Matrilin-2, a large, oligomeric matrix protein, is expressed by a great variety of cells and forms fibrillar networks

Dorothea Piecha, Selen Muratoglu, Matthias Mörgelin, Nik Hauser, Daniel Studer, Ibolya Kiss, Mats Paulsson, Ferenc Deák

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Matrilin-2 is a member of the protein superfamily with yon Willebrand factor type A-like modules. Mouse matrilin-2 cDNA fragments were expressed in 293-EBNA cells, and the protein was purified, characterized, and used to immunize rabbits. The affinity-purified antiserum detects matrilin-2 in dense and loose connective tissue structures, subepithelial connective tissue of the skin and digestive tract, specialized cartilages, and blood vessel walls. In situ hybridization of 35S-labeled riboprobes localizes the matrilin-2 mRNA to fibroblasts of dermis, tendon, ligaments, perichondrium, and periosteum; connective tissue elements in the heart; smooth muscle cells; and epithelia and loose connective tissue cells of the alimentary canal and respiratory tract. RNA blot hybridization and immunoblotting revealed both matrilin-2 mRNA and protein in cultures of a variety of cell types, confirming the tissue distribution. Alternative splicing affects a module unique for matrilin-2 in all of the above RNA sources, SDS-polyacrylamide gel electrophoresis and electron microscopy reveals matrilin-2 from tissue extracts and cell line cultures as a mixture of mono-, di-, tri-, and tetramers. Matrilin-2 is substituted with N-linked oligosaccharides but not with glycosaminoglycans. Because of other, yet unidentified, cell-type dependent posttranslational modifications, the monomer is heterogeneous in size. Immunofluorescence showed that matrilin-2 functions by forming an extracellular, filamentous network.

Original languageEnglish
Pages (from-to)13353-13361
Number of pages9
JournalJournal of Biological Chemistry
Issue number19
Publication statusPublished - May 7 1999


ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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