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A more recent version of this article appeared on June 30, 2006
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Papers In Press, published online ahead of print April 28, 2006
J. Biol. Chem, 10.1074/jbc.M510330200
Submitted on September 20, 2005
Revised on April 26, 2006
Accepted on April 28, 2006

Versican/PG-M aggregates in cartilage: identification and characterization

Kazu Matsumoto, Nobuhiro Kamiya, Keittisak Suwan, Fukiko Atsumi, Katsuji Shimizu, Tamayuki Shinomura, Yoshihiko Yamada, Koji Kimata, and Hideto Watanabe

Institute for Molecular Science of Medicine, Aichi Med Univ, Nagakute-chou, Aichi-gun 480-1195

Corresponding Author: wannabee{at}aichi-med-u.ac.jp

Versican/PG-M is a large chondroitin sulfate proteoglycan of the extracellular matrix with a common domain structure to aggrecan, and is present in cartilage at low levels. Here, we characterized cartilage versican during development and growth. Immunostaining showed that versican was mainly localized in the interterritorial zone of the articular surface at two weeks in mice, whereas aggrecan was in the pericellular zone of prehypertrophic and hypertrophic cells of the growth plate. Although its transcription level rapidly diminished during growth, versican remained in the articular cartilage. Biochemical analysis of normal articular cartilage and aggrecan-null cartilage from cmd/cmd mice revealed that versican was present as a proteoglycan aggregate with both link protein (LP) and hyaluronan (HA). Chondroitin sulfate chains of versican digested with chondroitinase ABC contained 71% non-sulfated and 28% 4-sulfated unsaturated disaccharides, whereas those of aggrecan contained 25% nonsulfated and 70% 4-sulfated. LP overexpression in chondrocytic N1511 cells at the early stage of differentiation, in which versican is expressed, enhanced versican deposition in the matrix and prevented subsequent aggrecan deposition. These results suggest that versican is present as an aggregate distinct from the aggrecan aggregate and may play specific roles in the articular surface.


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