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Volumn 5, Issue DEC, 2014, Pages

Cysteine cathepsins as regulators of the cytotoxicity of nk and t cells

Author keywords

Cathepsins; Cystatins; Cytotoxic T cells; Cytotoxicity; Natural killer cells

Indexed keywords

ALPHA ACTININ 1; CATHEPSIN H; CATHEPSIN L; CATHEPSIN V; CATHEPSIN W; CATHEPSIN X; COMPLEMENT MEMBRANE ATTACK COMPLEX; CYSTATIN; CYSTATIN C; DIPEPTIDYL PEPTIDASE I; FAS ANTIGEN; GRANZYME A; GRANZYME B; INTERCELLULAR ADHESION MOLECULE 1; INTERLEUKIN 2; LYMPHOCYTE FUNCTION ASSOCIATED ANTIGEN 1; LYSOSOME ASSOCIATED MEMBRANE PROTEIN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; PERFORIN; REGULATOR PROTEIN; TALIN;

EID: 84919710675     PISSN: None     EISSN: 16643224     Source Type: Journal    
DOI: 10.3389/fimmu.2014.00616     Document Type: Review
Times cited : (86)

References (144)
  • 1
    • 84859426282 scopus 로고    scopus 로고
    • MEROPS: the database of proteolytic enzymes, their substrates and inhibitors
    • Rawlings ND, Barrett AJ, Bateman A. MEROPS: the database of proteolytic enzymes, their substrates and inhibitors. Nucleic Acids Res (2012) 40:D343-50. doi: 10.1093/nar/gkr987
    • (2012) Nucleic Acids Res , vol.40 , pp. D343-D350
    • Rawlings, N.D.1    Barrett, A.J.2    Bateman, A.3
  • 2
    • 33748308883 scopus 로고    scopus 로고
    • Targeting proteases: successes, failures and future prospects
    • Turk B. Targeting proteases: successes, failures and future prospects. Nat Rev Drug Discov (2006) 5:785-99. doi:10.1038/nrd2092
    • (2006) Nat Rev Drug Discov , vol.5 , pp. 785-799
    • Turk, B.1
  • 3
    • 82755161948 scopus 로고    scopus 로고
    • Cysteine cathepsins: from structure, function and regulation to new frontiers
    • Turk V, Stoka V, Vasiljeva O, Renko M, Sun T, Turk B, et al. Cysteine cathepsins: from structure, function and regulation to new frontiers. Biochim Biophys Acta (2012) 1824:68-88. doi:10.1016/j.bbapap.2011.10.002
    • (2012) Biochim Biophys Acta , vol.1824 , pp. 68-88
    • Turk, V.1    Stoka, V.2    Vasiljeva, O.3    Renko, M.4    Sun, T.5    Turk, B.6
  • 4
    • 84874827034 scopus 로고    scopus 로고
    • The role of cysteine proteinases and their inhibitors in the host-pathogen cross talk
    • Kopitar-Jerala N. The role of cysteine proteinases and their inhibitors in the host-pathogen cross talk. Curr Protein Pept Sci (2012) 13:767-75. doi:10.2174/138920312804871102
    • (2012) Curr Protein Pept Sci , vol.13 , pp. 767-775
    • Kopitar-Jerala, N.1
  • 5
    • 33845327817 scopus 로고    scopus 로고
    • Cysteine cathepsins: regulators of antitumour immune response
    • Obermajer N, Doljak B, Kos J. Cysteine cathepsins: regulators of antitumour immune response. Expert Opin Biol Ther (2006) 6:1295-309. doi:10.1517/14712598.6.12.1295
    • (2006) Expert Opin Biol Ther , vol.6 , pp. 1295-1309
    • Obermajer, N.1    Doljak, B.2    Kos, J.3
  • 6
    • 72949113082 scopus 로고    scopus 로고
    • Endolysosomal proteases and their inhibitors in immunity
    • Bird PI, Trapani JA, Villadangos JA. Endolysosomal proteases and their inhibitors in immunity. Nat Rev Immunol (2009) 9:871-82. doi:10.1038/nri2671
    • (2009) Nat Rev Immunol , vol.9 , pp. 871-882
    • Bird, P.I.1    Trapani, J.A.2    Villadangos, J.A.3
  • 7
    • 0034599498 scopus 로고    scopus 로고
