ArticleMolecular biology of the cell1999
Assembly of a novel cartilage matrix protein filamentous network: molecular basis of differential requirement of von Willebrand factor A domains.
Article in Molecular biology of the cell, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers, 1 of them a synthesis that pooled it.
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Who cites it
18 citing papers in PubMed, 1 synthesis or guideline pooled it, 71 citations in OpenAlex.
- The association of rs1149048 polymorphism in matrilin-1(MATN1) gene with adolescent idiopathic scoliosis susceptibility: a meta-analysis.Molecular biology reports · 2014Pooled it
- Valproic acid modulates collagen architecture in the postoperative conjunctival scar.Journal of molecular medicine (Berlin, Germany) · 2022Article
- Mice Lacking the Matrilin Family of Extracellular Matrix Proteins Develop Mild Skeletal Abnormalities and Are Susceptible to Age-Associated Osteoarthritis.International journal of molecular sciences · 2020Article
- Matrilin-2 is proteolytically cleaved by ADAMTS-4 and ADAMTS-5.Molecules (Basel, Switzerland) · 2014Article
- Matrilin-1 is an inhibitor of neovascularization.The Journal of biological chemistry · 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
- The genetic epidemiology of idiopathic scoliosis.European spine journal : official publication of the European Spine Society, the European Spinal Deformity Society, and the European Section of the Cervical Spine Research Society · 2012Review
- Structural and functional investigations of Matrilin-1 A-domains reveal insights into their role in cartilage ECM assembly.The Journal of biological chemistry · 2010Article
- Proteolytic processing causes extensive heterogeneity of tissue matrilin forms.The Journal of biological chemistry · 2009Article
- Promoter polymorphism of matrilin-1 gene predisposes to adolescent idiopathic scoliosis in a Chinese population.European journal of human genetics : EJHG · 2009Article
- Multiple functions of the von Willebrand Factor A domain in matrilins: secretion, assembly, and proteolysis.Journal of orthopaedic surgery and research · 2008Article
- Structural and functional characterization of recombinant matrilin-3 A-domain and implications for human genetic bone diseases.The Journal of biological chemistry · 2007Article
- Functional knockout of the matrilin-3 gene causes premature chondrocyte maturation to hypertrophy and increases bone mineral density and osteoarthritis.The American journal of pathology · 2006Article
- Highly conserved proximal promoter element harbouring paired Sox9-binding sites contributes to the tissue- and developmental stage-specific activity of the matrilin-1 gene.The Biochemical journal · 2005Article
- Matrilin-3 is dispensable for mouse skeletal growth and development.Molecular and cellular biology · 2004Article
- Matrilin-2 interacts with itself and with other extracellular matrix proteins.The Biochemical journal · 2002Article
- Distribution and evolution of von Willebrand/integrin A domains: widely dispersed domains with roles in cell adhesion and elsewhere.Molecular biology of the cell · 2002Review
- Normal skeletal development of mice lacking matrilin 1: redundant function of matrilins in cartilage?Molecular and cellular biology · 1999Article
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
Cartilage matrix protein (CMP) is the prototype of the newly discovered matrilin family, all of which contain von Willebrand factor A domains. Although the function of matrilins remain unclear, we have shown that, in primary chondrocyte cultures, CMP (matrilin-1) forms a filamentous network, which is made up of two types of filaments, a collagen-dependent one and a collagen-independent one. In this study, we demonstrate that the collagen-independent CMP filaments are enriched in pericellular compartments, extending directly from chondrocyte membranes. Their morphology can be distinguished from that of collagen filaments by immunogold electron microscopy, and mimicked by that of self-assembled purified CMP. The assembly of CMP filaments can occur from transfection of a wild-type CMP transgene alone in skin fibroblasts, which do not produce endogenous CMP. Conversely, assembly of endogenous CMP filaments by chondrocytes can be inhibited specifically by dominant negative CMP transgenes. The two A domains within CMP serve essential but different functions during network formation. Deletion of the A2 domain converts the trimeric CMP into a mixture of monomers, dimers, and trimers, whereas deletion of the A1 domain does not affect the trimeric configuration. This suggests that the A2 domain modulates multimerization of CMP. Absence of either A domain from CMP abolishes its ability to form collagen-independent filaments. In particular, Asp22 in A1 and Asp255 in A2 are essential; double point mutation of these residues disrupts CMP network formation. These residues are part of the metal ion-dependent adhesion sites, thus a metal ion-dependent adhesion site-mediated adhesion mechanism may be applicable to matrilin assembly. Taken together, our data suggest that CMP is a bridging molecule that connects matrix components in cartilage to form an integrated matrix network.
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