ArticleThe Journal of biological chemistry2011
A novel functional role of collagen glycosylation: interaction with the endocytic collagen receptor uparap/ENDO180.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 86 citations in OpenAlex.
- The Recycling Collagen Receptor uPARAP Is a Unique Mediator of Stromal Drug Delivery to Carcinoma Cells.Molecular cancer therapeutics · 2026Article
- Collagen from Marine Sources for Potential Application in Wound Treatment.Progress in molecular and subcellular biology · 2026Review
- How Hydration Weakens Collagen: A Mesoscale Energy Decomposition of Type I and Type II Fibrils.Computational and structural biotechnology journal · 2026Article
- Collagen IV biosynthesis: Intracellular choreography of post-translational modifications.Matrix biology : journal of the International Society for Matrix Biology · 2025Review
- The life cycle of type IV collagen.Matrix biology : journal of the International Society for Matrix Biology · 2025Review
- The Tumour Glyco-Code: Sialylation as a Mediator of Stromal Cell Immunosuppression in the Tumour Microenvironment.European journal of immunology · 2025Review
- Is Exon Skipping a Viable Therapeutic Approach for Vascular Ehlers-Danlos Syndrome with Mutations inInternational journal of molecular sciences · 2024Article
- Impact of diabetes mellitus on osteoarthritis: a scoping review on biomarkers.Expert reviews in molecular medicine · 2024Article
- Glycosylation Modulates the Structure and Functions of Collagen: A Review.Molecules (Basel, Switzerland) · 2024Review
- Benzodiazepine Delorazepam Induces Locomotory Hyperactivity and Alterations in Pedal Mucus Texture in the Freshwater GastropodInternational journal of molecular sciences · 2023Article
- Framing Heartaches: The Cardiac ECM and the Effects of Age.International journal of molecular sciences · 2023Review
- Assessment of Collagen in Translational Models of Lung Research.Advances in experimental medicine and biology · 2023Article
- uPARAP/Endo180: a multifaceted protein of mesenchymal cells.Cellular and molecular life sciences : CMLS · 2022Review
- Identification and In Silico Characterization of a NovelInternational journal of molecular sciences · 2022Article
- Review
- Prokaryotic Collagen-Like Proteins as Novel Biomaterials.Frontiers in bioengineering and biotechnology · 2022Review
- 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
- Integrated proteomic, phosphoproteomic, and N-glycoproteomic analyses of theCurrent research in food science · 2022Article
- Exploring the cardiac ECM during fibrosis: A new era with next-gen proteomics.Frontiers in molecular biosciences · 2022Review
- Age-related type I collagen modifications reveal tissue-defining differences between ligament and tendon.Matrix biology plus · 2021Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Collagens make up the most abundant component of interstitial extracellular matrices and basement membranes. Collagen remodeling is a crucial process in many normal physiological events and in several pathological conditions. Some collagen subtypes contain specific carbohydrate side chains, the function of which is poorly known. The endocytic collagen receptor urokinase plasminogen activator receptor-associated protein (uPARAP)/Endo180 plays an important role in matrix remodeling through its ability to internalize collagen for lysosomal degradation. uPARAP/Endo180 is a member of the mannose receptor protein family. These proteins all include a fibronectin type II domain and a series of C-type lectin-like domains, of which only a minor part possess carbohydrate recognition activity. At least two of the family members, uPARAP/Endo180 and the mannose receptor, interact with collagens. The molecular basis for this interaction is known to involve the fibronectin type II domain but nothing is known about the function of the lectin domains in this respect. In this study, we have investigated a possible role of the single active lectin domain of uPARAP/Endo180 in the interaction with collagens. By expressing truncated recombinant uPARAP/Endo180 proteins and analyzing their interaction with collagens with high and low levels of glycosylation we demonstrated that this lectin domain interacts directly with glycosylated collagens. This interaction is functionally important because it was found to modulate the endocytic efficiency of the receptor toward highly glycosylated collagens such as basement membrane collagen IV. Surprisingly, this property was not shared by the mannose receptor, which internalized glycosylated collagens independently of its lectin function. This role of modulating its uptake efficiency by a specific receptor is a previously unrecognized function of collagen glycosylation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.