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

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

Research output: Contribution to journalArticlepeer-review

39 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)3601-3607
Number of pages7
JournalFEBS Letters
Issue number20
Publication statusPublished - 2012 Oct 19


  • Cathepsin L2
  • Cathepsin V
  • Glycosylation
  • Invasion
  • Trafficking

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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