    • Role for cathepsin F in invariant chain processing and major histocompatibility complex class II peptide loading by macrophages
    • Shi GP, Bryant RA, Riese R, Verhelst S, Driessen C, Li Z, et al. Role for cathepsin F in invariant chain processing and major histocompatibility complex class II peptide loading by macrophages. J Exp Med (2000) 191:1177-86. doi:10.1084/jem.191.7.1177
    • (2000) J Exp Med , vol.191 , pp. 1177-1186
    • Shi, G.P.1    Bryant, R.A.2    Riese, R.3    Verhelst, S.4    Driessen, C.5    Li, Z.6
  • 8
    • 66749093488 scopus 로고    scopus 로고
    • The role of cathepsin X in cell signaling
    • Kos J, Jevnikar Z, Obermajer N. The role of cathepsin X in cell signaling. Cell Adh Migr (2009) 3:164-6. doi:10.4161/cam.3.2.7403
    • (2009) Cell Adh Migr , vol.3 , pp. 164-166
    • Kos, J.1    Jevnikar, Z.2    Obermajer, N.3
  • 9
    • 84880510548 scopus 로고    scopus 로고
    • Neuroprotective role of gamma-enolase in microglia in a mouse model of Alzheimer's disease is regulated by cathepsin X
    • Hafner A, Glavan G, Obermajer N, Zivin M, Schliebs R, Kos J. Neuroprotective role of gamma-enolase in microglia in a mouse model of Alzheimer's disease is regulated by cathepsin X. Aging Cell (2013) 12:604-14. doi:10.1111/acel.12093
    • (2013) Aging Cell , vol.12 , pp. 604-614
    • Hafner, A.1    Glavan, G.2    Obermajer, N.3    Zivin, M.4    Schliebs, R.5    Kos, J.6
  • 10
    • 33645094397 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: structure, function and inhibition of cathepsins
    • Roberts R. Lysosomal cysteine proteases: structure, function and inhibition of cathepsins. Drug News Perspect (2005) 18:605-14. doi:10.1358/dnp.2005.18.10.949485
    • (2005) Drug News Perspect , vol.18 , pp. 605-614
    • Roberts, R.1
  • 11
    • 0035801514 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: facts and opportunities
    • Turk V, Turk B, Turk D. Lysosomal cysteine proteases: facts and opportunities. EMBO J (2001) 20:4629-33. doi:10.1093/emboj/20.17.4629
    • (2001) EMBO J , vol.20 , pp. 4629-4633
    • Turk, V.1    Turk, B.2    Turk, D.3
  • 12
    • 0345310073 scopus 로고    scopus 로고
    • Revised definition of substrate binding sites of papain-like cysteine proteases
    • Turk D, Guncar G, Podobnik M, Turk B. Revised definition of substrate binding sites of papain-like cysteine proteases. Biol Chem (1998) 379:137-47. doi:10.1515/bchm.1998.379.2.137
    • (1998) Biol Chem , vol.379 , pp. 137-147
    • Turk, D.1    Guncar, G.2    Podobnik, M.3    Turk, B.4
  • 13
    • 0037322932 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases (cathepsins): promising drug targets
    • Turk D, Guncar G. Lysosomal cysteine proteases (cathepsins): promising drug targets. Acta Crystallogr D Biol Crystallogr (2003) 59:203-13. doi:10.1107/S0907444902021479
    • (2003) Acta Crystallogr D Biol Crystallogr , vol.59 , pp. 203-213
    • Turk, D.1    Guncar, G.2
  • 14
    • 12044253640 scopus 로고
    • The refined 2 15 A X-ray crystal structure of human liver cathepsin B: the structural basis for its specificity
    • Musil D, Zucic D, Turk D, Engh RA I, Mayr R, Huber T, et al. The refined 2.15 A X-ray crystal structure of human liver cathepsin B: the structural basis for its specificity. EMBO J (1991) 10:2321-30.
