Determination of cathepsin v activity and intracellular trafficking by N-glycosylation

Yuki Niwa, Takehiro Suzuki, Naoshi Dohmae, Kazuo Umezawa, Siro Simizu

研究成果: Article査読

38 被引用数 (Scopus)

抄録

Cathepsin V (L2), a lysosomal cysteine protease, is a member of cathepsin family, relating to cancer invasion and metastasis. Cathepsin V contains two predicted N-glycosylation sites, but it has not been reported whether cathepsin V is glycosylated or not. In this study, we clarified the role of N-glycosylation of cathepsin V for its functions. We demonstrated that cathepsin V is N-glycosylated at both Asn221 and Asn292 using mass spectrometry and site-directed mutagenesis. N-glycosylation of cathepsin V was important for transportation to lysosome, secretion, and activity in HT1080 cells. These data demonstrated that functions of cathepsin V are controlled by N-glycosylation.

本文言語English
ページ(範囲)3601-3607
ページ数7
ジャーナルFEBS Letters
586
20
DOI
出版ステータスPublished - 2012 10月 19

ASJC Scopus subject areas

  • 生物理学
  • 構造生物学
  • 生化学
  • 分子生物学
  • 遺伝学
  • 細胞生物学

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