Matrilin-2 interacts with itself and with other extracellular matrix proteins

Biochem J. 2002 Nov 1;367(Pt 3):715-21. doi: 10.1042/BJ20021069.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Base Sequence
  • Cell Line
  • Collagen Type I / metabolism
  • DNA Primers
  • Extracellular Matrix Proteins / metabolism*
  • Glycoproteins / metabolism*
  • Humans
  • Ligands
  • Matrilin Proteins
  • Microscopy, Electron
  • Protein Binding
  • Recombinant Proteins / metabolism
  • Skin / metabolism
  • Surface Plasmon Resonance


  • Collagen Type I
  • DNA Primers
  • Extracellular Matrix Proteins
  • Glycoproteins
  • Ligands
  • MATN2 protein, human
  • Matrilin Proteins
  • Recombinant Proteins