    • (1991) EMBO J , vol.10 , pp. 2321-2330
    • Musil, D.1    Zucic, D.2    Turk, D.3    Engh, R.A.I.4    Mayr, R.5    Huber, T.6
  • 15
    • 0035814913 scopus 로고    scopus 로고
    • Cathepsins X and B can be differentiated through their respective mono- and dipeptidyl carboxypeptidase activities
    • Therrien C, Lachance P, Sulea T, Purisima EO, Qi H, Ziomek E, et al. Cathepsins X and B can be differentiated through their respective mono- and dipeptidyl carboxypeptidase activities. Biochemistry (2001) 40:2702-11. doi:10.1021/bi002460a
    • (2001) Biochemistry , vol.40 , pp. 2702-2711
    • Therrien, C.1    Lachance, P.2    Sulea, T.3    Purisima, E.O.4    Qi, H.5    Ziomek, E.6
  • 16
    • 0032518496 scopus 로고    scopus 로고
    • Crystal structure of porcine cathepsin H determined at 2 1 A resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function
    • Guncar G, Podobnik M, Pungercar J, Strukelj B, Turk V, Turk D. Crystal structure of porcine cathepsin H determined at 2.1 A resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function. Structure (1998) 6:51-61. doi:10.1016/S0969-2126(98)00007-0
    • (1998) Structure , vol.6 , pp. 51-61
    • Guncar, G.1    Podobnik, M.2    Pungercar, J.3    Strukelj, B.4    Turk, V.5    Turk, D.6
  • 18
    • 0345254939 scopus 로고    scopus 로고
    • Recombinant human cathepsin H lacking the mini chain is an endopeptidase
    • Vasiljeva O, Dolinar M, Turk V, Turk B. Recombinant human cathepsin H lacking the mini chain is an endopeptidase. Biochemistry (2003) 42:13522-8. doi:10.1021/bi035355k
    • (2003) Biochemistry , vol.42 , pp. 13522-13528
    • Vasiljeva, O.1    Dolinar, M.2    Turk, V.3    Turk, B.4
  • 19
    • 0027394245 scopus 로고
    • Two distinct gene subfamilies within the family of cysteine protease genes
    • Karrer KM, Peiffer SL, DiTomas ME. Two distinct gene subfamilies within the family of cysteine protease genes. Proc Natl Acad Sci U S A (1993) 90:3063-7. doi:10.1073/pnas.90.7.3063
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 3063-3067
    • Karrer, K.M.1    Peiffer, S.L.2    DiTomas, M.E.3
  • 20
    • 84881539601 scopus 로고    scopus 로고
    • Cathepsin K: a unique collagenolytic cysteine peptidase
    • Novinec M, Lenarcic B. Cathepsin K: a unique collagenolytic cysteine peptidase. Biol Chem (2013) 394:1163-79. doi:10.1515/hsz-2013-0134
    • (2013) Biol Chem , vol.394 , pp. 1163-1179
    • Novinec, M.1    Lenarcic, B.2
  • 21
    • 2342551977 scopus 로고    scopus 로고
    • Cysteine cathepsins (proteases) - on the main stage of cancer?
    • Turk V, Kos J, Turk B. Cysteine cathepsins (proteases) - on the main stage of cancer? Cancer Cell (2004) 5:409-10. doi:10.1016/S1535-6108(04)00117-5
    • (2004) Cancer Cell , vol.5 , pp. 409-410
    • Turk, V.1    Kos, J.2    Turk, B.3
  • 22
    • 17044379501 scopus 로고    scopus 로고
    • Proteinaceous cysteine protease inhibitors
    • Dubin G. Proteinaceous cysteine protease inhibitors. Cell Mol Life Sci (2005) 62:653-69. doi:10.1007/s00018-004-4445-9
    • (2005) Cell Mol Life Sci , vol.62 , pp. 653-669
    • Dubin, G.1
  • 23
    • 33646067439 scopus 로고    scopus 로고
    • Towards novel anti-cancer strategies based on cystatin function
    • Keppler D. Towards novel anti-cancer strategies based on cystatin function. Cancer Lett (2006) 235:159-76. doi:10.1016/j.canlet.2005.04.001
    • (2006) Cancer Lett , vol.235 , pp. 159-176
    • Keppler, D.1
  • 24
    • 0023024774 scopus 로고
    • Isolation of six cysteine proteinase inhibitors from human urine Their physicochemical and enzyme kinetic properties and concentrations in biological fluids
    • Abrahamson M, Barrett AJ, Salvesen G, Grubb A. Isolation of six cysteine proteinase inhibitors from human urine. Their physicochemical and enzyme kinetic properties and concentrations in biological fluids. J Biol Chem (1986) 261:11282-9.
    • (1986) J Biol Chem , vol.261 , pp. 11282-11289
    • Abrahamson, M.1    Barrett, A.J.2    Salvesen, G.3    Grubb, A.4
  • 26
    • 0024066065 scopus 로고
    • The 2 0 A X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases
    • Bode W, Engh R, Musil D, Thiele U, Huber R, Karshikov A, et al. The 2.0 A X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases. EMBO J (1988) 7:2593-9.
