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Media type:
E-Article
Title:
Impact of glycosylation and detergent-resistant membranes on the function of intestinal sucrase-isomaltase
Contributor:
Wetzel, Gabi;
Heine, Martin;
Rohwedder, Arndt;
Naim, Hassan Y.
Published:
Walter de Gruyter GmbH, 2009
Published in:
bchm, 390 (2009) 7, Seite 545-549
Language:
English
DOI:
10.1515/bc.2009.077
ISSN:
1431-6730;
1437-4315
Origination:
Footnote:
Description:
Abstract 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.