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Volumn 586, Issue 20, 2012, Pages 3601-3607

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

Author keywords

Cathepsin L2; Cathepsin V; Glycosylation; Invasion; Trafficking

Indexed keywords

ASPARAGINE; CATHEPSIN V;

EID: 84867577171     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2012.08.001     Document Type: Article
Times cited : (41)

References (26)
  • 2
    • 1642453678 scopus 로고    scopus 로고
    • Secretion of heparanase protein is regulated by glycosylation in human tumor cell lines
    • S. Simizu, K. Ishida, M.K. Wierzba, and H. Osada Secretion of heparanase protein is regulated by glycosylation in human tumor cell lines J. Biol. Chem. 279 2004 2697 2703
    • (2004) J. Biol. Chem. , vol.279 , pp. 2697-2703
    • Simizu, S.1    Ishida, K.2    Wierzba, M.K.3    Osada, H.4
  • 3
    • 70350445903 scopus 로고    scopus 로고
    • Therapeutically targeting protein-glycan interactions
    • A. Rek, E. Krenn, and A.J. Kungl Therapeutically targeting protein-glycan interactions Br. J. Pharmacol. 157 2009 686 694
    • (2009) Br. J. Pharmacol. , vol.157 , pp. 686-694
    • Rek, A.1    Krenn, E.2    Kungl, A.J.3
  • 4
    • 43049179836 scopus 로고    scopus 로고
    • Dolichol-phosphate mannose synthase: Structure, function and regulation
    • Y. Maeda, and T. Kinoshita Dolichol-phosphate mannose synthase: structure, function and regulation Biochim. Biophys. Acta 1780 2008 861 868
    • (2008) Biochim. Biophys. Acta , vol.1780 , pp. 861-868
    • Maeda, Y.1    Kinoshita, T.2
  • 5
    • 33751508817 scopus 로고    scopus 로고
    • N-glycan processing in ER quality control
    • L.W. Ruddock, and M. Molinari N-glycan processing in ER quality control J. Cell Sci. 119 2006 4373 4380
    • (2006) J. Cell Sci. , vol.119 , pp. 4373-4380
    • Ruddock, L.W.1    Molinari, M.2
  • 8
    • 0032522413 scopus 로고    scopus 로고
    • Cathepsin L2, a novel human cysteine proteinase produced by breast and colorectal carcinomas
    • I. Santamaría, G. Velasco, M. Cazorla, A. Fueyo, E. Campo, and C. López-Otín Cathepsin L2, a novel human cysteine proteinase produced by breast and colorectal carcinomas Cancer Res. 58 1998 1624 1630
    • (1998) Cancer Res. , vol.58 , pp. 1624-1630
    • Santamaría, I.1    Velasco, G.2    Cazorla, M.3    Fueyo, A.4    Campo, E.5    López-Otín, C.6
  • 10
    • 0028143072 scopus 로고
    • Subcellular localization and targeting of cathepsin e
    • E.M. Finley, and S. Kornfeld Subcellular localization and targeting of cathepsin E J. Biol. Chem. 269 1994 31259 31266
    • (1994) J. Biol. Chem. , vol.269 , pp. 31259-31266
    • Finley, E.M.1    Kornfeld, S.2
  • 11
    • 0028360298 scopus 로고
    • Identification of the U-937 membrane-associated proteinase interacting with the V3 loop of HIV-1 gp120 as cathepsin G
    • L.E. Avril, M. Di Martino-Ferrer, G. Pignede, M. Séman, and F. Gauthier Identification of the U-937 membrane-associated proteinase interacting with the V3 loop of HIV-1 gp120 as cathepsin G FEBS Lett. 345 1994 81 86
    • (1994) FEBS Lett. , vol.345 , pp. 81-86
    • Avril, L.E.1    Di Martino-Ferrer, M.2    Pignede, G.3    Séman, M.4    Gauthier, F.5
  • 13
    • 0035801514 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: Facts and opportunities
    • V. Turk, B. Turk, and D. Turk Lysosomal cysteine proteases: facts and opportunities EMBO J. 20 2001 4629 4633
    • (2001) EMBO J. , vol.20 , pp. 4629-4633
    • Turk, V.1    Turk, B.2    Turk, D.3
  • 17
    • 0038687865 scopus 로고    scopus 로고
    • Human cathepsin v functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization
    • D. Brömme, Z. Li, M. Barnes, and E. Mehler Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization Biochemistry 38 1999 2377 2385
