Preferencje help
Polish version English version Język
Widoczny [Schowaj] Abstrakt
Liczba wyników

Znaleziono wyników: 4

Liczba wyników na stronie
Pierwsza strona wyników Pięć stron wyników wstecz Poprzednia strona wyników Strona / 1 Następna strona wyników Pięć stron wyników wprzód Ostatnia strona wyników

Wyniki wyszukiwania

Wyszukiwano:
w słowach kluczowych:  dermatan sulphate
help Sortuj według:

help Ogranicz wyniki do:
Pierwsza strona wyników Pięć stron wyników wstecz Poprzednia strona wyników Strona / 1 Następna strona wyników Pięć stron wyników wprzód Ostatnia strona wyników
1

Biglycan is internalized via a chlorpromazine-sensitive route

100%
Gotte M., Feugaing D. D. S., Kresse H.
Cellular and Molecular Biology Letters
|
2004
|
tom 09
|
nr 3
The small leucine-rich proteoglycan biglycan (BGN) is abundantly expressed in mesenchymal tissues. Its expression level is related to the phenotypic differentiation of cells. A dysregulation in BGN expression occurs under several pathological conditions, including glomerulonephritis, mesothelioma, pancreatic cancer and a mouse model of osteoporosis. Since the extracellular concentration of BGN is regulated both by secretion and endocytosis, we performed mechanistic studies on BGN endocytosis in human skin fibroblasts in vitro, using inhibitors of different endocytic routes. Chlorpromazine, an inhibitor of the clathrin-coated pit-pathway reduced endocytosis of BGN in human skin fibroblasts by 40%, and decreased degradation of BGN by 66%. Filipin, an inhibitor of the caveolae pathway, and Tyrphostin AG 1478, a specific inhibitor of EGF-receptor phosphorylation that partially inhibits endocytosis of the structurally related proteoglycan decorin, had no influence on BGN internalization and degradation. Our data indicates that the classical clathrin-mediated endocytic pathway is a major route for the internalization of BGN. Based on the differential susceptibility to pharmacological inhibition, it appears that BGN endocytosis seems to be at least in part mechanistically different from decorin uptake.
2

Dermatan sulfate remodeling associated with advanced Dupuytren's contracture

72%
Kozma E. M., Glowacki A., Olczyk K., Ciecierska M.
Acta Biochimica Polonica
|
2007
|
tom 54
|
nr 4
821-830
Dermatan sulfate (DS) widespread as a component of extracellular matrix proteoglycans, is characterized by great bio-reactivity and remarkable structural heterogeneity due to distinct degrees of sulfation and glucuronosyl epimerization and different polymerization degrees. However, DS metabolism under various biological conditions is poorly known. Dupuytren’s contracture is a benign fibromatosis leading to complex remodeling of the palmar fascia structure and properties. However, it remains unclear whether the disease affects the structure of DS, which is the major tissue glycosaminoglycan. Thus the aim of the study was to examine the structure of the total DS in Dupuytren’s fascia. DS chains were extracted from 5 samples of normal fascia and 7 specimens of Dupuytren’s tissue by papain digestion followed by fractionation with cetylpyridinium chloride. Then, DS structure analysis was performed comprising the evaluation of its molecular masses and sensitivity to hyaluronidase and chondroitinase B. Dupuytren’s contracture is associated with significant remodeling of DS chain structure revealed by (1) a distinct profile of chain molecular masses characterized by the appearance of long size components as well as the increase in the content of small size chains; (2) a different glucuronosyl epimerization pattern connected with the enhanced content of glucuronate disaccharide blocks; (3) chain oversulfation. These structural alterations in total DS may modify the GAG interactions especially affecting collagen fibrillogenesis and growth factor availability. Thus, Dupuytren’s contracture associated DS remodeling may promote the phenomena typical for advanced disease: apoptosis and reduction in cell number as well as the appearance of dense pseudotendinous collagen matrix
3

Assessment of glucuronosyl epimerisation of dermatan sulfate chains in the course of burned wound healing

72%
Olczyk P., Komosinska-Vassev K., Kozma E., Winsz-Szczotka K., Stojko J., Klimek K., Olczyk K.
Bulletin of the Veterinary Institute in Puławy
|
2010
|
tom 54
|
nr 4
The objective of this study was to assess the extent of glucuronosyl epimerisation of dermatan sulfate (DS) chains, isolated from the matrix of burned wound bed. Dermatan sulfates were isolated and purified from normal and injured skin of domestic pigs, on days 3, 5, 10, 15, and 21 after the thermal damage. The wounds were treated with Propol T, silver sulfadiazine (SSD), physiological salt solution, and vehicle of Propol T. The isolated DS samples were depolymerised with chondroitinase ABC and chondroitinase B. The assessment of the amount of unsaturated disaccharides, released during DS enzymatic digestion was performed. It was found that in the course of the tissue repair the glucuronosyl epimerisation pattern of DS chains derived from burned wounds was altered as compared with epimerisation of DS isolated from normal skin. Propol T, in contrary to routinely used SSD, exerts a beneficial effect on DS metabolism leading to the formation of iduronate residue number similar to that of normal skin. The obtained results demonstrate that Propol T modulates DS structure resulting in the accelerated repair of burned tissue.
4
Content available remote

Syndecan signaling: when, where and why?

58%
Multhaupt H. A. B., Yoneda A., Whiteford J. R., Oh E.-S., Lee W., Couchman J. R.
Journal of Physiology and Pharmacology. Supplement
|
2009
|
tom 60
|
nr 4
Pierwsza strona wyników Pięć stron wyników wstecz Poprzednia strona wyników Strona / 1 Następna strona wyników Pięć stron wyników wprzód Ostatnia strona wyników
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.