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1.
Diabetologia ; 44(4): 488-94, 2001 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-11357480

RESUMO

AIMS/HYPOTHESIS: Changes in kidney function in diabetes could be due to changes in the kidney basement membranes. Proteoglycans are important constituents of this kidney extracellular matrix. This study explored the possibility that advanced glycation end products affect proteoglycan synthesis in cultured kidney epithelial cells. METHODS: Madin Darby Canine Kidney (MDCK) epithelial cells were cultured with either low glucose (5 mmol/l), low glucose with 10 micrograms/ml of N epsilon-(carboxymethyl)lysine bovine serum albumin (CML-BSA) or high glucose (25 mmol/l). From day 7-8 cells were labelled with either [35S]sulphate or [3H]glucosamine for 24 h. Labelled macromolecules were purified by gel and ion exchange chromatography, and isolated proteoglycans analysed by gel chromatography and electrophoresis. RESULTS: The CML-BSA treatment reduced the proteoglycan synthesis in MDCK cells. Neither the type of glycosaminoglycan chains made nor the molecular size of the chains was affected. CONCLUSION/INTERPRETATION: At concentrations found in the plasma of diabetes patients CML-BSA, decreases proteoglycan expression in kidney epithelial cells. Advanced glycation end products could, accordingly, promote pathological changes in kidneys of diabetics.


Assuntos
Produtos Finais de Glicação Avançada/farmacologia , Rim/efeitos dos fármacos , Rim/metabolismo , Lisina/química , Proteoglicanas/biossíntese , Albumina Sérica/farmacologia , Animais , Linhagem Celular , Cromatografia em Gel , Cromatografia por Troca Iônica , Cães , Eletroforese em Gel de Poliacrilamida , Células Epiteliais/efeitos dos fármacos , Células Epiteliais/metabolismo , Glucosamina/metabolismo , Glucose/farmacologia , Lisina/análogos & derivados , Albumina Sérica/química , Sulfatos/metabolismo , Radioisótopos de Enxofre , Trítio
2.
J Cell Sci ; 112 ( Pt 11): 1797-801, 1999 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-10318771

RESUMO

Sugar moieties have been shown to contain sufficient and necessary information to target examples of secreted and transmembrane glycoproteins to the apical surface of epithelial MDCK cells. We have investigated if the sugar chains of proteoglycans, the glycosaminoglycans, also contain structural determinants for apical transport. Here we show that although 75% of the proteoglycan secretion from MDCK cell monolayers is into the basolateral medium, 75% of the proteoglycans of the chondroitin sulphate type are secreted apically. The sorting information in the chondroitin sulphate proteoglycans is localized to the sugar chains, since protein-free chondroitin sulphate chains, initiated on hexyl beta-D-thioxyloside, were also predominantly secreted to the apical medium.


Assuntos
Sulfatos de Condroitina/metabolismo , Animais , Linhagem Celular , Cães , Rim/citologia
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