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2010 | 15 | 149 - 158
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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.

149 - 158
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  • Chair of Medical Biochemistry, Collegium Medium, Jagiellonian University
  • Chair of Medical Biochemistry, Collegium Medium, Jagiellonian University
  • Institute of Biopolymer and Chemical Fibres
  • Institute of Biotechnology and Chemical Fibers
  • Struszczyk H.; (ed.); (1995) New Aspects of Chemistry and Application of Chitin and its Deriwatives. Pol. Chitin. Soc., Łódź.
  • Knapczyk J., Krówczyński L.; (1987) Utylisation of chitin and chitosan properties in drug formulaction. Bull. Sea. Fisheries Inst. 18, pp. 46-47.
  • Nishimura K., Nishimura S., Nishi N., Saiki I., Tokura S., Mizukoshi N., Azuma I.; (1984) Immunological activity of chitin derivatives. Vacine, 2, pp. 93-99.
  • Munday V. K., Cox P. J.; (2000) Compressed xanthan and karaya gum matrices: Hydration, erosion and drug relase mechanism. International Journal of Parmaceutics, 203, pp. 179-192.
  • Nishimura K., Nishimura S., Nishi N., Tone Y., Azuma I.; (1987) Adjuvant activity of chitin derivatives in mice and guinea pigs. Vacine 3, pp. 379-384.
  • Sirica A. E., Woodman R. J.; (1971) Selective aggregation of L 1210 leukemia cells by the polycation chitosan. J. Nat. Cancer. Inst. 47, pp. 377-388.
  • Bakulin A., Kurchenko V., Gavrilenko N., Halavach T., Cherviakowski E.; (2009) Interaction of chitosan with whey proteins. 15th Workshop, “New aspects on chemistry and application of chitin and its derivatives” Toruń, September pp. 28-30.
  • Lai W.F., Lin M.Ch.M.; (2009) Nucleic acid delivery with chitosan and its derivatives. J.Control. Release, 134, pp. 158-168.
  • Lekka M., Laidler P., Ignacak J., Łabędź M., Lekki J., Struszczyk H., Stachura Z., Hrynkiewicz A. Z.; (2001) The effect of chitosan on stiffness and glycolitc activity of human bladder cells. Biochim. Biophys. Acta, 1540, pp. 127-136.
  • Ignacak J., Lekka M., Struszczyk H., Laidler P.; (2001) The influence mikrocrystalline chitosan of various deacetylation degree on energetic metabolism and elasticity of Ehrlich ascites tumourcells. In: Struszczyk H (ed.) Progress on Chemistry and Application of Chitin and its Derivatives. Polish Chitin Society, Monograph, vol.VII, pp. 117-123.
  • Weber G.; (1996) Gann Monograph 1, pp. 151-178.
  • Wojtczak L., Teplova V. V., Bogucka K., Czyż A., Makowska A., Więckowski M. R., Duszyński J., Evtodienko Yu. V.; (1999) Effect of glucose and deoxyglucose on the redistribution of calcium in Ehrlich ascites tumour and Zajdela hepatoma cells and its consequences for mitochondrial energetics. Further arguments for the role of Ca2+ in the mehanism of the crabtree effect. Eur. J. Biochem. 263, pp. 495-501.
  • Gumińska M., Ignacak J., Wójcik E.; (1996) In vitro inhibitory effect of chitosan and its degradation products on energy metabolism in Ehrlich ascites tumour cells (EAT). Pol. J. Parmacol. 48, pp. 495-501.
  • Gumińska M., Stachurska M. B., Ignacak J.; (1988) Pyruvate kinase isoenzymes in chromatin extracts of Ehrlich ascites tumour, Morris hepatoma 7777 and normal mouse and rat livers. Biochim. Biophys. Acta, 966, pp. 207-213.
  • Ignacak J., Dulińska J., Pałka I., Wrona-Wiśniewska M., Niekraszewicz A.; (2009) The effect of microcrystalline chitosan on the activity of pyruvate kinase M2 isoenzyme involved in regulating proliferation of Ehrlich ascites tumor (EAT) cells in vitro. In: Jaworska M. (ed.) Progress on Chemistry and Application of Chitin and its Derivatives. Polish Chitin Society, Monograph, vol.XV, pp. 111-120.