    • (1988) EMBO J , vol.7 , pp. 2593-2599
    • Bode, W.1    Engh, R.2    Musil, D.3    Thiele, U.4    Huber, R.5    Karshikov, A.6
  • 27
    • 0033516575 scopus 로고    scopus 로고
    • Inhibition of mammalian legumain by some cystatins is due to a novel second reactive site
    • Alvarez-Fernandez M, Barrett AJ, Gerhartz B, Dando PM, Ni J, Abrahamson M. Inhibition of mammalian legumain by some cystatins is due to a novel second reactive site. J Biol Chem (1999) 274:19195-203. doi:10.1074/jbc.274.27.19195
    • (1999) J Biol Chem , vol.274 , pp. 19195-19203
    • Alvarez-Fernandez, M.1    Barrett, A.J.2    Gerhartz, B.3    Dando, P.M.4    Ni, J.5    Abrahamson, M.6
  • 28
    • 82755195248 scopus 로고    scopus 로고
    • Internalization of exogenous cystatin F supresses cysteine proteases and induces the accumulation of single-chain cathepsin L by multiple mechanisms
    • Colbert JD, Matthews SP, Kos J, Watts C. Internalization of exogenous cystatin F supresses cysteine proteases and induces the accumulation of single-chain cathepsin L by multiple mechanisms. J Biol Chem (2011) 286:42082-90. doi:10.1074/jbc. M111.253914
    • (2011) J Biol Chem , vol.286 , pp. 42082-42090
    • Colbert, J.D.1    Matthews, S.P.2    Kos, J.3    Watts, C.4
  • 29
    • 84878759123 scopus 로고    scopus 로고
    • Cystatin C properties crucial for uptake and inhibition of intracellular target enzymes
    • Wallin H, Abrahamson M, Ekstrom U. Cystatin C properties crucial for uptake and inhibition of intracellular target enzymes. J Biol Chem (2013) 288:17019-29. doi:10.1074/jbc. M113.453449
    • (2013) J Biol Chem , vol.288 , pp. 17019-17029
    • Wallin, H.1    Abrahamson, M.2    Ekstrom, U.3
  • 30
    • 0017841848 scopus 로고
    • Isolation and characterization of E 64 a new thiol protease inhibitor
    • Hanada K, Tamai M, Yamagishi M, Ohmura S, Sawada J, Tanaka I. Isolation and characterization of E 64, a new thiol protease inhibitor. Agric Biol Chem (1978) 42:523-8. doi:10.1271/bbb1961.42.523
    • (1978) Agric Biol Chem , vol.42 , pp. 523-528
    • Hanada, K.1    Tamai, M.2    Yamagishi, M.3    Ohmura, S.4    Sawada, J.5    Tanaka, I.6
  • 31
    • 0026101682 scopus 로고
    • Novel epoxysuccinyl peptides. Selective inhibitors of cathepsin B, in vitro
    • Murata M, Miyashita S, Yokoo C, Tamai M, Hanada K, Hatayama K, et al. Novel epoxysuccinyl peptides. Selective inhibitors of cathepsin B, in vitro. FEBS Lett (1991) 280:307-10. doi:10.1016/0014-5793(91)80318-W
    • (1991) FEBS Lett , vol.280 , pp. 307-310
    • Murata, M.1    Miyashita, S.2    Yokoo, C.3    Tamai, M.4    Hanada, K.5    Hatayama, K.6
  • 32
    • 84906771257 scopus 로고    scopus 로고
    • The current stage of cathepsin B inhibitors as potential anti-cancer agents
    • Kos FJ, Mitrovic A, Mirkovic B. The current stage of cathepsin B inhibitors as potential anti-cancer agents. Future Med Chem (2014) 6:1335-71. doi:10.4155/fmc.14.73
    • (2014) Future Med Chem , vol.6 , pp. 1335-1371
    • Kos, F.J.1    Mitrovic, A.2    Mirkovic, B.3
  • 33
    • 0036217977 scopus 로고    scopus 로고
    • Lymphocyte-mediated cytotoxicity
    • Russell JH, Ley TJ. Lymphocyte-mediated cytotoxicity. Annu Rev Immunol (2002) 20:323-70. doi:10.1146/annurev.immunol.20.100201.131730
    • (2002) Annu Rev Immunol , vol.20 , pp. 323-370
    • Russell, J.H.1    Ley, T.J.2
  • 34
    • 0033598718 scopus 로고    scopus 로고
    • Granzymes are the essential downstream effector molecules for the control of primary virus infections by cytolytic leukocytes
    • Mullbacher A, Waring P, Tha Hla R, Tran T, Chin S, Stehle T, et al. Granzymes are the essential downstream effector molecules for the control of primary virus infections by cytolytic leukocytes. Proc Natl Acad Sci U S A (1999) 96:13950-5. doi:10.1073/pnas.96.24.13950
