disruption of the mitochondrial christae as a primary step of PDT. Time resolved phosphorescence measurements identified COX as the binding site for Pt(II)-TMPyP in living HeLa cells. As this photosensitizer competed with cytochrome C in binding to COX, destruction of COX might not only disturb ATP synthesis but could expedite the release of cytochrome C to the cytosol inducing apoptosis.

Paper Details

Date Published: 2 March 2010
PDF: 11 pages
Proc. SPIE 7551, Optical Methods for Tumor Treatment and Detection: Mechanisms and Techniques in Photodynamic Therapy XIX, 75510G (2 March 2010); doi: 10.1117/12.841284
Show Author Affiliations
Michael Börsch, Univ. Stuttgart (Germany)


Published in SPIE Proceedings Vol. 7551:
Optical Methods for Tumor Treatment and Detection: Mechanisms and Techniques in Photodynamic Therapy XIX
David H. Kessel, Editor(s)

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