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. 2022 Jul 26;23(15):8251. doi: 10.3390/ijms23158251

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© 2022 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

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Alterations in the N-glycoforms of galectin 3-binding protein in HT29 cells induced by 2DG. (A) Site-specific N-glycosylation changes in galectin 3-binding protein at N-glycosites of Asn69, Asn125, Asn398, and Asn551. (B,C) Glycoforms with high-mannose identified at Asn69 and Asn125 sites showing a significant decrease or even completely inhibition in glycosylation due to 2DG treatment. (D,E) Glycoforms at Asn398 and Asn551 with not only high-mannose, but also complex and hybrid N-glycans, showing a similar influence from 2DG treatment, in particular mannosylation. Ratio* represents the XIC of the target peptide/internal standard (THYG).