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J. Biol. Chem., Vol. 276, Issue 20, 17267-17275, May 18, 2001
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From the Institute for Biochemistry and the Matrilin-4 is the most recently identified member
of the matrilin family of von Willebrand factor A-like domain
containing extracellular matrix adapter proteins. Full-length
matrilin-4 was expressed in 293-EBNA cells, purified using affinity
tags, and subjected to biochemical characterization. The largest
oligomeric form of recombinantly expressed full-length matrilin-4 is a
trimer as shown by electron microscopy, SDS-polyacrylamide gel
electrophoresis, and mass spectrometry. Proteolytically processed
matrilin-4 species were also detected. The cleavage occurs in the short
linker region between the second von Willebrand factor A-like domain
and the coiled-coil domain leading to the release of large fragments
and the formation of dimers and monomers of intact subunits still containing a trimeric coiled-coil. In immunoblots of calvaria extracts
similar degradation products could be detected, indicating that a
related proteolytic processing occurs in vivo. Matrilin-4 was first observed at day 7.5 post-coitum in mouse embryos.
Affinity-purified antibodies detect a broad expression in dense and
loose connective tissue, bone, cartilage, central and peripheral
nervous systems and in association with basement membranes. In the
matrix formed by cultured primary embryonic fibroblasts, matrilin-4 is
found in a filamentous network connecting individual cells.
Molecular Structure, Processing, and Tissue Distribution of
Matrilin-4*
, Center
for Molecular Medicine Cologne Service Laboratory, Medical Faculty,
University of Cologne, Joseph-Stelzmann-Strasse 52, D-50931 Cologne, Germany
*
This work was supported by Deutsche Forschungsgemeinschaft
Grant WA 1338/2-1 and by Köln Fortune program of the Medical
Faculty of the University of Cologne.The costs of publication of this article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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