Archive 25/1/7

Galectins are not just β-galacside binding lectins, but have multifaceted functions

A group from Axe of Infectious and Immune Diseases, CHU de Quebec-Université Laval Research Centre, Faculty of Medicine, and Research Centre for Infectious Diseases, Laval University, Quebec, Canada etc. has reviewed about the multifaceted roles of galectins in self-defense.
https://www.sciencedirect.com/science/article/pii/S1044532324000642?via%3Dihub#bib63

Unlike other lectins, galectins lack signal peptides, so they are synthesized as soluble, non-glycosylated proteins in the cytosol, where glycan ligands are absent. Further, certain galectins, such as galectin-1 and galectin-3, have been found to translocate to the nucleus under specific conditions. This presents a paradox: galectins’ primary location is in the cytosol, an environment devoid of the glycans they bind.

Interestingly, however, galectins are also capable of reaching the extracellular space via a non-classical, leaderless secretory pathway.

This unique distribution of galectins both inside and outside the cell underscores their versatility, suggesting a layered regulatory mechanism that allows galectin function in host defense to be modulated both by their synthesis and by the spatial control of their access to ligands, extending their evolutionary role beyond traditional glycan recognition.

This must be one of the good reviews about Galectins.

A new lectin ALA might be effective on CCA treatments

A group from Department of Biochemistry, Faculty of Medicine, Khon Kaen University, Thailand has reported about a new lectin ALA extracted from the seeds of Artocarpus lakoocha.
https://www.nature.com/articles/s41598-024-84444-7

ALA exhibits agglutinin activity and has binding specificity to T- and Tn-associated glycoproteins and monosaccharides such as Gal and GalNAc.

It was confirmed that glycans identified by ALA were elevated in human Cholangiocarcinoma (CCA) tissues.
ALA significantly reduced cell viability of CCA cells, KKU-100 and KKU-213B, in a dose-dependent manner (up to 30 µg/mL) with approximately a 30% decrease observed at the highest concentration. And also, ALA significantly reduced the migration and invasion ability of KKU-100 and KKU-213B cells in a dose-dependent manner with 1–2 µg/mL which did not affect cell viability.

These results suggest their therapeutic potential effects on CCA treatments.

Glycan binding specificity of marine lectins

A group from School of Medicine and Life Sciences, Far Eastern Federal University, Vladivostok, Russia has summarized about marine lectins and applicationn to human brain tumores.
https://pmc.ncbi.nlm.nih.gov/articles/PMC11679326/

HOL-18 from the marine sponge Halichondria okadai binds to complex N-glycans
OXYL from marine star Anneissia japonica binds to LacNAc type 2 but does not bind to LacNAc type 1
AVL from marine sponge Aphrocallistes vastus binds to sialylated-mucin glycans
ESA from the seaweed Eucheuma serra binds to high mannose N-glycans
UPL1 from the seaweed Ulva pertusa binds to GlcNAc and high-mannose glycans
BPL2 from the seaweed Bryopsis plumosa binds to trimannosyl core
KSL from red alga Kappaphycus striatus binds to high mannose N-glycans
DIFBL from the sea bass Dicentrarchus labrax binds to fucose
APL from starfish Asterina pectinifera binds to Tn antigen
CGL from the bivalve Crenomytilus grayanus binds to GalNAc/Gal and recognizes Gb3
MytiLec from the Mediterranean mussel also binds to Gb3
HCL from the marine sponge Haliclona cratera binds to binds to GalNAc/Gal
DTL from the ascidian Didemnum ternatanum binds to GlcNAc

Powered by WordPress |Copyright © 2020 Emukk. All rights reserved