Impact of glycosylation and detergent-resistant membranes on the function of intestinal sucrase-isomaltase
| Autor: | Gabi Wetzel, Hassan Y. Naim, Arndt Rohwedder, Martin Heine |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
1-Deoxynojirimycin
Acetylgalactosamine Glycosylation Brush border Detergents Clinical Biochemistry Biochemistry Sucrase chemistry.chemical_compound Benzyl Compounds Humans Molecular Biology Lipid raft Microvilli biology Cell Membrane Apical membrane Sucrase-Isomaltase Complex Intestines carbohydrates (lipids) Membrane glycoproteins chemistry biology.protein Caco-2 Cells Sucrase-isomaltase Isomaltase |
| Zdroj: | bchm. 390:545-549 |
| ISSN: | 1437-4315 1431-6730 |
| Popis: | Sucrase-isomaltase (SI) is a highly N- and O-glycosylated intestinal brush border membrane protein. SI is sorted with high fidelity to the apical membrane via O-linked glycans that mediate its association with lipid rafts or detergent-resistant membranes (DRMs). Here, we show that N- and O-glycosylation and DRMs are implicated in the regulation of the function of SI in intestinal Caco-2 cells. The activities of sucrase (SUC) and isomaltase (IM) increase substantially in DRMs when N- and O-glycosylation patterns are intact. Disruption of DRMs by solubilization with Triton X-100 at 37°C substantially reduces the activities of SUC and IM. Furthermore, modulation of O-glycosylation by benzyl-2-acetamido-2-deoxy-α-d-galactopyranoside and N-glycosylation by deoxymannojirimycin is linked to a decreased capacity of SI to associate with DRMs, with a subsequent reduction of the enzymatic activities of SUC and IM. This is the first report that reveals a direct role of N- and O-glycans in association with DRMs in regulating the function of a membrane glycoprotein. |
| Databáze: | OpenAIRE |
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