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

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

doi:10.1016/j.febslet.2012.08.001

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

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

Department of Applied Chemistry

Research output: Contribution to journal › Article › peer-review

39 Citations (Scopus)

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 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 language	English
Pages (from-to)	3601-3607
Number of pages	7
Journal	FEBS Letters
Volume	586
Issue number	20
DOIs	https://doi.org/10.1016/j.febslet.2012.08.001
Publication status	Published - 2012 Oct 19

Keywords

Cathepsin L2
Cathepsin V
Glycosylation
Invasion
Trafficking

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1016/j.febslet.2012.08.001

Cite this

@article{4398ae468db949d2b2a639d517b5c824,

title = "Determination of cathepsin v activity and intracellular trafficking by N-glycosylation",

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 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.",

keywords = "Cathepsin L2, Cathepsin V, Glycosylation, Invasion, Trafficking",

author = "Yuki Niwa and Takehiro Suzuki and Naoshi Dohmae and Kazuo Umezawa and Siro Simizu",

note = "Funding Information: The work described in this report was supported in part by Grants from the programs Grants-in-Aid for Scientific Research (B) and Grants-in-Aid for Scientific Research on Innovative Areas of the Ministry of Education, Culture, Sports, Science and Technology (MEXT) of Japan, and by the Keio Gijuku Fukuzawa Memorial Fund for the Advancement of Education and Research. ",

year = "2012",

month = oct,

day = "19",

doi = "10.1016/j.febslet.2012.08.001",

language = "English",

volume = "586",

pages = "3601--3607",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "Elsevier",

number = "20",

}

TY - JOUR

T1 - Determination of cathepsin v activity and intracellular trafficking by N-glycosylation

AU - Niwa, Yuki

AU - Suzuki, Takehiro

AU - Dohmae, Naoshi

AU - Umezawa, Kazuo

AU - Simizu, Siro

N1 - Funding Information: The work described in this report was supported in part by Grants from the programs Grants-in-Aid for Scientific Research (B) and Grants-in-Aid for Scientific Research on Innovative Areas of the Ministry of Education, Culture, Sports, Science and Technology (MEXT) of Japan, and by the Keio Gijuku Fukuzawa Memorial Fund for the Advancement of Education and Research.

PY - 2012/10/19

Y1 - 2012/10/19

N2 - 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.

AB - 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.

KW - Cathepsin L2

KW - Cathepsin V

KW - Glycosylation

KW - Invasion

KW - Trafficking

UR - http://www.scopus.com/inward/record.url?scp=84867577171&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84867577171&partnerID=8YFLogxK

U2 - 10.1016/j.febslet.2012.08.001

DO - 10.1016/j.febslet.2012.08.001

M3 - Article

C2 - 22967898

AN - SCOPUS:84867577171

SN - 0014-5793

VL - 586

SP - 3601

EP - 3607

JO - FEBS Letters

JF - FEBS Letters

IS - 20

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

Access to Document

Other files and links

Fingerprint

Cite this