ArticleThe Journal of biological chemistry2013
Homotypic versican G1 domain interactions enhance hyaluronan incorporation into fibrillin microfibrils.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 19 citations in OpenAlex.
- Extracellular matrix remodeling in calcific aortic valve disease: Localized enrichment of type III collagen and LTBP-4.Matrix biology plus · 2026Article
- Desmosine: The Rationale for Its Use as a Biomarker of Therapeutic Efficacy in the Treatment of Pulmonary Emphysema.Diagnostics (Basel, Switzerland) · 2025Article
- The Role of the Extracellular Matrix in the Pathogenesis and Treatment of Pulmonary Emphysema.International journal of molecular sciences · 2024Review
- Defining the versican interactome in lung health and disease.American journal of physiology. Cell physiology · 2022Review
- Noncovalent hyaluronan crosslinking by TSG-6: Modulation by heparin, heparan sulfate, and PRG4.Frontiers in molecular biosciences · 2022Article
- Versican G1 domain enhances adenoviral-mediated transgene expression and can be modulated by inhibitors of the Janus kinase (JAK)/STAT and Src family kinase pathways.The Journal of biological chemistry · 2017Article
- Fell-Muir Lecture: Fibrillin microfibrils: structural tensometers of elastic tissues?International journal of experimental pathology · 2017Review
- G1 Domain of Versican Regulates Hyaluronan Organization and the Phenotype of Cultured Human Dermal Fibroblasts.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2016Article
- Versican and the regulation of cell phenotype in disease.Biochimica et biophysica acta · 2014Review
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Authors and funding
7 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Versican G1 domain-containing fragments (VG1Fs) have been identified in extracts from the dermis in which hyaluronan (HA)-versican-fibrillin complexes are found. However, the molecular assembly of VG1Fs in the HA-versican-microfibril macrocomplex has not yet been elucidated. Here, we clarify the role of VG1Fs in the extracellular macrocomplex, specifically in mediating the recruitment of HA to microfibrils. Sequential extraction studies suggested that the VG1Fs were not associated with dermal elements through HA binding properties alone. Overlay analyses of dermal tissue sections using the recombinant versican G1 domain, rVN, showed that rVN deposited onto the elastic fiber network. In solid-phase binding assays, rVN bound to isolated nondegraded microfibrils. rVN specifically bound to authentic versican core protein produced by dermal fibroblasts. Furthermore, rVN bound to VG1Fs extracted from the dermis and to nondenatured versican but not to fibrillin-1. Homotypic binding of rVN was also seen. Consistent with these binding properties, macroaggregates containing VG1Fs were detected in high molecular weight fractions of sieved dermal extracts and visualized by electron microscopy, which revealed localization to microfibrils at the microscopic level. Importantly, exogenous rVN enhanced HA recruitment both to isolated microfibrils and to microfibrils in tissue sections in a dose-dependent manner. From these data, we propose that cleaved VG1Fs can be recaptured by microfibrils through VG1F homotypical interactions to enhance HA recruitment to microfibrils.
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