Preferences help
enabled [disable] Abstract
Number of results
2011 | 16 | 89 - 98
Article title


Title variants
Languages of publication
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.
89 - 98
Physical description
  • Chair of Medical Biochemistry, Collegium Medium, Jagiellonian University
  • Institute of Biopolymers and Chemical Fibres
  • Chair of Medical Biochemistry, Collegium Medium, Jagiellonian University,
  • Chair of Medical Biochemistry, Collegium Medium, Jagiellonian University,
  • Institute of Biotechnology and Chemical Fibers
  • 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.
  • Weber G; (1996) Gann Monograph 1, pp. 151-178.
  • 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 proliferationof Ehrlich ascites tumor (EAT) cellsin vitro. In: Jaworska M. (ed.) Progress on Chemistry and Application of Chitin and its Derivatives. Polish Chitin Society, Monograph, vol. XIV, pp. 111-120.
  • Ignacak J., and 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.
  • 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 Chitozan 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. Inter. J. 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.
  • 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.
  • 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 glycolitic activity of human blader cells. Biochim. Biophys. Acta, 1540, pp. 127-136.
  • Ignacak J., Lekka M., Struszczyk H., Laidler P.: (2001) The influence microcrystalline chitosan of various deacetylation degree on energetic metabolism and elasticity of Ehrlich ascitestumour cells. In: Struszczyk ed.) Progress on Chemistry and Application of Chitin and its Derivatives. Polish Chitin Society, Monograph, Vol. VII, pp. 117-123.
  • Ignacak J., Pałka I., Struszczyk H.: (2004) The effect of microcrystalline chitosan on the in vitro proliferation of Ehrlich ascites tumor (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.
  • Struszczyk H.: (1987) Microcrystalline Chitozan. 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 reactions between low- and high-molecular-weight S-nitroso compounds and their tiols by high-performance liquid chromatography and gas chromatography – mass spectrometry. Anal. Biochem. 270, pp. 231-241.
  • Dominick P.K., Cassidy P.B., Roberts J.C.: (2001) A new and versatile method for determination of thiolamines of biological importance. J. Chromatogr. B, 761, pp. 1-12.
  • Bloom K.S., Anderson J.N.: (1978) Fractionation and characterization of chromosomal proteins by the hydroxyapatite dissociationmethod. J. Biol. Chem. 253, pp. 4446-4450.
  • Bucher I., Pfleiderer G.: (1955) Protein 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.
  • Alderton W.K., Cooper C.e., KnowlesR.G.: (2001) Nitric oxide synthasestructure, function and inhibition. Biochem. J., 357, pp. 593-615.
  • Brokes P.S.: (2004) Mitochondrial nitric oxide synthase. Mitochondrion, 3, pp. 187-204.
  • Ghafourifar P., Cadenas E.: (2005) Mitochondrial nitric oxide synthase. Trends Pharmacol. Sci., 26, pp. 190-195.
  • Rahman I., MacNee W.: (2000) Regulation of redox glutathione levels and gene transcription in lung inflammation: therapełtic approaches. Free Rad. Biol. Med. 28, pp. 1405-1420.
  • Lindermayr C., Saalbach G., Durner J.: (2005) Proteomic identification of S-nitrosylated proteins in Arabidopsis. Plant. Physiol. 132, pp. 921-930.
  • Hart C.M.: (1999) Nitric oxide in adult lung disease. CHEST 115, pp. 1407-1417.
  • Bogdan C.: (2001) Nitric oxide and the regulation of gene expression. Trends. Cell Biol. 11, pp. 66-75.
  • Ueno T., Yoshimura T.: (2000) The physiological activity and in vivo distribution of dinitrosyl dithiolato iron complex. Jpn. J. Pharmacol. 82, pp. 95-101.
  • Vanin A.F., Sanina N.A., Serezhenkov V.A., Burbaev D.S., Lozinsky V.I., Aldoshin S.M.: (2007) Dinitrosyl-iron complexes with thiol-containing ligands: spatial and electronic structures. Nitric Oxide 16, pp. 82-93.
  • Jerzmanowski A., Cole R.D.: (1993) Histone H1 in modulation of chromatintranscriptional activity. Acta Biochem. Pol. 40, pp. 17-22.
Document Type
Publication order reference
YADDA identifier
JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.