Brevican is degraded by matrix metalloproteinases and aggrecanase-1 (ADAMTS4) at different sites

Hiroyuki Nakamura, Yutaka Fujii, Isao Inoki, Kotaro Sugimoto, Kazuhiko Tanzawa, Hirokazu Matsuki, Ryu Miura, Yu Yamaguchi, Yasunori Okada

研究成果: Article査読

133 被引用数 (Scopus)

抄録

Brevican is a member of the lectican family of chondroitin sulfate proteoglycans that is predominantly expressed in the central nervous system. The susceptibility of brevican to digestion by matrix metalloproteinases (MMP-1, -2, -3, -7, -8, -9, -10, and -13 and membrane type 1 and 3 MMPs) and aggrecanase-1 (ADAMTS4) was examined. MMP-1, -2, -3, -7, -8, -10, and -13 degraded brevican into a few fragments with similar molecular masses, whereas the degradation products of aggrecanase-1 had apparently different sizes. NH2-terminal sequence analyses of the digestion fragments revealed that cleavages of the brevican core protein by these metalloproteinases occurred commonly within the central non-homologous domain. MMP-1, -2, -3, -7, -8, -10, and -13 preferentially attacked the Ala360-Phe361 bond, whereas aggrecanase-1 cleaved the Glu395-Ser396 bond, which are similar to the cleavage sites observed with cartilage proteoglycan (aggrecan) for the MMPs and aggrecanase-1, respectively. These data demonstrate that MMP-1, -2, -3, -7, -8, -10, and -13 and aggrecanase-1 digest brevican in a similar pattern to aggrecan and suggest that they may be responsible for the physiological turnover and pathological degradation of brevican.

本文言語English
ページ(範囲)38885-38890
ページ数6
ジャーナルJournal of Biological Chemistry
275
49
DOI
出版ステータスPublished - 2000 12 8

ASJC Scopus subject areas

  • 生化学
  • 分子生物学
  • 細胞生物学

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