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 13950-13955
    • Mullbacher, A.1    Waring, P.2    Tha Hla, R.3    Tran, T.4    Chin, S.5    Stehle, T.6
  • 36
    • 0036779576 scopus 로고    scopus 로고
    • Functional significance of the perforin/granzyme cell death pathway
    • Trapani JA, Smyth MJ. Functional significance of the perforin/granzyme cell death pathway. Nat Rev Immunol (2002) 2:735-47. doi:10.1038/nri911
    • (2002) Nat Rev Immunol , vol.2 , pp. 735-747
    • Trapani, J.A.1    Smyth, M.J.2
  • 37
    • 0037111464 scopus 로고    scopus 로고
    • Cutting edge: tumor rejection mediated by NKG2D receptor-ligand interaction is dependent upon perforin
    • Hayakawa Y, Kelly JM, Westwood JA, Darcy PK, Diefenbach A, Raulet D, et al. Cutting edge: tumor rejection mediated by NKG2D receptor-ligand interaction is dependent upon perforin. J Immunol (2002) 169:5377-81. doi:10.4049/jimmunol.169.10.5377
    • (2002) J Immunol , vol.169 , pp. 5377-5381
    • Hayakawa, Y.1    Kelly, J.M.2    Westwood, J.A.3    Darcy, P.K.4    Diefenbach, A.5    Raulet, D.6
  • 38
    • 0030823702 scopus 로고    scopus 로고
    • Perforin/granzyme-dependent and independent mechanisms are both important for the development of graft-versus-host disease after murine bone marrow transplantation
    • Graubert TA, DiPersio JF, Russell JH, Ley TJ. Perforin/granzyme-dependent and independent mechanisms are both important for the development of graft-versus-host disease after murine bone marrow transplantation. J Clin Invest (1997) 100:904-11. doi:10.1172/JCI119606
    • (1997) J Clin Invest , vol.100 , pp. 904-911
    • Graubert, T.A.1    DiPersio, J.F.2    Russell, J.H.3    Ley, T.J.4
  • 39
    • 0025597939 scopus 로고
    • The lytic granules of natural killer cells are dual-function organelles combining secretory and pre-lysosomal compartments
    • Burkhardt JK, Hester S, Lapham CK, Argon Y. The lytic granules of natural killer cells are dual-function organelles combining secretory and pre-lysosomal compartments. J Cell Biol (1990) 111:2327-40. doi:10.1083/jcb.111.6.2327
    • (1990) J Cell Biol , vol.111 , pp. 2327-2340
    • Burkhardt, J.K.1    Hester, S.2    Lapham, C.K.3    Argon, Y.4
  • 40
    • 0025905925 scopus 로고
    • Cytotoxic T lymphocyte granules are secretory lysosomes, containing both perforin and granzymes
    • Peters PJ, Borst J, Oorschot V, Fukuda M, Krahenbuhl O, Tschopp J, et al. Cytotoxic T lymphocyte granules are secretory lysosomes, containing both perforin and granzymes. J Exp Med (1991) 173:1099-109. doi:10.1084/jem.173.5.1099
    • (1991) J Exp Med , vol.173 , pp. 1099-1109
    • Peters, P.J.1    Borst, J.2    Oorschot, V.3    Fukuda, M.4    Krahenbuhl, O.5    Tschopp, J.6
  • 43
    • 0023693490 scopus 로고
    • Homology of perforin to the ninth component of complement (C9)
    • Shinkai Y, Takio K, Okumura K. Homology of perforin to the ninth component of complement (C9). Nature (1988) 334:525-7. doi:10.1038/334525a0
    • (1988) Nature , vol.334 , pp. 525-527
    • Shinkai, Y.1    Takio, K.2    Okumura, K.3
  • 44
    • 33845199637 scopus 로고    scopus 로고
    • Perforin-mediated target-cell death and immune homeostasis
    • Voskoboinik I, Smyth MJ, Trapani JA. Perforin-mediated target-cell death and immune homeostasis. Nat Rev Immunol (2006) 6:940-52. doi:10.1038/nri1983
    • (2006) Nat Rev Immunol , vol.6 , pp. 940-952
    • Voskoboinik, I.1    Smyth, M.J.2    Trapani, J.A.3
  • 45
    • 0031464539 scopus 로고    scopus 로고
    • Perforin is activated by a proteolytic cleavage during biosynthesis which reveals a phospholipid-binding C2 domain
    • Uellner R, Zvelebil J, Fau-Hopkins MJ, Hopkins J, Fau-Jones J, Jones LK, et al. Perforin is activated by a proteolytic cleavage during biosynthesis which reveals a phospholipid-binding C2 domain. EMBO J (1997) 16:7287-96.
