ArticleThe Journal of biological chemistry2016
Heterogeneity of Collagen VI Microfibrils: STRUCTURAL ANALYSIS OF NON-COLLAGENOUS REGIONS.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 30 citations in OpenAlex.
- The potential role of GLP-1 receptor agonists in the management of psoriatic disease: a scoping review.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2025Article
- Collagen VI microfibril structure reveals mechanism for molecular assembly and clustering of inherited pathogenic mutations.Nature communications · 2025Article
- Revealing the Solution Conformation and Hydration Structure of Type I Tropocollagen Using X-ray Scattering and Molecular Dynamics Simulation.Biomacromolecules · 2025Article
- Endotrophin, a Key Marker and Driver for Fibroinflammatory Disease.Endocrine reviews · 2024Review
- The coordinated activities of collagen VI and XII in maintenance of tissue structure, function and repair: evidence for a physical interaction.Frontiers in molecular biosciences · 2024Article
- Ageing of skeletal muscle extracellular matrix and mitochondria: finding a potential link.Annals of medicine · 2023Review
- Article
- Structural studies of elastic fibre and microfibrillar proteins.Matrix biology plus · 2021Article
- The critical role of collagen VI in lung development and chronic lung disease.Matrix biology plus · 2021Review
- Structure of a collagen VI α3 chain VWA domain array: adaptability and functional implications of myopathy causing mutations.The Journal of biological chemistry · 2020Article
- Skeletal Muscle Extracellular Matrix - What Do We Know About Its Composition, Regulation, and Physiological Roles? A Narrative Review.Frontiers in physiology · 2020Review
- Spatio-temporal expression and distribution of collagen VI during zebrafish development.Scientific reports · 2019Article
- C-terminal proteolysis of the collagen VI α3 chain by BMP-1 and proprotein convertase(s) releases endotrophin in fragments of different sizes.The Journal of biological chemistry · 2019Article
- Extracellular Distribution of Collagen II and Perifibrillar Adapter Proteins in Healthy and Osteoarthritic Human Knee Joint Cartilage.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2017Article
- Defining the hierarchical organisation of collagen VI microfibrils at nanometre to micrometre length scales.Acta biomaterialia · 2017Article
- Fell Muir Lecture: Collagen fibril formation in vitro and in vivo.International journal of experimental pathology · 2017Review
- Local effects of adipose tissue in psoriasis and psoriatic arthritis.Psoriasis (Auckland, N.Z.)Review
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Authors and funding
8 authors at 5 institutions in 5 countries.
Funding
Abstract
Collagen VI, a collagen with uncharacteristically large N- and C-terminal non-collagenous regions, forms a distinct microfibrillar network in most connective tissues. It was long considered to consist of three genetically distinct α chains (α1, α2, and α3). Intracellularly, heterotrimeric molecules associate to form dimers and tetramers, which are then secreted and assembled to microfibrils. The identification of three novel long collagen VI α chains, α4, α5, and α6, led to the question if and how these may substitute for the long α3 chain in collagen VI assembly. Here, we studied structural features of the novel long chains and analyzed the assembly of these into tetramers and microfibrils. N- and C-terminal globular regions of collagen VI were recombinantly expressed and studied by small angle x-ray scattering (SAXS). Ab initio models of the N-terminal globular regions of the α4, α5, and α6 chains showed a C-shaped structure similar to that found for the α3 chain. Single particle EM nanostructure of the N-terminal globular region of the α4 chain confirmed the C-shaped structure revealed by SAXS. Immuno-EM of collagen VI extracted from tissue revealed that like the α3 chain the novel long chains assemble to homotetramers that are incorporated into mixed microfibrils. Moreover, SAXS models of the C-terminal globular regions of the α1, α2, α4, and α6 chains were generated. Interestingly, the α1, α2, and α4 C-terminal globular regions dimerize. These self-interactions may play a role in tetramer formation.
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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.