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8. RELATIONSHIP BETWEEN PHOTODYNAMIC THERAPY AND THE REDOX STATUS OF COMPANION ANIMAL TUMORS.

Author

Szabó, Bernadett, Molnár, P., Vajdovich, P., Szécsényi, Dóra, and Jakus, Judit

Subjects
PHOTOCHEMOTHERAPY, ANIMAL diseases, TUMORS, CANCER treatment, PHOTOSYNTHETIC oxygen evolution, PRESERVATION of organs, tissues, etc., GLUTATHIONE, OLIGOPEPTIDES
Abstract

Photodynamic therapy is a relatively new modality of cancer treatment in human and veterinary medicine. It uses a photosensitizing drug called photosensitizer, which in the presence of oxygen delivers reactive species (singlet oxygen and flee radicals) upon irradiation of the tumor with visible light. In contrast to classical chemotherapy, the original compound (sensitizer or photosensitizer) has a minimal toxic effect on the whole body. Its effect is due to the activation of the accumulated sensitizer in a given tissue by visible light around 630 nm wavelength or above. Excitation by light produces activated oxygen- and nitrogen species, which are able to rapidly kill cells. No harming radiation is involved. The administered compound gets activated only in the illuminated area, mainly killing actively dividing cells. The treatment achieves its selectivity by illuminating only the area affected by the tumor. Apparently, it does not solve the problem of metastasis, but offers many advantages against chemotherapy, radiation or surgery. PDT offers an additional method in treat patients with certain kinds of cancer. Here we present some preliminary data on the application of PDT on companion animals with malignant tumors. We have applied 5-aminolevulinic acid (ALA)-based PDT on cats and dogs with different kinds of tumors, and investigated the effect of treatment on reduction-oxidation parameters of tissue samples taken from the tumors before and after PDT. Results of free radical concentrations measured using Electron Spin Resonance and of reduced glutathione in tumor tissues give a direct correlation with the outcome of PDT. [ABSTRACT FROM AUTHOR]

Published
2008

9. Carboxyl-terminal Domain of p27Kip1Activates CDC2*

Author

Üren, Aykut, Jakus, Judit, de Mora, Jaime Font, Yeudall, Andrew, Santos, Eugenio, Gutkind, Silvio, and Heidaran, Mohammad A.

Abstract

A variant form of p27 was unexpectedly detected in a synchronized culture of NIH3T3 cells treated with serum. The expression levels of this form of p27 which lacked its amino (NH2)-terminal region reached maximum during G2/M phase. Since the appearance of the NH2-terminal truncated form of p27 coincided with increased expression of Cdc2, we hypothesized that p27 may play a role in regulating Cdc2 catalytic activity. To test this hypothesis, wild type p27, as well as the amino-terminal (Np27) and carboxyl-terminal (Cp27), were individually expressed, purified, and examined for their ability to regulate CDC2 kinase activity in vitro. Our data showed that both p27 and Np27 inhibited CDC2 kinase activity. However, in marked contrast, Cp27 enhanced the CDC2 kinase activity. In vitrokinase assays showed that Cp27 and p27 were phosphorylated by CDC2, whereas Np27 was not. In addition, we demonstrated that deletion of the putative CDC2 phosphorylation site in the carboxyl-terminal domain of Cp27 diminished activation of CDC2 kinase activity otherwise stimulated by Cp27. A similar deletion did not have any effect on the inhibitory function of p27. Together these results suggest that the carboxyl-terminal domain of p27 may activate CDC2 kinase activity in vivoduring G2/M and that this effect may be regulated by serine/threonine phosphorylation.

Published
1997
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