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Article Dans Une Revue Biochimie Année : 2011

Interaction between DMBT1 and galectin 3 is modulated by the structure of the oligosaccharides carried by DMBT1

Résumé

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.

Dates et versions

hal-00641761 , version 1 (16-11-2011)

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Yannick Rossez, Bernadette Coddeville, Elisabeth Elass, J.-F. Quinchon, Olivier Vidal, et al.. Interaction between DMBT1 and galectin 3 is modulated by the structure of the oligosaccharides carried by DMBT1. Biochimie, 2011, 93 (3), pp.593-603. ⟨10.1016/j.biochi.2010.12.002⟩. ⟨hal-00641761⟩
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