How to extend your (polylactosamine) antennae

Kimber, M.S.

doi:10.1016/j.jbc.2020.100212

Cited by 2 publications

(1 citation statement)

References 8 publications

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“…Gal-1 recognizes glycoconjugates bearing the N-acetyllactosamine (LacNAc) moieties with terminal and internal β1,4-linked galactose residues [ 20 ]. Gal-1 binding to LacNAc units is regulated via the action of one of seven ß1,4 galactosyltransferases synthesizing N -acetyllactosamine (Gal β 1-4GlcNAc), and its binding to repeating poly-LacNAc units is regulated via the action of ß1,3 N-acetylglucosaminyltransferase 2 ( B3GNT2 ), which is frequently decorated with other functional groups such as sialic acid [ 21 , 22 , 23 ]. Binding is further enhanced by the amplification of branching in complex-type N-glycans, repeated LacNAc motifs in N- and O-glycans, and 3- O -sulfation of the ligand [ 24 ].…”

Section: Molecular Structure Of Gal-1 -3 and -9 And Their Involvement...mentioning

confidence: 99%

Decoding Strategies to Evade Immunoregulators Galectin-1, -3, and -9 and Their Ligands as Novel Therapeutics in Cancer Immunotherapy

Lau

Dimitroff

2022

IJMS

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Galectins are a family of ß-galactoside-binding proteins that play a variety of roles in normal physiology. In cancer, their expression levels are typically elevated and often associated with poor prognosis. They are known to fuel a variety of cancer progression pathways through their glycan-binding interactions with cancer, stromal, and immune cell surfaces. Of the 15 galectins in mammals, galectin (Gal)-1, -3, and -9 are particularly notable for their critical roles in tumor immune escape. While these galectins play integral roles in promoting cancer progression, they are also instrumental in regulating the survival, differentiation, and function of anti-tumor T cells that compromise anti-tumor immunity and weaken novel immunotherapies. To this end, there has been a surge in the development of new strategies to inhibit their pro-malignancy characteristics, particularly in reversing tumor immunosuppression through galectin–glycan ligand-targeting methods. This review examines some new approaches to evading Gal-1, -3, and -9–ligand interactions to interfere with their tumor-promoting and immunoregulating activities. Whether using neutralizing antibodies, synthetic peptides, glyco-metabolic modifiers, competitive inhibitors, vaccines, gene editing, exo-glycan modification, or chimeric antigen receptor (CAR)-T cells, these methods offer new hope of synergizing their inhibitory effects with current immunotherapeutic methods and yielding highly effective, durable responses.

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