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

Research output: Contribution to journalArticle

118 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)38885-38890
Number of pages6
JournalJournal of Biological Chemistry
Volume275
Issue number49
DOIs
Publication statusPublished - 2000 Dec 8

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Brevican
Matrix Metalloproteinase 1
Matrix Metalloproteinases
Aggrecans
Digestion
Chondroitin Sulfate Proteoglycans
Degradation
Metalloproteases
Proteoglycans
Cartilage
Neurology
Molecular mass
Sequence Analysis
ADAMTS4 Protein
aggrecanase
Central Nervous System
Membranes

ASJC Scopus subject areas

  • Biochemistry

Cite this

Nakamura, H., Fujii, Y., Inoki, I., Sugimoto, K., Tanzawa, K., Matsuki, H., ... Okada, Y. (2000). Brevican is degraded by matrix metalloproteinases and aggrecanase-1 (ADAMTS4) at different sites. Journal of Biological Chemistry, 275(49), 38885-38890. https://doi.org/10.1074/jbc.M003875200

Brevican is degraded by matrix metalloproteinases and aggrecanase-1 (ADAMTS4) at different sites. / Nakamura, Hiroyuki; Fujii, Yutaka; Inoki, Isao; Sugimoto, Kotaro; Tanzawa, Kazuhiko; Matsuki, Hirokazu; Miura, Ryu; Yamaguchi, Yu; Okada, Yasunori.

In: Journal of Biological Chemistry, Vol. 275, No. 49, 08.12.2000, p. 38885-38890.

Research output: Contribution to journalArticle

Nakamura, H, Fujii, Y, Inoki, I, Sugimoto, K, Tanzawa, K, Matsuki, H, Miura, R, Yamaguchi, Y & Okada, Y 2000, 'Brevican is degraded by matrix metalloproteinases and aggrecanase-1 (ADAMTS4) at different sites', Journal of Biological Chemistry, vol. 275, no. 49, pp. 38885-38890. https://doi.org/10.1074/jbc.M003875200
Nakamura, Hiroyuki ; Fujii, Yutaka ; Inoki, Isao ; Sugimoto, Kotaro ; Tanzawa, Kazuhiko ; Matsuki, Hirokazu ; Miura, Ryu ; Yamaguchi, Yu ; Okada, Yasunori. / Brevican is degraded by matrix metalloproteinases and aggrecanase-1 (ADAMTS4) at different sites. In: Journal of Biological Chemistry. 2000 ; Vol. 275, No. 49. pp. 38885-38890.
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