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Wyszukujesz frazę "Wrona, Maria" wg kryterium: Autor


Wyświetlanie 1-4 z 4
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:
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
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
    Wyświetlanie 1-4 z 4

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