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Wyszukujesz frazę "Ignacak, Jan" wg kryterium: Autor

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    Wyświetlanie 1-13 z 13
    Tytuł:
    N-Acetylneuraminic acid, phosphate and thiol groups of pyruvate kinase isoenzymes from Morris hepatoma 7777 and normal rat liver
    Autorzy:
    Ignacak, Jan
    Gumińska, Maria
    Powiązania:
    https://bibliotekanauki.pl/articles/1044937.pdf
    Data publikacji:
    1997
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Źródło:
    Acta Biochimica Polonica; 1997, 44, 2; 201-208
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Comparison of pyruvate kinase variants from rat liver and Morris hepatoma 7777, by an affinity chromatography on Blue Sepharose CL-6B
    Autorzy:
    Ignacak, Jan
    Gumińska, Maria
    Powiązania:
    https://bibliotekanauki.pl/articles/1045484.pdf
    Data publikacji:
    1993
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Źródło:
    Acta Biochimica Polonica; 1993, 40, 2; 261-267
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Tumor-specific pyruvate kinase isoenzyme M_2 involved in biochemical strategy of energy generation in neoplastic cells
    Autorzy:
    Gumińska, Maria
    Ignacak, Jan
    Kędryna, Teresa
    Stachurska, Maria
    Powiązania:
    https://bibliotekanauki.pl/articles/1044896.pdf
    Data publikacji:
    1997
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Źródło:
    Acta Biochimica Polonica; 1997, 44, 4; 711-724
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    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
    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 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:
    The role of oligochitosans in akt kinase regulation
    Autorzy:
    Ignacak, Jan
    Wiśniewska-Wrona, Maria
    Dulińska-Litewka, Joanna
    Pałka, Iwona
    Kucharska, Magdalena
    Powiązania:
    https://bibliotekanauki.pl/articles/1034912.pdf
    Data publikacji:
    2015
    Wydawca:
    Sieć Badawcza Łukasiewicz - Polskie Towarzystwo Chitynowe
    Tematy:
    Akt kinase – PKB
    EAT cells proliferation
    HIF-1 factor.
    M2 pyruvate kinase
    Opis:
    Among characteristic properties of cancers, there is their increased glycolytic activity.Contrary to normal cells, neoplastic cells use anaerobic glycolysis, even when a sufficient amount of oxygen is available. The intensity of the process is associated with a considerable demand for energy in the form of ATP. Akt, which - acting through the mTOR pathway - activates the HIF-1 factor, which in turn activates hexokinase that participates in glucose phosphorylation, stimulates the transport of glucose to cells via increasing glucose transporters (GLUT) and activates lactate dehydrogenase (which transforms pyruvate to lactate). Chitosan, as well as products of its degradation - oligochitosans - contribute to inhibiting the activity of the Akt kinase, and thus contribute to inhibiting excessive glycolytic activity of Ehrlich ascites tumor (EAT) cells and to decreasing proliferation of these cells.
    Źródło:
    Progress on Chemistry and Application of Chitin and its Derivatives; 2015, 20; 73-81
    1896-5644
    Pojawia się w:
    Progress on Chemistry and Application of Chitin and its Derivatives
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Inhibition of ehrlich ascites tumour (eat) cells proliferation through chitosan-mediated regulation of activity of the akt pathway
    Autorzy:
    Ignacak, Jan
    Wiśniewska-Wrona, Maria
    Dulińska-Litewka, Joanna
    Pałka, Iwona
    Kucharska, Magdalena
    Powiązania:
    https://bibliotekanauki.pl/articles/1035195.pdf
    Data publikacji:
    2014
    Wydawca:
    Sieć Badawcza Łukasiewicz - Polskie Towarzystwo Chitynowe
    Tematy:
    Akt kinase - PKB
    EAT cells proliferation
    M2 pyruvate kinase
    chitosan
    Opis:
    Isoenzyme M2 pyruvate kinase, which is a marker of cancer transformation, can take both tetramer (cytosol) and dimer (nucleus) forms. The former is responsible for ATP synthesis, and the latter demonstrates histone H1 kinase activity. Regulation of the expression of pyruvate kinase through which Akt controls the expression of genes involved in Ehrlich ascites tumour (EAT) cell proliferation, migration and death, also involves cross-talk with the other signalling pathways, transcription factors and co-regulatory proteins such as β-catenin and c-Myc. Treatment of EAT cells with chitosans significantly reduced their proliferation (by 45-60%), expression of nuclear β-catenin, c-Myc as well as cell migration. After 48–72 hours of treatment of the cell with oligochitosans, lower levels of p-Akt were detected. Simultaneously, decreased expression of isoenzyme M2 PK protein levels was observed. The dimeric form (nucleus) can participate in H1 histone phosphorylation, which contributes to increased EAT cell proliferation.
