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.
journal_name
Proc Natl Acad Sci U S Aauthors
Joeh E,O'Leary T,Li W,Hawkins R,Hung JR,Parker CG,Huang MLdoi
10.1073/pnas.2009206117subject
Has Abstractpub_date
2020-11-03 00:00:00pages
27329-27338issue
44eissn
0027-8424issn
1091-6490pii
2009206117journal_volume
117pub_type
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