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    Wyświetlanie 1-4 z 4
    Tytuł:
    Role of chitosan oligomers in regulation of ehrlich ascites tumor cells proliferation in vitro
    Autorzy:
    Ignacak, Jan
    Wiśniewska-Wrona, Maria
    Pałka, Iwona
    Zagajewski, Jacek
    Niekraszewicz, Antoni
    Powiązania:
    https://bibliotekanauki.pl/articles/1035427.pdf
    Data publikacji:
    2011
    Wydawca:
    Sieć Badawcza Łukasiewicz - Polskie Towarzystwo Chitynowe
    Tematy:
    EAT cells proliferation
    L-S-nitrosocysteine.
    chitosan oligomers
    pyruvate kinase M2 isoenzyme
    Opis:
    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.
    Źródło:
    Progress on Chemistry and Application of Chitin and its Derivatives; 2011, 16; 89-98
    1896-5644
    Pojawia się w:
    Progress on Chemistry and Application of Chitin and its Derivatives
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    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
    Autorzy:
    Ignacak, Jan
    Zagajewski, Jacek
    Pałka, Iwona
    Wiśniewska-Wrona, Maria
    Niekraszewicz, Antoni
    Powiązania:
    https://bibliotekanauki.pl/articles/1035527.pdf
    Data publikacji:
    2010
    Wydawca:
    Sieć Badawcza Łukasiewicz - Polskie Towarzystwo Chitynowe
    Tematy:
    L-S-nitrosocysteine
    L-cysteine
    inhibition of EAT cell proliferation
    microcrystalline chitosan
    pyruvate kinase M2 isoenzyme
    Opis:
    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.
    Źródło:
    Progress on Chemistry and Application of Chitin and its Derivatives; 2010, 15; 149-158
    1896-5644
    Pojawia się w:
    Progress on Chemistry and Application of Chitin and its Derivatives
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Role of oligochitosans in regulation of cellular activity and location of pyruvate kinase (pk) isoenzyme m2 that affects proliferation of ehrlich ascites tumor cells (eat)
    Autorzy:
    Ignacak, Jan
    Wiśniewska-Wrona, Maria
    Pałka, Iwona
    Niekraszewicz, Antoni
    Powiązania:
    https://bibliotekanauki.pl/articles/1035231.pdf
    Data publikacji:
    2013
    Wydawca:
    Sieć Badawcza Łukasiewicz - Polskie Towarzystwo Chitynowe
    Tematy:
    isoenzyme M1 and M2 pyruvate kinase
    nucleus
    oligochitosans
    ε-methyl-L-lysyne
    Opis:
    The pyruvate kinase isoenzyme M2 originating from the nucleoplasm and cytoplasm of tumor cells, with its highest affinity to the 2-phosphoenolpyruvate (2-PEP) and sensitivity to L-cysteine, contributes to an increased generation of energy as ATP, necessary for tumor cell proliferation. In the presence of L-cysteine, the isoenzyme M2 PK demonstrates the activity of histone kinase, transferring the phosphoryl group from 2-PEP to the ε-amine residue of the H1 histone lysine. Oligochitosans induce expression of the inducible nitric oxide synthase gene (iNOS), what results in an increased synthesis of nitric oxide, which reacts with L-cysteine and produces L-S-nitrosocysteine. Lack of L-cysteine contributes to inhibition of kinase activity of the H1 histone, an M2 PK isoenzyme. Decreased phosphorylation of the H1 histone contributes to inhibition of EAT cell proliferation. No effect on proliferation of normal cells that include the PK M1 isoenzyme has been observed in the presence of oligochitosans.
    Źródło:
    Progress on Chemistry and Application of Chitin and its Derivatives; 2013, 18, 18; 67-76
    1896-5644
    Pojawia się w:
    Progress on Chemistry and Application of Chitin and its Derivatives
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Role of oligochitosans in regulation of cellular activity and location of pyruvate kinase (pk) isoenzyme m2 that affects proliferation of ehrlich ascites tumor cells (eat)
    Autorzy:
    Ignacak, Jan
    Wiśniewska-Wrona, Maria
    Pałka, Iwona
    Niekraszewicz, Antoni
    Powiązania:
    https://bibliotekanauki.pl/articles/1035209.pdf
    Data publikacji:
    2013
    Wydawca:
    Sieć Badawcza Łukasiewicz - Polskie Towarzystwo Chitynowe
    Tematy:
    isoenzyme M1 and M2 pyruvate kinase
    nucleus
    oligochitosans
    ε-methyl-L-lysyne
    Opis:
    The pyruvate kinase isoenzyme M2 originating from the nucleoplasm and cytoplasm of tumor cells, with its highest affinity to the 2-phosphoenolpyruvate (2-PEP) and sensitivity to L-cysteine, contributes to an increased generation of energy as ATP, necessary for tumor cell proliferation. In the presence of L-cysteine, the isoenzyme M2 PK demonstrates the activity of histone kinase, transferring the phosphoryl group from 2-PEP to the ε-amine residue of the H1 histone lysine. Oligochitosans induce expression of the inducible nitric oxide synthase gene (iNOS), what results in an increased synthesis of nitric oxide, which reacts with L-cysteine and produces L-S-nitrosocysteine. Lack of L-cysteine contributes to inhibition of kinase activity of the H1 histone, an M2 PK isoenzyme. Decreased phosphorylation of the H1 histone contributes to inhibition of EAT cell proliferation. No effect on proliferation of normal cells that include the PK M1 isoenzyme has been observed in the presence of oligochitosans.
    Źródło:
    Progress on Chemistry and Application of Chitin and its Derivatives; 2013, 18, 18; 67-76
    1896-5644
    Pojawia się w:
    Progress on Chemistry and Application of Chitin and its Derivatives
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-4 z 4

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