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ROLE OF CHITOSAN OLIGOMERS IN REGULATION OF EHRLICH ASCITES TUMOR CELLS PROLIFERATION IN VITRO

100%

Ignacak J., Wiśniewska-Wrona M., Pałka I., Zagajewski J., Niekraszewicz A.

Progress on Chemistry and Application of Chitin and its Derivatives

2011

vol. 16

89 - 98

Preliminary studies of proliferation of Ehrlich ascites tumor (EAT) cells and normal mammary gland epithelial cells have demonstrated the process to be inhibited by degradation products of microcrystalline chitosan, i.e. oligomers. Inhibition of proliferation has been also accompanied by a decreased activity of the M2 pyruvate kinase (PK) isoenzyme in nucleoplasm, what may indicate the role of this enzyme in regulation of tumor cell proliferation. Determinations of nitrogen oxide in tumor and normal cells point to a higher level of this endogenous effector in normal cells. An increase of nitrogen oxide levels in Ehrlich ascites tumor cells effected by chitosan oligomers may indicate increased nitrosylation, and particularly an increased amount of compounds containing sulfhydryl groups and their participation in regulation of nucleoplasm M2 PK isoenzyme activity. Chitosan oligomers have smaller molecules as compared to microcrystalline chitosan and for this reason appear to be more effective than the latter in acting upon the negatively charged cell membrane surfaces, thus contributing to proliferation inhibition.

THE EFFECT OF CHITOSAN ON THE SYNTHESIS OF L-S-NITROSOCYSTEINE THAT PARTICIPATES IN THE REGULATION OF THE M2 PYRUVATE KINASE ISOENZYME ACTIVITY ASSOCIATED WITH EHRLICH ASCITES CELLS PROLIFERATION IN VITRO

88%

Ignacak J., Zagajewski J., Pałka I., Wiśniewska-Wrona M., Niekraszewicz A.

Progress on Chemistry and Application of Chitin and its Derivatives

2010

vol. 15

149 - 158

L-S-nitrosocysteine formation in EAT tumor cells and normal CRL-1636 cells incubated with microcrystalline chitosan was confirmed by RP-HPLC. The metabolite was identified based on UV-VIS spectra. The formation of L-S-nitrosocysteine in EAT tumor cells contributes to decreasing the level of L-cysteine in these cells. L-cysteine as an effector of the bifunctional M2 isoenzyme of pyruvate kinase (PK) initiates its histone kinase activity, which is responsible for histone H1 phosphorylation. A decrease of L-cysteine level in EAT tumor cells contributes to lack of histone H1 phosphorylation by the M2 PK isoenzyme and by the same token to inhibition of EAT cell proliferation.

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2 Progress on Chemistry and Application of Chitin and its Derivatives

1 2011

1 2010

2 Ignacak J.

2 Niekraszewicz A.

2 Pałka I.

2 Wiśniewska-Wrona M.

2 Zagajewski J.

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ROLE OF CHITOSAN OLIGOMERS IN REGULATION OF EHRLICH ASCITES TUMOR CELLS PROLIFERATION IN VITRO

THE EFFECT OF CHITOSAN ON THE SYNTHESIS OF L-S-NITROSOCYSTEINE THAT PARTICIPATES IN THE REGULATION OF THE M2 PYRUVATE KINASE ISOENZYME ACTIVITY ASSOCIATED WITH EHRLICH ASCITES CELLS PROLIFERATION IN VITRO