Short CommunicationCharacterization of Human Matrilin-3 (MATN3)☆,☆☆
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Cited by (41)
A novel homozygous missense variant in MATN3 causes spondylo-epimetaphyseal dysplasia Matrilin 3 type in a consanguineous family
2020, European Journal of Medical GeneticsCitation Excerpt :It is caused by biallelic variants in MATN3 (OMIM# 602109) (Borochowitz et al., 2004). MATN3 is located on chromosome 2 and consists of eight exons (Belluoccio et al., 1998). It encodes a modular protein Matrilin-3 which is found specifically in the extracellular matrix of cartilage (Wagener et al., 2000).
Spondylo-epi-metaphyseal dysplasia due to a homozygous missense mutation in the gene encoding Matrilin-3 (T120M)
2020, Bone ReportsCitation Excerpt :The mechanism by which matrilins stabilise the ECM structure is by self-association to form supramolecular filamentous networks. Matrilin 1 and matrilin 3 are similar in terms of expression in the physis (growth plate) but the latter is different owing to its high expression during early development (Belluoccio et al., 1998). Matrilin 3, like other members of its family, consists of a vWFA domain, epidermal growth factor (EGFR) domain and a C-terminal coiled-coil domain (Frank et al., 2002), but unlike other members, is highly specific to cartilage tissue.
Measurement of matrilin-3 levels in human serum and synovial fluid using a competitive enzyme-linked immunosorbent assay
2012, Osteoarthritis and CartilageCitation Excerpt :Matrilin-3 (MATN3) is a skeletal-specific, tetrameric pericellular protein1–3, localizing to the pericellular matrix of chondrocytes.
Matrilin-3 switches from anti- to pro-anabolic upon integration to the extracellular matrix
2012, Matrix BiologyCitation Excerpt :MATN3 is one such skeletal-specific protein. MATN3 is tetrameric and localizes predominantly to the peri-cellular matrix of chondrocytes (Wagener et al., 1997; Belluoccio et al., 1998; Klatt et al., 2000; Klatt et al., 2011), acting as a scaffold for the assembly of fibrillar constituents of cartilage. MATN3 accumulates particularly in the ECM of osteoarthritic cartilage in human (Pullig et al., 2002).
Structural and functional characterization of recombinant matrilin-3 A-domain and implications for human genetic bone diseases
2007, Journal of Biological Chemistry
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Sequence data reported in this article have been deposited with the EMBL/GenBank/DDBJ Data Libraries under Accession No. AJ224741.
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K. E. KuettnerR. SchleyerbachJ. PeyronV. C. Hascall
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