Characterization of Human Matrilin-3 (MATN3)

Belluoccio, Daniele; Schenker, Thomas; Baici, Antonio; Trüeb, Beat

doi:10.1006/geno.1998.5519

Cited by 41 publications

(33 citation statements)

References 13 publications

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“…Matrilin-3 [Belluoccio et al, 1998] is the third member of a family of oligomeric extracellular matrix proteins [Deak et al, 1999]. The domain structure of the matrilin family of proteins is similar.…”

Section: Med and Matrilin-3 Defects (Edm5)mentioning

confidence: 99%

“…Mutations in COL9A3 [Paassilta et al, 1999b;Bonnemann et al, 2000;Lohiniva et al, 2000] Recent investigations in our laboratory have shown that mutations in the gene encoding matrilin 3 (MATN3), located on chromosome 2p24-23 can cause a distinctive form of mild MED Mortier et al, 2001]. Matrilin-3 is a member of the matrilin family of proteins [Belluoccio et al, 1998], which also comprise matrilin -1 (cartilage matrix protein), -2, and -4 , but a role for these latter genes in the pathology of MED remains to be determined.Previously, on the basis of pedigree structure, the existence of autosomal recessive forms of PSACH and MED had been proposed [Young and Moore, 1985;Wynne-Davies et al, 1986]. All available data now suggest that the apparently autosomal recessive forms of PSACH are actually the result of parental germline mosaicism for a dominant COMP mutation [Hall et al, 1987;Ferguson et al, 1997].…”

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confidence: 99%

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Pseudoachondroplasia and multiple epiphyseal dysplasia: Mutation review, molecular interactions, and genotype to phenotype correlations

2002

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Pseudoachondroplasia (PSACH) and multiple epiphyseal dysplasia (MED) constitute a bone dysplasia family, which is both genetically and phenotypically heterogeneous. The disease spectrum ranges from mild MED, which manifests with pain and stiffness in the joints and delayed and irregular ossification of the epiphyses, to the more severe PSACH, which is characterized by marked short stature, deformity of the legs, and ligamentous laxity. PSACH is almost exclusively caused by mutations in cartilage oligomeric matrix protein (COMP) whereas various forms of MED are caused by mutations in the genes encoding COMP, type IX collagen (COL9A1, COL9A2, and COL9A3), matrilin-3 (MATN3), and solute carrier member 26, member 2 gene (SLC26A2). In this review we discuss specific disease-causing mutations and the clustering of these mutations in functionally and structurally important regions of the respective gene products, genotype to phenotype correlations, and the diagnostic relevance of mutation screening in these osteochondrodysplasias.

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Section: Med and Matrilin-3 Defects (Edm5)mentioning

confidence: 99%

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confidence: 99%

Pseudoachondroplasia and multiple epiphyseal dysplasia: Mutation review, molecular interactions, and genotype to phenotype correlations

2002

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“…We have recently set out to identify and characterize novel cartilage proteins by a subtractive cDNA cloning approach (6,7). Special emphasis was put on regulatory proteins that might play a role during chondrocyte proliferation and differentiation.…”

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confidence: 99%

“…In addition, our libraries contained several novel clones whose sequences have not yet been stored in public data banks. Some of the novel clones coded for a structural protein that was highly related to the family of the matrilins (6,7). Another set of clones was found to code for a novel transmembrane protein related to members of the fibroblast growth factor receptor family.…”

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confidence: 99%

Characterization of FGFRL1, a Novel Fibroblast Growth Factor (FGF) Receptor Preferentially Expressed in Skeletal Tissues

Trüeb

Zhuang

Taeschler

et al. 2003

Journal of Biological Chemistry

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Clones for a novel transmembrane receptor termed FGFRL1 were isolated from a subtracted, cartilage-specific cDNA library prepared from chicken sterna. Homologous sequences were identified in other vertebrates, including man, mouse, rat and fish, but not in invertebrates such as Caenorhabditis elegans and Drosophila. FGFRL1 was expressed preferentially in skeletal tissues as demonstrated by Northern blotting and in situ hybridization. Small amounts of the FGFRL1 mRNA were also detected in other tissues such as skeletal muscle and heart. The novel protein contained three extracellular Ig-like domains that were related to the members of the fibroblast growth factor (FGF) receptor family. However, it lacked the intracellular protein tyrosine kinase domain required for signal transduction by transphosphorylation. When expressed in cultured cells as a fusion protein with green fluorescent protein, FGFRL1 was specifically localized to the plasma membrane where it might interact with FGF ligands. Recombinant FGFRL1 protein was produced in a baculovirus system with intact disulfide bonds. Similar to FGF receptors, the expressed protein interacted specifically with heparin and with FGF2. When overexpressed in MG-63 osteosarcoma cells, the novel receptor had a negative effect on cell proliferation. Taken together our data are consistent with the view that FGFRL1 acts as a decoy receptor for FGF ligands.Most bones of the vertebrate skeleton are formed by a complex process termed endochondral ossification which involves a cartilage intermediate (1). This intermediate represents a highly specialized connective tissue. It consists of a single cell type, the chondrocytes, which are embedded in a rich extracellular matrix (2). Typically, this matrix makes up more than 90% of the cartilage volume and consists of collagens (types II, IX, X, and XI), proteoglycans (aggrecan, small leucine-rich proteins), and glycoproteins (matrilins, COMP).During the first step of endochondral ossification, mesenchymal cells condense and differentiate into chondrocytes (3). These chondrocytes proliferate rapidly and lay down the cartilaginous model of the future bones. The chondrocytes undergo a complex series of distinct developmental stages, including proliferation, maturation, and hypertrophy. The hypertrophic cartilage is calcified and becomes vascularized. Finally, the calcified cartilage is invaded by osteoclasts and osteoblasts, which replace the cartilaginous tissue by bone.Cartilage has become a popular tissue to study cell proliferation and differentiation in vitro (3). When cultivated on plastic dishes, chondrocytes rapidly dedifferentiate into fibroblast-like cells. In three-dimensional lattices, however, the chondrocytes undergo the ordered sequence of events observed during differentiation and maturation of cartilage in vivo. Three stages of chondrocyte differentiation have been defined in vitro: proliferative chondrocytes producing mainly collagen II, hypertrophic chondrocytes producing collagen X, and osteoblast-like cells producing...

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“…In vitro studies of MATN-3 identified its anti-anabolic and pro-catabolic functions, suggesting that it plays an important role in OA (22,23 Two studies conducted by Vincourt et al (25,26) revealed higher levels of MATN-3 in both the serum and synovial fluid of OA patients.…”

Section: Discussionmentioning

confidence: 99%

Clinical significance of Matrilin-3 gene polymorphism in Egyptian patients with primary knee osteoarthritis

et al. 2017

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Characterization of Human Matrilin-3 (MATN3)

Cited by 41 publications

References 13 publications

Pseudoachondroplasia and multiple epiphyseal dysplasia: Mutation review, molecular interactions, and genotype to phenotype correlations

Pseudoachondroplasia and multiple epiphyseal dysplasia: Mutation review, molecular interactions, and genotype to phenotype correlations

Characterization of FGFRL1, a Novel Fibroblast Growth Factor (FGF) Receptor Preferentially Expressed in Skeletal Tissues

Clinical significance of Matrilin-3 gene polymorphism in Egyptian patients with primary knee osteoarthritis

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