Mapping glycan-mediated galectin-3 interactions by live cell proximity labeling.

Abstract:

:Galectin-3 is a glycan-binding protein (GBP) that binds β-galactoside glycan structures to orchestrate a variety of important biological events, including the activation of hepatic stellate cells and regulation of immune responses. While the requisite glycan epitopes needed to bind galectin-3 have long been elucidated, the cellular glycoproteins that bear these glycan signatures remain unknown. Given the importance of the three-dimensional (3D) arrangement of glycans in dictating GBP interactions, strategies that allow the identification of GBP receptors in live cells, where the native glycan presentation and glycoprotein expression are preserved, have significant advantages over static and artificial systems. Here we describe the integration of a proximity labeling method and quantitative mass spectrometry to map the glycan and glycoprotein interactors for galectin-3 in live human hepatic stellate cells and peripheral blood mononuclear cells. Understanding the identity of the glycoproteins and defining the structures of the glycans will empower efforts to design and develop selective therapeutics to mitigate galectin-3-mediated biological events.

authors

Joeh E,O'Leary T,Li W,Hawkins R,Hung JR,Parker CG,Huang ML

doi

10.1073/pnas.2009206117

subject

Has Abstract

pub_date

2020-11-03 00:00:00

pages

27329-27338

issue

44

eissn

0027-8424

issn

1091-6490

pii

2009206117

journal_volume

117

pub_type

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