  • Ignacak J., Stachurska M. B.; (2003) The dual activity of pyruvate kinase type M2 from chromatin extracts of neoplastic cells. Comp. Biochem. Phys. 134, pp. 425-433.
  • Lind D.S.; (2004) Arginine and cancer. J.Nutr. 134, pp. 2837S-2841S.
  • Porębska Z., Nyckowski P., Skwarek A., Mielczarek M., Barańczyk-Kuźma A.; (2002) Arginase a marker of carcogenesis. II. Monitoring of patients after resection of colorectal liver metastases. Pol. Merkuriusz Lek. 13, pp. 286-288.
  • Xie K., G. S., Dong Z., Juang S. H. Gutman M., Xie Q. W., Nathan C., Fidler I. J.; (1995) Transfection with inducible nitric oxide synthase gene supresses tumorogenicity and abrogates metastasis by K-1735 murine melanoma cells. J. Exp. Med. 181, pp. 1333-1343.
  • Ignacak J., Pałka I., Struszczyk H.; (2004) The effect of microcrystalline chitosan on the in vitro proliferation of Ehrlich ascites tumour (EAT) cells and mouse mammary epithelium. In. Struszczyk H. ed. Progress on Chemistry and Application of Chitin and its Derivatives. Polish Chitin Society, Monograph, vol. X, pp. 114-119.
  • Adam C., Garcia-Rio L., Ribeiro L.; (2005) Nitroso group transfer in S-nitrosocysteine: evidence of a new decomposition pathway for nitrosothiols. J. Org. Chem. 70, pp. 6353-6361.
  • Ryzhov V., Lam A. K. Y., O’Hair R. A. J.; (2009) Gas-phase fragmentation of long-lived cysteine radical cations via NO loss from protonated S-nitrosocysteine. J. Am. Soc. Mass. Spectrom. 20, pp. 985-995.
  • Struszczyk H.; (1987) Microcrystalline chitosan. I. Properties and preparation. J. Appl. Polym. Sci. 33, pp. 177-187.
  • Tsikas D., Gutzki F. M., Rossan S., Bauer H., Neumann Ch., Dockendorff K., Sandmann J., Frolich J. C.; (1997) Measurement of nitrite and nitrate in biological fluids by gas chromatography – mass spectrometry and by the Griess assay: problems with the Griess assay – solutions by gas chromatography – mass spectrometry. Anal. Biochem. 244, pp. 208-220.
  • Tsikas D., Sandmann J., Rossa S., Gutzki F. M., Frolich J. C.; (1999) Investigations of S- transnitrosylation reactions between low- and high-molecular-weight S-nitroso compounds and their thiols by high-performance liquid chromatography and gas chromatography – mass spectrometry. Anal. Biochem. 270, pp. 231-241.
  • Wróbel M., Lewandowska I., Bronowicka-Adamska P., Paszewski A.; (2009) The level of sulfane sulfur in the fungus Aspergillus nidulans wild type and mutant stratus. Amino Acids, 37, pp. 565-571.
  • Bloom K. S., Anderson J.N.; (1978) Fractionation and characterization of chromosomal proteins by the hydroxyapatite dissociation method. J. Biol. Chem. 253, pp. 4446-4450.
  • Bucher I., Pfleiderer G.; (1955) Pyruvate kinase from muscle. In: Collowick S P, Kaplan N D (eds), Methods in Enzymology, Acad. Press. New York 1, pp. 435-440.
  • Lowry O. H., Rosebrouggh N. J., Farr A. L., Randal R .J.; (1951) Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, pp. 265-273.
  • Ignacak J., Dulińska-Litewka J., Pałka I., Struszczyk H.; (2006) The effect of highly deacetylated microcrystalline chitosan on the pyruvate kinase gene expression in normal mouse mammary epithelial cells and Ehrlich ascites tumor (EAT) cells. In: Jaworska M. (ed.) Progress on Chemistry and Application of Chitin and its Derivatives. Polish Chitin Society, Monograph, vol. XI, pp. 137-143.
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