ArticleThe Journal of biological chemistry2014
Glycosylation modulates melanoma cell α2β1 and α3β1 integrin interactions with type IV collagen.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 38 citations in OpenAlex.
- Molecular basis of collagen galactosylation by GLT25D1.Nature communications · 2026Article
- The life cycle of type IV collagen.Matrix biology : journal of the International Society for Matrix Biology · 2025Review
- Structure of an FeActa crystallographica. Section F, Structural biology communications · 2025Article
- Melanoma Glycome Regulates the Pro-Oncogenic Properties of Extracellular Galectin-3.International journal of molecular sciences · 2025Article
- Lysyl hydroxylase 2 glucosylates collagen VI to drive lung cancer progression.The Journal of clinical investigation · 2025Article
- Post-translational modifications of collagen and its related diseases in metabolic pathways.Acta pharmaceutica Sinica. B · 2025Review
- Post-translational modifications in the Protein Data Bank.Acta crystallographica. Section D, Structural biology · 2024Review
- Glycosylation Modulates the Structure and Functions of Collagen: A Review.Molecules (Basel, Switzerland) · 2024Review
- A recombinant technique for mapping functional sites of heterotrimeric collagen helices: Collagen IV CB3 fragment as a prototype for integrin binding.The Journal of biological chemistry · 2023Article
- N-Linked Glycosylation in Chinese Hamster Ovary Cells Is Critical for Insulin-like Growth Factor 1 Signaling.International journal of molecular sciences · 2022Article
- Exploring the cardiac ECM during fibrosis: A new era with next-gen proteomics.Frontiers in molecular biosciences · 2022Review
- Integrated proteomic, phosphoproteomic, and N-glycoproteomic analyses of theCurrent research in food science · 2022Article
- Comprehensive Mapping and Dynamics of Site-Specific Prolyl-Hydroxylation, Lysyl-Hydroxylation and Lysyl O-Glycosylation of Collagens Deposited in ECM During Zebrafish Heart Regeneration.Frontiers in molecular biosciences · 2022Article
- A collagen glucosyltransferase drives lung adenocarcinoma progression in mice.Communications biology · 2021Article
- Estrogen receptor α is involved in the regulation of ITGA8 methylation in estrogen receptor-positive breast cancer.Annals of translational medicine · 2020Article
- Modulation of receptor binding to collagen by glycosylated 5-hydroxylysine: Chemical biology approaches made feasible by Carpino's Fmoc group.Peptide science (Hoboken, N.J.) · 2020Article
- The role of collagen in cancer: from bench to bedside.Journal of translational medicine · 2019Review
- Collagen Accumulation in Osteosarcoma Cells lacking GLT25D1 Collagen Galactosyltransferase.The Journal of biological chemistry · 2016Article
- Light-emitting diode therapy increases collagen deposition during the repair process of skeletal muscle.Lasers in medical science · 2016Article
- Comprehensive Characterization of Glycosylation and Hydroxylation of Basement Membrane Collagen IV by High-Resolution Mass Spectrometry.Journal of proteome research · 2016Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Although type IV collagen is heavily glycosylated, the influence of this post-translational modification on integrin binding has not been investigated. In the present study, galactosylated and nongalactosylated triple-helical peptides have been constructed containing the α1(IV)382-393 and α1(IV)531-543 sequences, which are binding sites for the α2β1 and α3β1 integrins, respectively. All peptides had triple-helical stabilities of 37 °C or greater. The galactosylation of Hyl(393) in α1(IV)382-393 and Hyl(540) and Hyl(543) in α1(IV)531-543 had a dose-dependent influence on melanoma cell adhesion that was much more pronounced in the case of α3β1 integrin binding. Molecular modeling indicated that galactosylation occurred on the periphery of α2β1 integrin interaction with α1(IV)382-393 but right in the middle of α3β1 integrin interaction with α1(IV)531-543. The possibility of extracellular deglycosylation of type IV collagen was investigated, but no β-galactosidase-like activity capable of collagen modification was found. Thus, glycosylation of collagen can modulate integrin binding, and levels of glycosylation could be altered by reduction in expression of glycosylation enzymes but most likely not by extracellular deglycosylation activity.
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