메뉴 건너뛰기




Volumn 21, Issue 9, 2014, Pages 957-965

Cystatin f regulates proteinase activity in il-2-activated natural killer cells

Author keywords

Cathepsin C.; Cathepsin V; Cystatin F; Natural Killer Cells

Indexed keywords

CATHEPSIN V; CYSTATIN; CYSTATIN F; DIPEPTIDYL PEPTIDASE I; INTERLEUKIN 2; PROTEINASE; UNCLASSIFIED DRUG; (3-ETHOXYCARBONYLOXIRANE-2-CARBONYL)LEUCINE (3-METHYLBUTYL) AMIDE; CST7 PROTEIN, HUMAN; ENZYME INHIBITOR; LEUCINE; PEPTIDE HYDROLASE; TUMOR MARKER;

EID: 84906267525     PISSN: 09298665     EISSN: 18755305     Source Type: Journal    
DOI: 10.2174/0929866521666140403124146     Document Type: Article
Times cited : (30)

References (45)
  • 1
    • 1842670944 scopus 로고    scopus 로고
    • The dynamic life of natural killer cells
    • Yokoyama, W.M.; Kim, S.; French, A.R. The Dynamic Life of Natural Killer Cells. Annu. Rev. Immunol, 2004, 22(1), 405-429
    • (2004) Annu. Rev. Immunol , vol.22 , Issue.1 , pp. 405-429
    • Yokoyama, W.M.1    Kim, S.2    French, A.R.3
  • 2
    • 33745401218 scopus 로고    scopus 로고
    • Natural killer cells as an initial defense against pathogens
    • Lodoen, M.B.; Lanier, L.L. Natural killer cells as an initial defense against pathogens. Curr. Opin. Immunol, 2006, 18(4), 391-398
    • (2006) Curr. Opin. Immunol , vol.18 , Issue.4 , pp. 391-398
    • Lodoen, M.B.1    Lanier, L.L.2
  • 3
    • 72949113082 scopus 로고    scopus 로고
    • Endolysosomal proteases and their inhibitors in immunity
    • Bird, P.I.; Trapani, J.A.; Villadangos, J.A. Endolysosomal proteases and their inhibitors in immunity. Nat. Rev. Immunol, 2009, 9(12), 871-882
    • (2009) Nat. Rev. Immunol , vol.9 , Issue.12 , pp. 871-882
    • Bird, P.I.1    Trapani, J.A.2    Villadangos, J.A.3
  • 4
    • 77955946409 scopus 로고    scopus 로고
    • Proteases in lymphocyte killer function: Redundancy, polymorphism and questions remaining
    • Sutton, V.R.; Trapani, J.A. Proteases in lymphocyte killer function: redundancy, polymorphism and questions remaining. Biol Chem., 2010, 391(8), 873-9
    • (2010) Biol Chem. , vol.391 , Issue.8 , pp. 873-879
    • Sutton, V.R.1    Trapani, J.A.2
  • 5
    • 70449336081 scopus 로고    scopus 로고
    • Diverse regulatory roles for lysosomal proteases in the immune response
    • Colbert, J.D.; Matthews, S.P.; Miller, G.; Watts, C. Diverse regulatory roles for lysosomal proteases in the immune response. Eur. J. Immunol, 2009, 39(11), 2955-2965
    • (2009) Eur. J. Immunol , vol.39 , Issue.11 , pp. 2955-2965
    • Colbert, J.D.1    Matthews, S.P.2    Miller, G.3    Watts, C.4
  • 6
    • 58149196159 scopus 로고    scopus 로고
    • Cathepsin W expressed exclusively in CD8+ T cells and NK cells, is secreted during target cell killing but is not essential for cytotoxicity in human CTLs
    • Stoeckle, C; Gouttefangeas, C; Hammer, M.; Weber, E.; Melms, A.; Tolosa, E., Cathepsin W expressed exclusively in CD8+ T cells and NK cells, is secreted during target cell killing but is not essential for cytotoxicity in human CTLs. Exp. Hematol, 2009, 37(2), 266-275
    • (2009) Exp. Hematol , vol.37 , Issue.2 , pp. 266-275
    • Stoeckle, C.1    Gouttefangeas, C.2    Hammer, M.3    Weber, E.4    Melms, A.5    Tolosa, E.6
  • 8
    • 33750072307 scopus 로고    scopus 로고
    • Cytotoxic T Lymphocytes from cathepsin B-deficient mice survive normally in vitro and in vivo after encountering and killing target cells
