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Wyszukujesz frazę "Jaworski, Edward." wg kryterium: Autor


Wyświetlanie 1-6 z 6
Tytuł:
FGF binding by extracellular matrix components of Whartons jelly
Autorzy:
Malkowski, Andrzej
Sobolewski, Krzysztof
Jaworski, Stefan
Bankowski, Edward
Powiązania:
https://bibliotekanauki.pl/articles/1041086.pdf
Data publikacji:
2007
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
umbilical cord
fibroblast growth factor
metalloproteinases
Opis:
Our earlier paper has reported that Wharton's jelly is a reservoir of several peptide growth factors, including acidic and basic fibroblast growth factors (aFGF and bFGF, respectively). Both can be extracted by buffered salts solutions in the form of high molecular mass complexes, probably with a component(s) of the extracellular matrix. Both aFGF and bFGF from such extracts hardly penetrate 10% polyacrylamide gels during electrophoresis. Pre-treatment of Wharton's jelly with hyaluronidase slightly increased the extractability of aFGF, but did not affect the extractability of bFGF. In contrast, the pre-treatment of tissue homogenate with bacterial collagenase (2000 U/ml, 37°C, 18 h) increased the extractability of bFGF. The presence of β-mercaptoethanol in the extracting solutions increased the extractability of both FGFs, but did not release FGFs in their free form, despite reducing the molecular mass of the FGF-containing complexes. We conclude that both aFGF and bFGF are bound through disulphide bonds to a protein component of Wharton's jelly. We propose that ground substance composed mainly of collagen fibrils and hyaluronate molecules, which surrounds the cells of Wharton's jelly, prevents the access of the extracting solution to aFGF and bFGF. Although hyaluronate and collagen do not bind aFGF or bFGF directly, they may constitute a barrier which prevents the dispersion of FGFs in Wharton's jelly. Thus, the high concentration of FGFs around the cells of Wharton's jelly may facilitate the interaction of these factors with membrane receptors, thereby resulting in stimulation of cell division and differentiation, as well as of the synthesis of extracellular matrix components.
Źródło:
Acta Biochimica Polonica; 2007, 54, 2; 357-363
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Electrophoretic and chromatographic patterns of glycosaminoglycans of the umbilical cord vessels and their alteration in EPH-gestosis
Autorzy:
Romanowicz, Lech
Bańkowski, Edward
Jaworski, Stefan
Powiązania:
https://bibliotekanauki.pl/articles/1044793.pdf
Data publikacji:
1998
Wydawca:
Polskie Towarzystwo Biochemiczne
Źródło:
Acta Biochimica Polonica; 1998, 45, 3; 805-809
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Binding of the basic fibroblast growth factor (bFGF) by soluble components of human umbilical cord.
Autorzy:
Sobolewski, Krzysztof
Bańkowski, Edward
Pałka, Jerzy
Jaworski, Stefan
Powiązania:
https://bibliotekanauki.pl/articles/1043707.pdf
Data publikacji:
2002
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
umbilical cord artery
fibroblast growth factor
Wharton's jelly
pre-eclampsia
EPH-gestosis
Opis:
Pre-eclampsia, the most common pregnancy associated syndrome, is connected with remodelling of extracellular matrix of the umbilical cord tissues. Since the fibroblast growth factor (FGF) is known to be a stimulator of collagen and glycosaminoglycan biosynthesis, one may expect that it plays an important role in such a remodelling. Studies performed on the umbilical cords of 10 control and 10 pre-eclamptic newborns demonstrated that both the umbilical cord arterial wall and Wharton's jelly contain FGF mainly in complexes with the components of different molecular mass. Pre-eclampsia is associated with a decrease of endogenous FGF-binding by soluble high molecular mass components of the umbilical cord. It is suggested that FGF released from these complexes may be actively bound by fibroblasts of the umbilical cord, stimulating them to produce collagen and sulphated glycosaminoglycans.
Źródło:
Acta Biochimica Polonica; 2002, 49, 4; 999-1004
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-6 z 6

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