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    Wyświetlanie 1-4 z 4
    Tytuł:
    The γ-glutamyltransferase activity and non-protein sulfhydryl compounds levels in rat kidney of different age groups.
    Autorzy:
    Włodek, Przemysław
    Sokołowska, Maria
    Smoleński, Olgierd
    Włodek, Lidia
    Powiązania:
    https://bibliotekanauki.pl/articles/1043788.pdf
    Data publikacji:
    2002
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    L-cysteine
    kidney
    aging
    γ-glutamyl transferase
    reactive oxygen species
    protein-bound cysteine
    glutathione
    sulfane sulfur compounds
    Opis:
    The present work was aimed to obtain information about age-dependent changes of γ-glutamyltransferase (GGT) activity and the levels of non-protein sulfhydryl compounds (NPSH) in rat kidneys. In addition, protein-bound cysteine (PB-Cys), sulfane sulfur compounds and reactive oxygen species (ROS) were estimated The results indicate that the activity of GGT and NPSH levels in the kidneys are reduced with age. At the same time, a significant increase in the level of protein-bound cysteine was observed. Simultaneously, the content of sulfane sulfur compounds was increased in the group of the oldest animals. These findings indicate that the capacity for extracellular glutathione degradation and, in consequence, the availability of cysteine for intracellular glutathione biosynthesis may be impaired. The increased PB-Cys level indicates potentiation of the thiolation reaction, i.e. development of protein-mixed disulfides. These results reveal age dependent disturbances in the thiol-disulfide equilibrium in the kidneys which leads to an imbalance between pro- and antioxidatory processes.
    Źródło:
    Acta Biochimica Polonica; 2002, 49, 2; 501-507
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Mass spectrometry identification of membrane-bound respiratory nitrate reductase from Bradyrhizobium sp. (Lupinus)
    Autorzy:
    Polcyn, Władysław
    Powiązania:
    https://bibliotekanauki.pl/articles/1040683.pdf
    Data publikacji:
    2008
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    immunoblot screening
    membrane-bound nitrate reductase [EC 1.7.99.4]
    enzyme purification
    Bradyrhizobium sp. (Lupinus)
    rhizobia
    mass spectrometry sequencing
    Opis:
    Respiratory nitrate reductase (NR) from Bradyrhizobium sp. (Lupinus) USDA 3045 has biochemical properties of the membrane-bound NR type. However, in the completely sequenced rhizobium genomes only genes for the periplasmic type of dissimilatory NR were found. Therefore purification and identification of the enzyme by tandem mass spectrometry (MS/MS) was undertaken. MS/MS spectra representing 149 unique tryptic peptides derived from purified 137-kDa subunit matched the NCBInr-deposited NarG sequences. MS/MS sequencing of two other SDS/PAGE bands (65- and 59-kDa) identified them as derivatives of the NarH-type protein. Applying additional validation criteria, 73% of the sequence of the NarG subunit (902 aa) and 52% of NarH sequence (266 aa) was assembled (UniProt KB acc. no. P85097 and P85098). This is the first unambiguous identification of an active NarGH-like NR in rhizobia. Moreover, arguments are provided here for the existence of a functional enzyme of this type also among other rhizobial species, basing on immunoblot screening and the presence of membrane-associated NR-active electrophoretic forms.
    Źródło:
    Acta Biochimica Polonica; 2008, 55, 4; 753-760
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Sp1 mediates phorbol ester (PMA)-induced expression of membrane-bound guanylyl cyclase GC-A in human monocytic THP-1 cells
    Autorzy:
    Mitkiewicz, Małgorzata
    Bac, Bernadeta
    Kuropatwa, Marianna
    Kurowska, Ewa
    Matuszyk, Janusz
    Siednienko, Jakub
    Powiązania:
    https://bibliotekanauki.pl/articles/1038369.pdf
    Data publikacji:
    2018
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    membrane-bound guanylyl cyclase type A
    phorbol 12-myristate 13-acetate
    human monocytic cell line THP-1
    protein kinases
    Sp1 transcription factor
    Opis:
    Cyclic guanosine monophosphate (cGMP) is synthesized by two types of enzymes: particulate (membrane-bound) guanylyl cyclases (pGCs) and soluble (cytosolic) guanylyl cyclases (sGCs). sGCs are primarily activated by binding of nitric oxide to their prosthetic heme group while pGCs are activated by binding of peptide ligands to their extracellular domains. One of them, pGC type A (GC-A) is activated by atrial and brain natriuretic peptides (ANP and BNP, respectively). Human monocytes isolated from peripheral blood mononuclear cells have been found to display sGC expression without concomitant expression of GC-A. However, GC-A activity appears in monocytes under certain conditions but a molecular mechanism of GC-A expression is still poorly understood. In this report we show that phorbol ester (PMA) induces transcription of a gene encoding GC-A in human monocytic THP-1 cells. Moreover, we find that PMA-treated THP-1 cells raise cGMP content following treatment with ANP. Studies using pharmacological inhibitors of protein kinases suggest involvement of protein kinase C (PKC), mitogen extracellular kinases (MEK1/2), and extracellular signal-regulated kinases (ERK1/2) in PMA-induced expression of the GC-A encoding gene in THP-1 cells. Finally, we show that PMA stimulates binding of Sp1 transcription factor to GC-rich DNA sequences and mithramycin A (a selective Sp1 inhibitor) inhibits expression of the GC-A mRNA in PMA-treated THP-1 cells. Taken together, our findings suggest that the PMA-stimulated PKC and MEK/ERK signaling pathways induce Sp1-mediated transcription of the GC-A encoding gene in human monocytic THP-1 cells.
    Źródło:
    Acta Biochimica Polonica; 2018, 65, 3; 409-414
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Nitrate-related down-regulation of respiratory nitrate reductase from Bradyrhizobium sp. (Lupinus)
    Autorzy:
    Polcyn, Władysław
    Powiązania:
    https://bibliotekanauki.pl/articles/1040684.pdf
    Data publikacji:
    2008
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    multiple enzyme forms
    membrane-bound nitrate reductase [EC 1.7.99.4]
    down-regulation
    nitrate and nitrite induction
    stability of subunits
    Bradyrhizobium sp. (Lupinus)
    Opis:
    Previously, we showed that anaerobic induction of respiratory nitrate reductase (NR) activity in Bradyrhizobium sp. (Lupinus) USDA 3045 is strongly enhanced by nitrate or nitrite through de novo synthesis. Here, multiple NR-active soluble forms, ranging from 75 kDa to 190 kDa, were observed under anaerobic conditions. Electrophoretic activity band patterns differed depending on the level and the type of the N oxyanion added. The intensity of the membrane-bound NR activity band of 230 kDa changed with time along with consumption of 2 mM nitrate. It was associated with a parallel 5-fold increase and then 2-fold reduction in the amount of membrane-bound NR protein. In contrast, on 4 mM nitrate, the level of NR protein was much more stable, apparently due to slower nitrate depletion. Moreover, in cells anaerobically grown without nitrate addition, a 42-kDa derivative of NR degradation was immunodetected, which was not observed if nitrate was present in the medium. These findings suggest that the amount of the respiratory NR protein could be negatively regulated by endogenous proteases in relation to the level of nitrate available. It seems, therefore, that multiple native forms might be not different isoenzymes but immature complexes or derivatives of the enzyme protein turnover. This report adds to a modest list of bacterial enzymes apparently regulated by proteolysis, such as GS, MurAA, EnvA, GdhA, and MetA.
    Źródło:
    Acta Biochimica Polonica; 2008, 55, 4; 761-766
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-4 z 4

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