    • Baran, K; Ciccone, A.; Peters, C; Yagita, H; Bird, P.I.; Villadangos, J.A.; Trapani, J.A. Cytotoxic T Lymphocytes from Cathepsin B-deficient Mice Survive Normally in vitro and in vivo after Encountering and Killing Target Cells. J. Biol. Chem., 2006, 281(41), 30485-30491
    • (2006) J. Biol. Chem. , vol.281 , Issue.41 , pp. 30485-30491
    • Baran, K.1    Ciccone, A.2    Peters, C.3    Yagita, H.4    Bird, P.I.5    Villadangos, J.A.6    Trapani, J.A.7
  • 11
    • 0038687865 scopus 로고    scopus 로고
    • Human cathepsin v functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization
    • Bromme, D.; Li, Z.; Barnes, M.; Mehler, E. Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization. Biochemistry, 1999, 38(8), 2377-85
    • (1999) Biochemistry , vol.38 , Issue.8 , pp. 2377-2385
    • Bromme, D.1    Li, Z.2    Barnes, M.3    Mehler, E.4
  • 12
    • 33750984761 scopus 로고    scopus 로고
    • The role of cystatins in cells of the immune system
    • Kopitar-Jerala, N. The role of cystatins in cells of the immune system. FEBS Lett., 2006, 580, 6295-6301
    • (2006) FEBS Lett. , vol.580 , pp. 6295-6301
    • Kopitar-Jerala, N.1
  • 13
    • 52049096824 scopus 로고    scopus 로고
    • Cystatins: Biochemical and structural properties, and medical relevance
    • Turk, V.; Stoka, V.; Turk, D. Cystatins: biochemical and structural properties, and medical relevance. Front. Biosci., 2008, 13, 5406-5420
    • (2008) Front. Biosci. , vol.13 , pp. 5406-5420
    • Turk, V.1    Stoka, V.2    Turk, D.3
  • 14
    • 0038835365 scopus 로고    scopus 로고
    • Thyropins-new structurally related proteinase inhibitors
    • Lenarčič, B.; Bevec, T. Thyropins-new structurally related proteinase inhibitors. Biol. Chem., 1998, 379(2), 105-11
    • (1998) Biol. Chem. , vol.379 , Issue.2 , pp. 105-111
    • Lenarčič, B.1    Bevec, T.2
  • 15
    • 0035986219 scopus 로고    scopus 로고
    • Regulating cysteine protease activity: Essential role of protease inhibitors as guardians and regulators
    • Turk, B.; Turk, D.; Salvesen, G.S. Regulating cysteine protease activity: essential role of protease inhibitors as guardians and regulators. Curr. Pharm. Des., 2002, 8(18), 1623-37
    • (2002) Curr. Pharm. Des. , vol.8 , Issue.18 , pp. 1623-1637
    • Turk, B.1    Turk, D.2    Salvesen, G.S.3
  • 16
    • 15944426682 scopus 로고    scopus 로고
    • Inhibitory properties of cystatin F and its localization in U937 promonocyte cells
    • Langerholc, T.; Zavasnik-Bergant, V.; Turk, B.; Turk, V.; Abrahamson, M.; Kos, J., Inhibitory properties of cystatin F and its localization in U937 promonocyte cells. FEBS J., 2005, 272(6), 1535-1545
    • (2005) FEBS J. , vol.272 , Issue.6 , pp. 1535-1545
    • Langerholc, T.1    Zavasnik-Bergant, V.2    Turk, B.3    Turk, V.4    Abrahamson, M.5    Kos, J.6
  • 17
    • 33745203738 scopus 로고    scopus 로고
    • Structural basis of reduction-dependent activation of human cystatin f
    • Schüttelkopf, A.W.; Hamilton, G.; Watts, C; van Aalten, D.M.F. Structural Basis of Reduction-dependent Activation of Human Cystatin F. J. Biol. Chem., 2006, 281(24), 16570-16575
    • (2006) J. Biol. Chem. , vol.281 , Issue.24 , pp. 16570-16575
    • Schüttelkopf, A.W.1    Hamilton, G.2    Watts, C.3    Van Aalten, D.M.F.4
