Distribution of cathepsin L in human umbilical cord tissues

• Authors: Tomasz Gogiel , Małgorzata Wolańska , Zofia Galewska , Piotr Kinalski , Krzysztof Sobolewski , Lech Romanowicz
• Languages of publication: EN

Abstracts

EN

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.

Keywords

EN

cathepsin L; cysteine protease inhibitors; umbilical cord; umbilical cord artery; umbilical cord vein; Wharton's jelly

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 2017
• Volume: 64
• Issue: 3
• Pages: 507-512

Dates

published

2017

received

2017-01-26

revised

2017-04-06

accepted

2017-04-30

(unknown)

2017-08-09

Contributors

author

Tomasz Gogiel

• Department of Medical Biochemistry, Medical University of Białystok, Poland

author

Małgorzata Wolańska

• Department of Medical Biochemistry, Medical University of Białystok, Poland

author

Zofia Galewska

• Department of Medical Biochemistry, Medical University of Białystok, Poland

author

Piotr Kinalski

• Department of Gynaecology and Obstetrics, Provincial Hospital in Bialystok, Bialystok, Poland

author

Krzysztof Sobolewski

• Department of Medical Biochemistry, Medical University of Białystok, Poland

author

Lech Romanowicz

• Department of Medical Biochemistry, Medical University of Białystok, Poland

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Identifiers

DOI

10.18388/abp.2017_1513