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Lysosomes as photochemical targets

K Berg1, J Moan

  • 1Institute for Cancer Research, Department of Biophysics, Montebello, Oslo, Norway.

International Journal of Cancer
|December 15, 1994
PubMed
Summary
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Photochemical treatment with sulfonated tetraphenyl porphines (TPPSn) inactivates lysosomal enzymes in NHIK 3025 cells. Cell death is not caused by lysosomal disruption, but by enzyme inactivation and cytosolic inhibitors.

Area of Science:

  • Photochemistry
  • Cell Biology
  • Biochemistry

Background:

  • Sulfonated tetraphenyl porphines (TPPSn) are photosensitizers that accumulate in cell lysosomes.
  • Photochemical treatment is a potential cancer therapy, but its cell inactivation mechanisms require elucidation.

Purpose of the Study:

  • To investigate the mechanisms of cell inactivation by photochemical treatment with TPPSn.
  • To examine lysosomal enzyme inactivation and release of lysosomal contents following TPPSn treatment.

Main Methods:

  • NHIK 3025 cells were treated with various TPPSn compounds and light.
  • Lysosomal enzyme (beta-N-acetyl-D-glucosaminidase and cathepsin) activity and release were measured.
  • Cytosolic cathepsin activity and inhibition were assessed.

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Main Results:

  • TPPS4 and light almost completely inactivated lysosomal enzymes without release.
  • TPPS1 and TPPS2a caused partial release of beta-N-acetyl-D-glucosaminidase.
  • Cytosolic factors inhibited cathepsin activity, independent of photochemical treatment.

Conclusions:

  • NHIK 3025 cell inactivation is not primarily due to lysosomal disruption.
  • Photochemical inactivation of lysosomal enzymes and cytosolic cathepsin inhibitors contribute to cell death.
  • Cells can survive partial lysosomal disruption following photochemical treatment.