  • 18
    • 0032569023 scopus 로고    scopus 로고
    • Leukocystatin a new class II cystatin expressed selectively by hematopoietic cells
    • Halfon, S. Leukocystatin, a new class II cystatin expressed selectively by hematopoietic cells. J. Biol. Chem., 1998, 273, 16400-16408
    • (1998) J. Biol. Chem. , vol.273 , pp. 16400-16408
    • Halfon, S.1
  • 21
    • 2942746230 scopus 로고    scopus 로고
    • Cystatin F is secreted, but artificial modification of its C-terminus can induce its endocytic targeting
    • Cappello, F.; Gatti, E.; Camossetto, V.; David, A.; Lelouard, H; Pierre, P. Cystatin F is secreted, but artificial modification of its C-terminus can induce its endocytic targeting. Exp. Cell Res., 2004, 297, 607-618
    • (2004) Exp. Cell Res. , vol.297 , pp. 607-618
    • Cappello, F.1    Gatti, E.2    Camossetto, V.3    David, A.4    Lelouard, H.5    Pierre, P.6
  • 22
    • 63049116236 scopus 로고    scopus 로고
    • Glycosylation directs targeting and activation of cystatin f from intracellular and extracellular sources
    • Colbert, J.D.; Plechanovová, A.; Watts, C. Glycosylation Directs Targeting and Activation of Cystatin F from Intracellular and Extracellular Sources. Traffic, 2009, 10(4), 425-437
    • (2009) Traffic , vol.10 , Issue.4 , pp. 425-437
    • Colbert, J.D.1    Plechanovová, A.2    Watts, C.3
  • 24
    • 38949174026 scopus 로고    scopus 로고
    • Cystatin F is a cathepsin C-directed protease inhibitor regulated by proteolysis
    • Hamilton, G.; Colbert, J.D.; Schuettelkopf, A.W.; Watts, C. Cystatin F is a cathepsin C-directed protease inhibitor regulated by proteolysis. EMBO J., 2008, 27(3), 499-508
    • (2008) EMBO J. , vol.27 , Issue.3 , pp. 499-508
    • Hamilton, G.1    Colbert, J.D.2    Schuettelkopf, A.W.3    Watts, C.4
  • 25
    • 0027265549 scopus 로고
    • Modulation of perforin and granzyme messenger RNA expression in human natural killer cells
    • Salcedo, T.; Azzoni, L.; Wolf, S.; Perussia, B. Modulation of perforin and granzyme messenger RNA expression in human natural killer cells. J. Immunol, 1993, 151(5), 2511-2520
    • (1993) J. Immunol , vol.151 , Issue.5 , pp. 2511-2520
    • Salcedo, T.1    Azzoni, L.2    Wolf, S.3    Perussia, B.4
  • 26
    • 29144498235 scopus 로고    scopus 로고
    • IL-2 regulates perforin and granzyme gene expression in CD8+ T cells independently of its effects on survival and proliferation
    • Janas, M.L.; Groves, P.; Kienzle, N; Kelso, A. IL-2 Regulates Perforin and Granzyme Gene Expression in CD8+ T Cells Independently of Its Effects on Survival and Proliferation. J. Immunol, 2005, 175(12), 8003-8010
    • (2005) J. Immunol , vol.175 , Issue.12 , pp. 8003-8010
    • Janas, M.L.1    Groves, P.2    Kienzle, N.3    Kelso, A.4
  • 27
    • 0034937134 scopus 로고    scopus 로고
    • Anti-cathepsin L monoclonal antibodies that distinguish cathepsin L from cathepsin V
    • Kopitar-Jerala, N; Bevec, T.; Barlic-Maganja, D.; Gubensek, F.; Turk, V. Anti-cathepsin L monoclonal antibodies that distinguish cathepsin L from cathepsin V. Biol. Chem., 2001, 382(5), 867-70
    • (2001) Biol. Chem. , vol.382 , Issue.5 , pp. 867-870
    • Kopitar-Jerala, N.1    Bevec, T.2    Barlic-Maganja, D.3    Gubensek, F.4    Turk, V.5
  • 28
    • 77952951447 scopus 로고    scopus 로고