    Źródło:
    Progress on Chemistry and Application of Chitin and its Derivatives; 2014, 19; 33-40
    1896-5644
    Pojawia się w:
    Progress on Chemistry and Application of Chitin and its Derivatives
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Effect of oligochitosans on expression of inos gene in ehrlich ascites tumour in vitro
    Autorzy:
    Ignacak, Jan
    Wiśniewska-Wrona, Maria
    Dulińska-Litewka, Joanna
    Pałka, Iwona
    Zagajewski, Jacek
    Niekraszewicz, Antoni
    Powiązania:
    https://bibliotekanauki.pl/articles/1035407.pdf
    Data publikacji:
    2012
    Wydawca:
    Sieć Badawcza Łukasiewicz - Polskie Towarzystwo Chitynowe
    Tematy:
    chitosan oligomers
    histone H1
    iNOS (inducible nitric oxide synthase)
    nitric oxide
    Opis:
    Oligochitosans obtained through degradation of macromolecules of chitosan with a high degree of deacetylation turned out to be biologically active, contributing to an increase of nitric oxide levels in Ehrlich ascites tumor (EAT) cells through inducing expression of the isoform of inducible nitric oxide synthase (iNOS) gene. An increase of NO levels in EAT cells in the presence of the investigated oligochitosans might contribute to nitrosylation of L-cysteine – an allosteric effector of the M2 isoenzyme of pyruvate kinase (PK), which switches the PK kinase activity, responsible for ATP synthesis, to the histone kinase activity that may participate in histone H1 phosphorylation. Lack of the histone activity of the PK M2 isoenzyme may contribute to decreased histone H1 phosphorylation and thus inhibit EAT cells proliferation.
    Źródło:
    Progress on Chemistry and Application of Chitin and its Derivatives; 2012, 17; 141-148
    1896-5644
    Pojawia się w:
    Progress on Chemistry and Application of Chitin and its Derivatives
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    The role of chitosan in akt kinase regulation activity
    Autorzy:
    Ignacak, Jan
    Wiśniewska-Wrona, Maria
    Dulińska-Litewka, Joanna
    Pałka, Iwona
    Kucharska, Magdalena
    Kazimierski, Jan
    Powiązania:
    https://bibliotekanauki.pl/articles/1034695.pdf
    Data publikacji:
    2016
    Wydawca:
    Sieć Badawcza Łukasiewicz - Polskie Towarzystwo Chitynowe
    Tematy:
    Akt kinase (PKB)
    M2 pyruvate kinase
    cells migration
    metalloproteinases
    Opis:
    A decrease in migration of tumor cells incubated with the investigated chitosan preparations was correlated with a decreased activity of MMP-2 and MMP-9 metalloproteinases, what significantly affected inhibition of tumor cell proliferation. In the investigations of the effects of various chitosan preparations on expression of PCNA, Akt and β-catenin in the normal human 184A1 cells and in breast carcinoma MCF7 cells evaluated at the protein level, significant differences in inhibition of expression of selected genes were noted in the tumor cells. Similarly as in the case of human cells, in mouse cells, the differences in expression of the investigated genes involved solely the Ehrlich carcinoma cells. In the presence of the investigated chitosan preparations, there was observed inhibition of expression of the N-cadherin, β-catenin, Akt and PCNA genes. In case of p21 protein, its level increased, similarly as in the human breast carcinoma cells, what may also be related to phosphorylation of the protein, its capture by the cytosol and prolonging its half-life as compared to the non-phosphorylated form. In case of the normal human 181A1 cells and mouse CRL 1636 cells, no significant alterations were noted in expression of the investigated genes in presence of the employed chitosan preparations.
    Źródło:
    Progress on Chemistry and Application of Chitin and its Derivatives; 2016, 21; 73-82
    1896-5644
    Pojawia się w:
    Progress on Chemistry and Application of Chitin and its Derivatives
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-13 z 13

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