Autor: Romanowicz, Małgorzata. - Katalog OPAC zbiorów

Skocz do pozycji: 3.

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

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