    • Increased nucleolar localization of SpiA3G in classically but not alternatively activated macrophages
    • Konjar, Š; Yin, F.; Bogyo, M.; Turk, B.; Kopitar-Jerala, N. Increased nucleolar localization of SpiA3G in classically but not alternatively activated macrophages. FEBS Lett., 2010, 584(11), 2201-2206
    • (2010) FEBS Lett. , vol.584 , Issue.11 , pp. 2201-2206
    • Konjar, Š.1    Yin, F.2    Bogyo, M.3    Turk, B.4    Kopitar-Jerala, N.5
  • 31
    • 0035852855 scopus 로고    scopus 로고
    • Human recombinant pro-dipeptidyl peptidase i (cathepsin C) can be activated by cathepsins L and S but not by autocatalytic processing
    • Dahl, S.W.; Halkier, T.; Lauritzen, C.; Dolenc, I.; Pedersen, J.; Turk, V.; Turk, B. Human recombinant pro-dipeptidyl peptidase I (cathepsin C) can be activated by cathepsins L and S but not by autocatalytic processing. Biochemistry, 2001, 40, 1671-1678
    • (2001) Biochemistry , vol.40 , pp. 1671-1678
    • Dahl, S.W.1    Halkier, T.2    Lauritzen, C.3    Dolenc, I.4    Pedersen, J.5    Turk, V.6    Turk, B.7
  • 32
    • 33646394866 scopus 로고    scopus 로고
    • A family with Papillon-Lefevre syndrome reveals a requirement for cathepsin C in granzyme B activation and NK cell cytolytic activity
    • Meade, J.L.; de Wynter, E.A.; Brett, P.; Sharif, S.M.; Woods, C.G.; Markham, A.F.; Cook, G.P. A family with Papillon-Lefevre syndrome reveals a requirement for cathepsin C in granzyme B activation and NK cell cytolytic activity. Blood, 2006, 107, 3665-3668
    • (2006) Blood , vol.107 , pp. 3665-3668
    • Meade, J.L.1    De Wynter, E.A.2    Brett, P.3    Sharif, S.M.4    Woods, C.G.5    Markham, A.F.6    Cook, G.P.7
  • 33
    • 0019448114 scopus 로고
    • Interleukin-2 augments natural killer cell activity
    • Henney, C.S.; Kuribayashi, K.; Kern, D.E.; Gillis, S. Interleukin-2 augments natural killer cell activity. Nature, 1981, 291(5813), 335-8
    • (1981) Nature , vol.291 , Issue.5813 , pp. 335-338
    • Henney, C.S.1    Kuribayashi, K.2    Kern, D.E.3    Gillis, S.4
  • 34
    • 0019862911 scopus 로고
    • Murine NK cell cultures: Effects of interleukin-2 and interferon on cell growth and cytotoxic reactivity
    • Kuribayashi, K.; Gillis, S.; Kern, D.E.; Henney, C.S. Murine NK cell cultures: effects of interleukin-2 and interferon on cell growth and cytotoxic reactivity. J. Immunol., 1981, 126(6), 2321-7
    • (1981) J. Immunol. , vol.126 , Issue.6 , pp. 2321-2327
    • Kuribayashi, K.1    Gillis, S.2    Kern, D.E.3    Henney, C.S.4
  • 35
    • 33846188177 scopus 로고    scopus 로고
    • Design of cell-permeable, fluorescent activity-based probes for the lysosomal cysteine protease asparaginyl endopeptidase (AEP)/legumain
    • Sexton, K.B.; Witte, M.D.; Blum, G.; Bogyo, M. Design of cell-permeable, fluorescent activity-based probes for the lysosomal cysteine protease asparaginyl endopeptidase (AEP)/legumain. Bioorg. Med. Chem. Lett., 2007, 17(3), 649-653
    • (2007) Bioorg. Med. Chem. Lett. , vol.17 , Issue.3 , pp. 649-653
    • Sexton, K.B.1    Witte, M.D.2    Blum, G.3    Bogyo, M.4
  • 36
    • 4344670363 scopus 로고    scopus 로고
    • Cathepsin v a novel and potent elastolytic activity expressed in activated macrophages
    • Yasuda, Y.; Li, Z.; Greenbaum, D.; Bogyo, M.; Weber, E.; Bromme, D. Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages. J. Biol. Chem., 2004, 279(35), 36761-70
