ArticleThe Journal of biological chemistry2010
Bisecting GlcNAc residues on laminin-332 down-regulate galectin-3-dependent keratinocyte motility.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 78 citations in OpenAlex.
- Melanoma Glycome Regulates the Pro-Oncogenic Properties of Extracellular Galectin-3.International journal of molecular sciences · 2025Article
- Glycosylation in Cancer.Handbook of experimental pharmacology · 2025Review
- Galectin-3/Gelatin Electrospun Scaffolds Modulate Collagen Synthesis in Skin Healing but Do Not Improve Wound Closure Kinetics.Bioengineering (Basel, Switzerland) · 2024Article
- Galectins in epithelial-mesenchymal transition: roles and mechanisms contributing to tissue repair, fibrosis and cancer metastasis.Biological research · 2024Review
- Altered galectin-3 distribution and migratory function in the pre-diabetic non-obese diabetic mouse thymus.Frontiers in endocrinology · 2024Article
- Bisecting GlcNAc modification reverses the chemoresistance via attenuating the function of P-gp.Theranostics · 2024Article
- Integrin α6β4 Confers Doxorubicin Resistance in Cancer Cells by Suppressing Caspase-3-Mediated Apoptosis: Involvement of N-Glycans on β4 Integrin Subunit.Biomolecules · 2023Article
- Characterization of a HIR-Fab-IDS, Novel Iduronate 2-Sulfatase Fusion Protein for the Treatment of Neuropathic Mucopolysaccharidosis Type II (Hunter Syndrome).BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2023Article
- Development of Galectin-3 Targeting Drugs for Therapeutic Applications in Various Diseases.International journal of molecular sciences · 2023Review
- The pleiotropic role of galectin-3 in melanoma progression: Unraveling the enigma.Advances in cancer research · 2023Review
- Galectin-3 Plays an Important Role in BMP7-Induced Cementoblastic Differentiation of Human Periodontal Ligament Cells by Interacting with Extracellular Components.Stem cells international · 2023Article
- TM4SF1 promotes esophageal squamous cell carcinoma metastasis by interacting with integrin α6.Cell death & disease · 2022Article
- Expression Pattern and Immunoregulatory Roles of Galectin-1 and Galectin-3 in Atopic Dermatitis and Psoriasis.Inflammation · 2022Article
- Diminished Expression of Galectin-3 Around Blisters in Bullous Pemphigoid: An Immunohistochemistry Study.Dermatology practical & conceptual · 2020Article
- Bisecting GlcNAc modification diminishes the pro-metastatic functions of small extracellular vesicles from breast cancer cells.Journal of extracellular vesicles · 2020Article
- Multiple strategies to improve the yield of chitinase a from Bacillus licheniformis in Pichia pastoris to obtain plant growth enhancer and GlcNAc.Microbial cell factories · 2020Article
- β4GALT1 controls β1 integrin function to govern thrombopoiesis and hematopoietic stem cell homeostasis.Nature communications · 2020Article
- Bisecting N-Acetylglucosamine on EGFR Inhibits Malignant Phenotype of Breast Cancer via Down-Regulation of EGFR/Erk Signaling.Frontiers in oncology · 2020Article
- N-Glycosylation in progression of skin cancer.Medical oncology (Northwood, London, England) · 2019Review
- Proteome-wide Identification of Glycosylation-dependent Interactors of Galectin-1 and Galectin-3 on Mesenchymal Retinal Pigment Epithelial (RPE) Cells.Molecular & cellular proteomics : MCP · 2017Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Laminin-332 (Lm332; formerly laminin-5) is a basement membrane protein in the skin, which promotes cell motility in wound healing and cancer invasion. In a previous study, we reported that the introduction of bisecting GlcNAc into Lm332 (GnT-III-Lm332), catalyzed by N-acetylglucosaminyltransferase III (GnT-III), reduced cell migration (Kariya, Y., Kato, R., Itoh, S., Fukuda, T., Shibukawa, Y., Sanzen, N., Sekiguchi, K., Wada, Y., Kawasaki, N., and Gu, J. (2008) J. Biol. Chem. 283, 33036-33045). However, the underlying molecular mechanism by which GnT-III-Lm332 suppresses the normal biological functions of Lm332 remains to be elucidated. In this study, we show that galectin-3, which is a beta-galactoside-binding protein, strongly bound to unmodified Lm332 but not to GnT-III-Lm332 and that binding of galectin-3 was completely blocked by lactose. Exogenous galectin-3 significantly enhanced keratinocyte cell motility on control Lm332 but not on GnT-III-Lm332. A functional blocking antibody against galectin-3 inhibited Lm332-induced alpha3beta1 and alpha6beta4 integrin clustering and focal contact formation. Co-immunoprecipitation revealed that galectin-3 associated with both beta4 integrin and epidermal growth factor receptor, thereby cross-linking the two molecules. The associations were inhibited by either the presence of lactose or expression of GnT-III. Moreover, galectin-3 consistently enhanced ERK activation. Taken together, the results of this study are the first to clearly identify the molecular mechanism responsible for the inhibitory effects of GnT-III on extracellular matrix-integrin-meditated cell adhesion, migration, and signal transduction. The findings presented herein shed light on the importance of N-glycosylation-mediated supramolecular complex formation on the cell surface.
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