Elsevier

Genomics

Volume 53, Issue 3, 1 November 1998, Pages 391-394
Genomics

Short Communication
Characterization of Human Matrilin-3 (MATN3),☆☆

https://doi.org/10.1006/geno.1998.5519Get rights and content

Abstract

We have isolated a cDNA clone for human matrilin-3 from a cartilage-specific cDNA library. The polypeptide predicted from the nucleotide sequence of this clone shared 83% identity with matrilin-3 from mouse and 61% with that from chicken. It was composed of 486 amino acid residues that were arranged in seven domains: a signal peptide, a von Willebrand factor A domain, four EGF repeats, and an α-helical region. The gene for human matrilin-3 (MATN3) was assigned to chromosome region 2p24–p23. The corresponding mRNA of 2.8 kb was expressed in every type of cartilage investigated thus far. It was also producedin vitroby primary chondrocytes isolated from articular cartilage. However, dedifferentiated chondrocytes of the third passage did not express it at all. Matrilin-3 might therefore serve as a marker for the differentiation state of chondrocytes.

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    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

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    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).

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Sequence data reported in this article have been deposited with the EMBL/GenBank/DDBJ Data Libraries under Accession No. AJ224741.

☆☆

K. E. KuettnerR. SchleyerbachJ. PeyronV. C. Hascall

1

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