Determination of cathepsin V activity and intracellular trafficking by N-glycosylation.
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Niwa Y, Suzuki T, Dohmae N, Umezawa K, Simizu S
Determination of cathepsin V activity and intracellular trafficking by N-glycosylation.
FEBS Lett. 2012 Oct 19;586(20):3601-7. doi: 10.1016/j.febslet.2012.08.001. Epub 2012 Aug 9.
- PubMed ID
- 22967898 [ View in PubMed]
- Abstract
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 Asn(221) and Asn(292) 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.