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1
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Accumulation of collagen in ovarian benign tumours

100%
Wolańska M., Sobolewski K., Bańkowski E., Drożdżewicz M.
Acta Biochimica Polonica
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1999
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vol. 46
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issue 4
941-947
EN
Extracellular matrix components of benign ovarian tumours (cystadenoma, adenofibroma, cystadenofibroma) were analysed. The investigated tumours contained twice as much collagen than control ovarian tissues. Significant alterations in mutual quantitative relationships between collagens of various types were observed. The proportion of type I collagen decreased and that of type III collagen increased. The accumulation of collagen was accompanied by a reduction in sulphated glycosaminoglycan content whereas the amount of hyaluronic acid was not changed. Dermatan sulphate was the most abundant glycosaminoglycan component. It is suggested that the accumulation of collagen (natural barrier to the migration of tumour cells) and underexpression of glycosaminoglycans/proteoglycans (binding some growth factors and interleukins) may exert an inhibitory effect on tumour growth.
2
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Collagen, elastin and glycosaminoglycans in aortic aneurysms

88%
Sobolewski K., Wolańska M., Bańkowski E., Gacko M., Głowiński S.
Acta Biochimica Polonica
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1995
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vol. 42
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issue 3
301-307
3
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Distribution of cathepsin L in human umbilical cord tissues

76%
Gogiel T., Wolańska M., Galewska Z., Kinalski P., Sobolewski K., Romanowicz L.
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2017
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vol. 64
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issue 3
507-512
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.
4
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Proteolytic activity of vitreous-humour

75%
Wolańska M., Bakunowicz-Łazarczyk A., Bańkowski E.
Acta Biochimica Polonica
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1991
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vol. 38
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issue 1
119-122
5
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Soluble non-collagen proteins of bovine vitreous humour

74%
Wolańska M., Bańkowski E.
Acta Biochimica Polonica
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1989
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vol. 36
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issue 1
37-43
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