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    Wyświetlanie 1-3 z 3
    Tytuł:
    Differential distribution of cathepsin b in human umbilical cord tissues
    Autorzy:
    Gogiel, Tomasz
    Galewska, Zofia
    Romanowicz, Lech
    Powiązania:
    https://bibliotekanauki.pl/articles/1039685.pdf
    Data publikacji:
    2012
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    umbilical cord
    pregnancy
    cathepsin B
    umbilical cord artery
    umbilical cord vein
    Wharton's jelly
    Opis:
    The extracellular matrix components are differentially distributed among various structures of the umbilical cord. Wharton's jelly is especially rich in collagens and growth factors. Cathepsin B is a major cysteine protease involved in collagen degradation, as well as in the activation of precursor forms of other collagenolytic enzymes and growth factors. We assessed the activity and expression of cathepsin B in the umbilical cord arteries, veins and Wharton's jelly. Extracts of separated umbilical cord components were subjected to an activity assay with the use of specific fluorogenic substrate. The expression of cathepsin B protein was qualitatively evaluated by Western immunoblotting and quantitatively determined with an immunoenzymatic method. The total cathepsin B activity and content calculated per gram of DNA were higher in Wharton's jelly than in the umbilical cord vessels, and the latter parameter was the lowest in the umbilical cord arteries. Moreover, the expression and the activity of latent cathepsin B (following activation by pepsin digestion) calculated per gram of DNA were the highest in Wharton's jelly and the lowest in the umbilical cord arteries. High expression and activity of latent, pepsin-activatable cathepsin B related to DNA content in Wharton's jelly seem to reflect the stimulation of its cells by high amounts of collagen I and growth factors.
    Źródło:
    Acta Biochimica Polonica; 2012, 59, 4; 679-684
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    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:
    Pre-eclampsia-associated alterations in Whartons jelly proteoglycans.
    Autorzy:
    Gogiel, Tomasz
    Galewska, Zofia
    Jaworski, Stefan
    Powiązania:
    https://bibliotekanauki.pl/articles/1041438.pdf
    Data publikacji:
    2005
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    umbilical cord
    proteoglycans
    Wharton's jelly
    glycosaminoglycans
    pre-eclampsia
    Opis:
    Proteoglycans of Wharton's jelly contain mainly chondroitin/dermatan sulphate chains. The predominant proteoglycan is decorin (core proteins of 45 and 47 kDa), although the core proteins of biglycan (45 kDa), versican (260 kDa) and of other proteoglycans (90, 110, 220 kDa) were also detected (Gogiel et al., 2003). The aim of the present study was to compare the proteoglycan composition of Wharton's jelly of newborns delivered by healthy mothers and those with pre-eclampsia. Proteoglycans from pre-eclamptic Wharton's jelly had a higher sulphated glycosaminoglycan/protein ratio than those of normal tissue. Pre-eclampsia is associated with a lower level of all proteoglycan core proteins, especially those of higher molecular mass (such as versican), although the same set of core proteins were found in normal and pre-eclamptic Wharton's jelly. The alterations in the proteoglycan composition of Wharton's jelly may affect the mechanical properties of the umbilical cord and, in the case of pre-eclampsia, disturb foetal blood circulation.
    Źródło:
    Acta Biochimica Polonica; 2005, 52, 2; 501-507
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-3 z 3

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