Interaction between DMBT1 and galectin 3 is modulated by the structure of the oligosaccharides carried by DMBT1 |
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Authors: | Rossez Yannick Coddeville Bernadette Elass Elisabeth Quinchon Jean-François Vidal Olivier Corfield Anthony P Gosset Pierre Lacroix Jean-Marie Michalski Jean-Claude Robbe-Masselot Catherine |
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Institution: | a Univ Lille Nord de France, F-59000 Lille, France b USTL, UGSF, IFR 147, F-59650 Villeneuve d’Ascq, France c CNRS, UMR 8576, F-59650 Villeneuve d’Ascq, France d Department of Pathology, Hôpital Saint-Vincent, Faculté libre de Médecine de Lille, Boulevard de Belfort, 59020 Lille, France e Mucin Research Group, Clinical Science at South Bristol, Bristol BS2 8HW, UK |
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Abstract: | DMBT1 (deleted in malignant brain tumor 1), a human mucin-like glycoprotein, belonging to the scavenger receptor cystein-rich (SRCR) superfamily, is mainly secreted from mucosal epithelia. It has been shown previously that interaction of hensin, the rabbit ortholog of DMBT1, with galectin 3, a β-galactoside-binding lectin, induces a terminal differentiation of epithelial cells. In this paper, we have used surface plasmon resonance (SPR), to analyse the binding of galectin 3 to two purified samples of human DMBT1:recombinant DMBT1 produced in CHO cells and DMBT1 isolated from intestinal tissues. Characterization of their glycosylation profile by nano-ESI-Q-TOF tandem mass spectrometry showed significant differences in O-glycans between the two DMBT1 samples. Results obtained by SPR demonstrated that the oligosaccharide side chains of DMBT1 are recognized by the carbohydrate-recognition domain (CRD) of galectin 3 and modification in the pattern of oligosaccharides modulates the binding parameters of DMBT1 with galectin 3. Moreover, using immunohistochemistry on paraffin-embedded colonic tissue sections, we could show a co-localisation of DMBT1 and galectin 3 in human intestine, suggesting a potential physiological interaction. |
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Keywords: | DMBT1 Galectin 3 Glycosylation Mass spectrometry Surface plasmon resonance |
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