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    Wyświetlanie 1-2 z 2
    Tytuł:
    Distribution of cathepsin L in human umbilical cord tissues
    Autorzy:
    Gogiel, Tomasz
    Wolańska, Małgorzata
    Galewska, Zofia
    Kinalski, Piotr
    Sobolewski, Krzysztof
    Romanowicz, Lech
    Powiązania:
    https://bibliotekanauki.pl/articles/1038609.pdf
    Data publikacji:
    2017
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    cathepsin L
    cysteine protease inhibitors
    umbilical cord
    umbilical cord artery
    umbilical cord vein
    Wharton's jelly
    Opis:
    The extracellular matrix components show specific distribution patterns within various structures of the umbilical cord, among which Wharton's jelly is especially collagen-rich tissue. Cathepsin L is a potent cysteine protease engaged in degradation of extracellular matrix proteins, including collagens. We evaluated the activity and expression of cathepsin L, and the inhibitory effect of cysteine protease inhibitors in the umbilical cord arteries, vein and Wharton's jelly. Cathepsin L activity and anti-papain inhibitory effect of cysteine protease inhibitors were quantified in extracts of separated umbilical cord tissues using fluorogenic substrates. The results were calculated per DNA content. The enzyme expression was assessed by Western immunoblotting. The active cathepsin L activity (without activation by pepsin digestion), its percentage in the total activity (after pepsin activation), and the expression of the mature single-chain enzyme were the lowest in the umbilical cord arteries and the highest in Wharton's jelly. The effect of cysteine protease inhibitors showed similar distribution as in the case of the active enzyme, being the highest in Wharton's jelly. Distribution of the activity and expression of mature cathepsin L within the umbilical cord probably results from distinctions in the proenzyme activation process. Differences in the action of cysteine protease inhibitors can partly restrict divergences in the enzyme activity that could reflect its expression alone. Differential enzyme action seems to contribute to tissue-specific collagen turnover within the umbilical cord cells, especially those of Wharton's jelly.
    Źródło:
    Acta Biochimica Polonica; 2017, 64, 3; 507-512
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Theoretical studies of binding modes of two covalent inhibitors of cysteine proteases.
    Autorzy:
    Drabik, Piotr
    Politowska, Ewa
    Czaplewski, Cezary
    Kasprzykowski, Franciszek
    Łankiewicz, Leszek
    Ciarkowski, Jerzy
    Powiązania:
    https://bibliotekanauki.pl/articles/1044228.pdf
    Data publikacji:
    2000
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    cysteine proteases
    covalent protease inhibitors
    constrained simulated annealing
    papain
    molecular dynamics
    Opis:
    Physiological and pathological roles of cysteine proteases make them important targets for inhibitor development. Although highly potent inhibitors of this group of enzymes are known, their major drawback is a lack of sufficient specificity. Two cysteine protease covalent inhibitors, viz. (i) Z-RL-deoxo-V-peptide-epoxysuccinyl hybrid, and (ii) Z-RLVG-methyl-, have been developed and modeled in the catalytic pocket of papain, an archetypal thiol protease. A number of configurations have been generated and relaxed for each system using the AMBER force field. The catalytic pockets S3 and S4 appear rather elusive in view of the observed inhibitors' flexibility. This suggest rather limited chances for the development of selective structure-based inhibitors of thiol proteases, designed to exploit differences in the structure of catalytic pockets of various members of this family.
    Źródło:
    Acta Biochimica Polonica; 2000, 47, 4; 1061-1066
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-2 z 2

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