    • (1999) Biochemistry , vol.38 , pp. 2377-2385
    • Brömme, D.1    Li, Z.2    Barnes, M.3    Mehler, E.4
  • 18
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • S.N. Ho, H.D. Hunt, R.M. Horton, J.K. Pullen, and L.R. Pease Site-directed mutagenesis by overlap extension using the polymerase chain reaction Gene 77 1989 51 59
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 19
    • 0019424254 scopus 로고
    • Studies on a new proteolytic enzyme from A chromobacter lyticus M497-1. I. Purification and some enzymatic properties
    • T. Masaki, M. Tanabe, K. Nakamura, and M. Soejima Studies on a new proteolytic enzyme from A chromobacter lyticus M497-1. I. Purification and some enzymatic properties Biochim. Biophys. Acta 660 1981 44 50
    • (1981) Biochim. Biophys. Acta , vol.660 , pp. 44-50
    • Masaki, T.1    Tanabe, M.2    Nakamura, K.3    Soejima, M.4
  • 20
    • 0019948262 scopus 로고
    • L-trans-Epoxysuccinyl-leucylamido (4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L
    • A.J. Barrett, A.A. Kembhavi, M.A. Brown, H. Kirschke, C.G. Knight, M. Tamai, and K. Hanada L-trans-Epoxysuccinyl-leucylamido (4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L Biochem. J. 201 1982 189 198
    • (1982) Biochem. J. , vol.201 , pp. 189-198
    • Barrett, A.J.1    Kembhavi, A.A.2    Brown, M.A.3    Kirschke, H.4    Knight, C.G.5    Tamai, M.6    Hanada, K.7
  • 21
    • 0018803824 scopus 로고
    • Mechanism of action of tunicamycin on the UDP-GlcNAc:dolichyl-phosphate Glc-NAc-1-phosphate transferase
    • A. Heifetz, R.W. Keenan, and A.D. Elbein Mechanism of action of tunicamycin on the UDP-GlcNAc:dolichyl-phosphate Glc-NAc-1-phosphate transferase Biochemistry 18 1979 2186 2192
    • (1979) Biochemistry , vol.18 , pp. 2186-2192
    • Heifetz, A.1    Keenan, R.W.2    Elbein, A.D.3
  • 22
    • 0038699625 scopus 로고    scopus 로고
    • Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry
    • H. Zhang, X.J. Li, D.B. Martin, and R. Aebersold Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry Nat. Biotechnol. 21 2003 660 666
    • (2003) Nat. Biotechnol. , vol.21 , pp. 660-666
    • Zhang, H.1    Li, X.J.2    Martin, D.B.3    Aebersold, R.4
  • 24
    • 77953703296 scopus 로고    scopus 로고
    • Molecular imaging of N-linked glycosylation suggests glycan biosynthesis is a novel target for cancer therapy
    • J.N. Contessa, M.S. Bhojani, H.H. Freeze, B.D. Ross, A. Rehemtulla, and T.S. Lawrence Molecular imaging of N-linked glycosylation suggests glycan biosynthesis is a novel target for cancer therapy Clin. Cancer Res. 16 2010 3205 3214
    • (2010) Clin. Cancer Res. , vol.16 , pp. 3205-3214
    • Contessa, J.N.1    Bhojani, M.S.2    Freeze, H.H.3    Ross, B.D.4    Rehemtulla, A.5    Lawrence, T.S.6
  • 25
    • 0034014642 scopus 로고    scopus 로고
    • N-Glycans influence the in vitro adhesive and invasive behaviour of three metastatic cell lines
    • D. Bironaite, J.M. Nesland, H. Dalen, B. Risberg, and M. Bryne N-Glycans influence the in vitro adhesive and invasive behaviour of three metastatic cell lines Tumor Biol. 21 2000 165 175
    • (2000) Tumor Biol. , vol.21 , pp. 165-175
    • Bironaite, D.1    Nesland, J.M.2    Dalen, H.3    Risberg, B.4    Bryne, M.5
  • 26
    • 0027359837 scopus 로고
    • Inhibition of experimental metastasis by an α-glucosidase inhibitor, 1,6-epi-cyclophellitol
    • S. Atsumi, C. Nosaka, Y. Ochi, H. Iinuma, and K. Umezawa Inhibition of experimental metastasis by an α-glucosidase inhibitor, 1,6-epi-cyclophellitol Cancer Res. 53 1993 4896 4899
    • (1993) Cancer Res. , vol.53 , pp. 4896-4899
    • Atsumi, S.1    Nosaka, C.2    Ochi, Y.3    Iinuma, H.4    Umezawa, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.