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Cited by 44Galectins and Cancer BiologyProteoglycans and glycosaminoglycans researchGlycosylation and Glycoproteins Research

The DOI matches its Crossref record; 40 of the 40 references it cites were found in a registry or an index.

Multitasking Human Lectin Galectin-3 Interacts with Sulfated Glycosaminoglycans and Chondroitin Sulfate Proteoglycans

Talaga, Melanie L., Fan, Ni, Fueri, Ashli L., Brown, Robert K., Bandyopadhyay, Purnima, Dam, Tarun K.·2016·Biochemistry
DOI 10.1021/acs.biochem.6b00504
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Abstract

Glycosaminoglycan (GAG) binding proteins (GAGBPs), including growth factors, cytokines, morphogens, and extracellular matrix proteins, interact with both free GAGs and those covalently linked to proteoglycans. Such interactions modulate a variety of cellular and extracellular events, such as cell growth, metastasis, morphogenesis, neural development, and inflammation. GAGBPs are structurally and evolutionarily unrelated proteins that typically recognize internal sequences of sulfated GAGs. GAGBPs are distinct from the other major group of glycan binding proteins, lectins. The multifunctional human galectin-3 (Gal-3) is a β-galactoside binding lectin that preferentially binds to N-acetyllactosamine moieties on glycoconjugates. Here, we demonstrate through microcalorimetric and spectroscopic data that Gal-3 possesses the characteristics of a GAGBP. Gal-3 interacts with unmodified heparin, chondroitin sulfate-A (CSA), -B (CSB), and -C (CSC) as well as chondroitin sulfate proteoglycans (CSPGs). While heparin, CSA, and CSC bind with micromolar affinity, the affinity of CSPGs is nanomolar. Significantly, CSA, CSC, and a bovine CSPG were engaged in multivalent binding with Gal-3 and formed noncovalent cross-linked complexes with the lectin. Binding of sulfated GAGs was completely abolished when Gal-3 was preincubated with β-lactose. Cross-linking of Gal-3 by CSA, CSC, and the bovine CSPG was reversed by β-lactose. Both observations strongly suggest that GAGs primarily occupy the lactose/LacNAc binding site of Gal-3. Hill plot analysis of calorimetric data reveals that the binding of CSA, CSC, and a bovine CSPG to Gal-3 is associated with progressive negative cooperativity effects. Identification of Gal-3 as a GAGBP should help to reveal new functions of Gal-3 mediated by GAGs and proteoglycans.

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Research works printed but not linked: 4

  1. Esko J. D., 2009, Essentials of Glycobiology
  2. Cummings R. D., 2009, Essentials of Glycobiology
  3. Cummings R. D., 2009, Essentials of Glycobiology
  4. Varki A., 2009, Essentials of Glycobiology

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Metadata

Authors
Talaga, M. L., Fan, N., Fueri, A. L., Brown, R. K., Bandyopadhyay, P., & Dam, T. K.
Affiliations
Michigan Technological University (US)
Corresponding author
Dam, Tarun K.
ORCID
Venue
Biochemistry
Publisher
American Chemical Society (ACS)
Published
2016-08-02
Volume
55
Issue
32
Pages
4541-4551
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
DOI
10.1021/acs.biochem.6b00504
OpenAlex
W2504287313
Cited by
44
References
40
Citations by year
2026: 4 · 2025: 2 · 2024: 4 · 2023: 7 · 2022: 6 · 2021: 6 · 2020: 5 · 2019: 3 · 2018: 3 · 2017: 3 · 2016: 1
FWCI
2.02
Type
journal article
Language
en
Open access
closed
Locations
  • Biochemistry (publishedVersion)
  • PubMed (publishedVersion)
  • Digital Commons - Michigan Tech (Michigan Technological University) (submittedVersion)
Topics
  • Life Sciences › Immunology and Microbiology › Immunology › Galectins and Cancer Biology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
Keywords
galectin-3, glycosaminoglycan-binding proteins, sulfated glycosaminoglycans, chondroitin sulfate proteoglycans, heparin, multivalent binding, non-covalent crosslinking, beta-lactose, negative cooperativity, binding affinity, lectin-glycan interactions
MeSH terms
Amino Sugars, Animals, Binding Sites, Cattle, Dermatan Sulfate, Dose-Response Relationship, Drug, Glycosaminoglycans, Heparin, Humans, Hydrogen-Ion Concentration, Lactose, Protein Binding, Chondroitin Sulfate Proteoglycans, Sodium Chloride, Galectin 3

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