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- W1538642904 abstract "The mechanisms of photoinactivation of NHIK 3025 cells in culture sensitized by tetrasulfonated phenylporphines (TPPS<SUB>4</SUB>) are described). Ultracentrifugation studies on postnuclear supernatants indicated that the intracellular distribution of TPPS<SUB>4</SUB> resembles that of (beta) -N-acetyl-D-glucosaminidase ((beta) -AGA), a lysosomal marker enzyme, and that the cytosolic content of TPPS<SUB>4</SUB> is below the detection limit of the ultracentrifugation method. Upon light exposure more than 90% of TPPS<SUB>4</SUB> was lost from the lysosomal fractions, due to lysosomal rupture. The content of TPPS<SUB>4</SUB> in the postnuclear supernatants was reduced by 30 - 40% upon exposure to light. This is most likely due to binding of TPPS<SUB>4</SUB> to the nuclei, which were removed from the cell extracts before ultracentrifugation, after photochemical treatment. The unpolymerized form of tubulin seems to be an important target for the photochemical inactivation of NHIK 3025 cells. Since TPPS<SUB>4</SUB> is mainly localized in lysosomes it was assumed that a dose of light disrupting a substantial number of lysosomes followed by microtubule depolymerization by nocodazole would enhance the sensitivity of the cells to photoinactivation. This was confirmed by using a colony-forming assay. The increased phototoxic effect exerted by such a treatment regime could be explained by an enhanced sensitivity of tubulin to light. Another cytosolic constituent, lactate dehydrogenase, was not photoinactivated by TPPS<SUB>4</SUB> and light." @default.
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- W1538642904 date "1995-01-01" @default.
- W1538642904 modified "2023-10-09" @default.
- W1538642904 title "Primary targets in photochemical inactivation of cells in culture" @default.
- W1538642904 doi "https://doi.org/10.1117/12.199143" @default.
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