ArticleThe Biochemical journal2002
Matrilin-2 interacts with itself and with other extracellular matrix proteins.
Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 61 citations in OpenAlex.
- Differential activity of transcription factors and neuronal effectors during the development of pikeperch brain.Biology open · 2025Article
- Matrilin-2 with a K-Chitosan Scaffold Enhances Functional Recovery and Nerve Regeneration in a Segmental Rat Sciatic Nerve Injury Model.Pharmaceuticals (Basel, Switzerland) · 2025Article
- Genome-Wide Association Study of Gallstone Disease Identifies Novel Candidate Genomic Variants in a Latino Community of Southwest USA.Journal of racial and ethnic health disparities · 2025Article
- Basonuclin-2 regulates extracellular matrix production and degradation.Life science alliance · 2023Article
- Review
- Matrilin-2 within a three-dimensional lysine-modified chitosan porous scaffold enhances Schwann cell migration and axonal outgrowth for peripheral nerve regeneration.Frontiers in bioengineering and biotechnology · 2023Article
- Monocytes augment inflammatory responses in human aortic valve interstitial cells via βInflammation research : official journal of the European Histamine Research Society ... [et al.] · 2022Article
- Valproic acid modulates collagen architecture in the postoperative conjunctival scar.Journal of molecular medicine (Berlin, Germany) · 2022Article
- A basement membrane discovery pipeline uncovers network complexity, regulators, and human disease associations.Science advances · 2022Article
- Initial WNT/β-Catenin Activation Enhanced Mesoderm Commitment, Extracellular Matrix Expression, Cell Aggregation and Cartilage Tissue Yield From Induced Pluripotent Stem Cells.Frontiers in cell and developmental biology · 2020Article
- Yersinia pestis YopK Inhibits Bacterial Adhesion to Host Cells by Binding to the Extracellular Matrix Adaptor Protein Matrilin-2.Infection and immunity · 2017Article
- Characterization of recombinantly expressed matrilin VWA domains.Protein expression and purification · 2015Article
- Extracellular deposition of matrilin-2 controls the timing of the myogenic program during muscle regeneration.Journal of cell science · 2014Article
- Matrilin-2 is proteolytically cleaved by ADAMTS-4 and ADAMTS-5.Molecules (Basel, Switzerland) · 2014Article
- Matrilin-2 is a widely distributed extracellular matrix protein and a potential biomarker in the early stage of osteoarthritis in articular cartilage.BioMed research international · 2014Article
- Lack of Matrilin-2 favors liver tumor development via Erk1/2 and GSK-3β pathways in vivo.PloS one · 2014Article
- Fibrillin-2, tenascin-C, matrilin-2, and matrilin-4 are strongly expressed in the epithelium of human granular and lattice type I corneal dystrophies.Molecular vision · 2012Article
- Article
- Defining elastic fiber interactions by molecular fishing: an affinity purification and mass spectrometry approach.Molecular & cellular proteomics : MCP · 2009Article
- Compositional differences between infant and adult human corneal basement membranes.Investigative ophthalmology & visual science · 2007Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Matrilin-2 is a component of extracellular filamentous networks. To study the interactions by which it can be integrated into such assemblies, full-length and truncated forms of matrilin-2 were recombinantly expressed in HEK-293 cells and purified from conditioned medium. The recombinant proteins, when used in interaction assays, showed affinity to matrilin-2 itself, but also to other collagenous and non-collagenous extracellular matrix proteins. The interaction between matrilin-2 and collagen I was studied in greater detail and could be shown to occur at distinct sites on the collagen I molecule and to have a K (D) of about 3 x 10(-8) M. Interactions with some non-collagenous protein ligands were even stronger, with matrilin-2 binding to fibrillin-2, fibronectin and laminin-1-nidogen-1 complexes, with K (D) values in the range of 10(-8)-10(-11) M. Co-localization of matrilin-2 with these ligands in the dermal-epidermal basement membrane, in the microfibrils extending from the basement membrane into the dermis, and in the dermal extracellular matrix, indicates a physiological relevance of the interactions in the assembly of supramolecular extracellular matrix structures.
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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.