    • (1997) EMBO J , vol.16 , pp. 7287-7296
    • Uellner, R.1    Zvelebil, J.2    Fau-Hopkins, M.J.3    Hopkins, J.4    Fau-Jones, J.5    Jones, L.K.6
  • 46
    • 0028219791 scopus 로고
    • Cytotoxicity mediated by T cells and natural killer cells is greatly impaired in perforin-deficient mice
    • Kagi D, Ledermann K, Fau-Burki B, Burki P, Fau-Seiler K, Seiler B, et al. Cytotoxicity mediated by T cells and natural killer cells is greatly impaired in perforin-deficient mice. Nature (1994) 369:31-7.
    • (1994) Nature , vol.369 , pp. 31-37
    • Kagi, D.1    Ledermann, K.2    Fau-Burki, B.3    Burki, P.4    Fau-Seiler, K.5    Seiler, B.6
  • 47
    • 84879522053 scopus 로고    scopus 로고
    • Visualization of cytolytic T cell differentiation and granule exocytosis with T cells from mice expressing active fluorescent granzyme B
    • Mouchacca P, Schmitt-Verhulst AM, Boyer C. Visualization of cytolytic T cell differentiation and granule exocytosis with T cells from mice expressing active fluorescent granzyme B. PLoS One (2013) 8:e67239. doi:10.1371/journal.pone.0067239
    • (2013) PLoS One , vol.8 , pp. e67239
    • Mouchacca, P.1    Schmitt-Verhulst, A.M.2    Boyer, C.3
  • 50
    • 0023820255 scopus 로고
    • Granzymes, a family of serine proteases released from granules of cytolytic T lymphocytes upon T cell receptor stimulation
    • Jenne DE, Tschopp J. Granzymes, a family of serine proteases released from granules of cytolytic T lymphocytes upon T cell receptor stimulation. Immunol Rev (1988) 103:53-71. doi:10.1111/j.1600-065X.1988.tb00749.x
    • (1988) Immunol Rev , vol.103 , pp. 53-71
    • Jenne, D.E.1    Tschopp, J.2
  • 51
    • 0024465841 scopus 로고
    • Isolation and complete structure of the lymphocyte serine protease granzyme G, a novel member of the granzyme multigene family in murine cytolytic T lymphocytes, Evolutionary origin of lymphocyte proteases
    • Jenne DE, Masson D, Zimmer M, Haefliger JA, Li WH, Tschopp J. Isolation and complete structure of the lymphocyte serine protease granzyme G, a novel member of the granzyme multigene family in murine cytolytic T lymphocytes. Evolutionary origin of lymphocyte proteases. Biochemistry (1989) 28:7953-61.