    • (2004) J. Biol. Chem , vol.279 , Issue.35 , pp. 36761-36770
    • Yasuda, Y.1    Li, Z.2    Greenbaum, D.3    Bogyo, M.4    Weber, E.5    Bromme, D.6
  • 38
    • 0041876230 scopus 로고    scopus 로고
    • Biosynthetic processing of cathepsins and lysosomal degradation are abolished in asparaginyl endopeptidase-deficient mice
    • Shirahama-Noda, K.; Yamamoto, A.; Sugihara, K.; Hashimoto, N.; Asano, M.; Nishimura, M.; Hara-Nishimura, I. Biosynthetic Processing of Cathepsins and Lysosomal Degradation Are Abolished in Asparaginyl Endopeptidase-deficient Mice. J. Biol. Chem., 2003, 278(35), 33194-33199
    • (2003) J. Biol. Chem. , vol.278 , Issue.35 , pp. 33194-33199
    • Shirahama-Noda, K.1    Yamamoto, A.2    Sugihara, K.3    Hashimoto, N.4    Asano, M.5    Nishimura, M.6    Hara-Nishimura, I.7
  • 39
    • 82755195248 scopus 로고    scopus 로고
    • Internalisation of exogenous cystatin F suppresses cysteine proteases and induces the accumulation of single-chain cathepsin L by multiple mechanisms
    • Colbert, J.D.; Matthews, S.P.; Kos, J.; Watts, C. Internalisation of exogenous cystatin F suppresses cysteine proteases and induces the accumulation of single-chain cathepsin L by multiple mechanisms. J. Biol. Chem., 2011, 286(49), 42082-90
    • (2011) J. Biol. Chem. , vol.286 , Issue.49 , pp. 42082-42090
    • Colbert, J.D.1    Matthews, S.P.2    Kos, J.3    Watts, C.4
  • 40
    • 0030888065 scopus 로고    scopus 로고
    • Molecular cloning, chromosomal localization, and expression of murine dipeptidyl peptidase I
    • Pham, C.T.N.; Armstrong, R.J.; Zimonjic, D.B.; Popescu, N.C.; Payan, D.G.; Ley, T.J. Molecular Cloning, Chromosomal Localization, and Expression of Murine Dipeptidyl Peptidase I. J. Biol. Chem., 1997, 272(16), 10695-10703
    • (1997) J. Biol. Chem. , vol.272 , Issue.16 , pp. 10695-10703
    • Pham, C.T.N.1    Armstrong, R.J.2    Zimonjic, D.B.3    Popescu, N.C.4    Payan, D.G.5    Ley, T.J.6
  • 41
    • 0032995222 scopus 로고    scopus 로고
    • Cathepsin L is capable of truncating cystatin C of 11 N-terminal amino acids
    • Popovic, T.; Cimerman, N.; Dolenc, I.; Ritonja, A.; Brzin, J., Cathepsin L is capable of truncating cystatin C of 11 N-terminal amino acids. FEBS Lett., 1999, 455(1-2), 92-96
    • (1999) FEBS Lett. , vol.455 , Issue.1-2 , pp. 92-96
    • Popovic, T.1    Cimerman, N.2    Dolenc, I.3    Ritonja, A.4    Brzin, J.5
  • 42
    • 0033039015 scopus 로고    scopus 로고
    • The affinity and kinetics of inhibition of cysteine proteinases by intact recombinant bovine cystatin C
    • Olsson, S.-L.; Ek, B.; Björk, I. The affinity and kinetics of inhibition of cysteine proteinases by intact recombinant bovine cystatin C. Biochim. Biophys. Acta, 1999, 1432(1), 73-81
    • (1999) Biochim. Biophys. Acta , vol.1432 , Issue.1 , pp. 73-81
    • Olsson, S.-L.1    Ek, B.2    Björk, I.3
  • 45
    • 0026101681 scopus 로고
    • Inactivation of human cystatin C and kininogen by human cathepsin D
    • Lenarčič, B.; Krašovec, M.; Ritonja, A.; Olafsson, I.; Turk, V. Inactivation of human cystatin C and kininogen by human cathepsin D. FEBS Lett., 1991, 280(2), 211-215.
    • (1991) FEBS Lett. , vol.280 , Issue.2 , pp. 211-215
    • Lenarčič, B.1    Krašovec, M.2    Ritonja, A.3    Olafsson, I.4    Turk, V.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.