    • (1989) Biochemistry , vol.28 , pp. 7953-7961
    • Jenne, D.E.1    Masson, D.2    Zimmer, M.3    Haefliger, J.A.4    Li, W.H.5    Tschopp, J.6
  • 52
    • 2942700101 scopus 로고    scopus 로고
    • Discordant regulation of granzyme H and granzyme B expression in human lymphocytes
    • Sedelies KA, Sayers TJ, Edwards KM, Chen W, Pellicci DG, Godfrey DI, et al. Discordant regulation of granzyme H and granzyme B expression in human lymphocytes. J Biol Chem (2004) 279:26581-7. doi:10.1074/jbc. M312481200
    • (2004) J Biol Chem , vol.279 , pp. 26581-26587
    • Sedelies, K.A.1    Sayers, T.J.2    Edwards, K.M.3    Chen, W.4    Pellicci, D.G.5    Godfrey, D.I.6
  • 53
    • 27744511323 scopus 로고    scopus 로고
    • Differential expression of the granzymes A K and M and perforin in human peripheral blood lymphocytes
    • Bade B, Boettcher HE, Lohrmann J, Hink-Schauer C, Bratke K, Jenne DE, et al. Differential expression of the granzymes A, K and M and perforin in human peripheral blood lymphocytes. Int Immunol (2005) 17:1419-28. doi:10.1093/intimm/dxh320
    • (2005) Int Immunol , vol.17 , pp. 1419-1428
    • Bade, B.1    Boettcher, H.E.2    Lohrmann, J.3    Hink-Schauer, C.4    Bratke, K.5    Jenne, D.E.6
  • 54
    • 26044436515 scopus 로고    scopus 로고
    • Differential expression of human granzymes A, B, and K in natural killer cells and during CD8+ T cell differentiation in peripheral blood
    • Bratke K, Kuepper M, Bade B, Virchow JC Jr, Luttmann W. Differential expression of human granzymes A, B, and K in natural killer cells and during CD8+ T cell differentiation in peripheral blood. Eur J Immunol (2005) 35:2608-16. doi:10.1002/eji.200526122
    • (2005) Eur J Immunol , vol.35 , pp. 2608-2616
    • Bratke, K.1    Kuepper, M.2    Bade, B.3    Virchow Jr., J.C.4    Luttmann, W.5
  • 55
    • 42949098879 scopus 로고    scopus 로고
    • Death by a thousand cuts: granzyme pathways of programmed cell death
    • Chowdhury D, Lieberman J. Death by a thousand cuts: granzyme pathways of programmed cell death. Annu Rev Immunol (2008) 26:389-420. doi:10.1146/annurev.immunol.26.021607.090404
    • (2008) Annu Rev Immunol , vol.26 , pp. 389-420
    • Chowdhury, D.1    Lieberman, J.2
  • 57
    • 0027169762 scopus 로고
    • Activation of recombinant murine cytotoxic cell proteinase-1 requires deletion of an amino-terminal dipeptide
    • Caputo A, Garner RS, Winkler U, Hudig D, Bleackley RC. Activation of recombinant murine cytotoxic cell proteinase-1 requires deletion of an amino-terminal dipeptide. J Biol Chem (1993) 268:17672-5.
    • (1993) J Biol Chem , vol.268 , pp. 17672-17675
    • Caputo, A.1    Garner, R.S.2    Winkler, U.3    Hudig, D.4    Bleackley, R.C.5
  • 58
    • 0141629530 scopus 로고    scopus 로고
    • Granzyme B: pro-apoptotic, antiviral and antitumor functions
    • Trapani JA, Sutton VR. Granzyme B: pro-apoptotic, antiviral and antitumor functions. Curr Opin Immunol (2003) 15:533-43. doi:10.1016/S0952-7915(03)00107-9
    • (2003) Curr Opin Immunol , vol.15 , pp. 533-543
    • Trapani, J.A.1    Sutton, V.R.2
  • 59
    • 0033673428 scopus 로고    scopus 로고
    • DFF45/ICAD can be directly processed by granzyme B during the induction of apoptosis
    • Thomas DA, Du C, Xu M, Wang X, Ley TJ. DFF45/ICAD can be directly processed by granzyme B during the induction of apoptosis. Immunity (2000) 12:621-32. doi:10.1016/S1074-7613(00)80213-7
    • (2000) Immunity , vol.12 , pp. 621-632
    • Thomas, D.A.1    Du, C.2    Xu, M.3    Wang, X.4    Ley, T.J.5
  • 60
    • 0037423932 scopus 로고    scopus 로고
    • Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor
    • Fan Z, Beresford PJ, Oh DY, Zhang D, Lieberman J. Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor. Cell (2003) 112:659-72. doi:10.1016/S0092-8674(03)00150-8
    • (2003) Cell , vol.112 , pp. 659-672
    • Fan, Z.1    Beresford, P.J.2    Oh, D.Y.3    Zhang, D.4    Lieberman, J.5
  • 62
    • 0030723209 scopus 로고    scopus 로고
    • In vitro- and ex vivo-derived cytolytic leukocytes from granzyme A x B double knockout mice are defective in granule-mediated apoptosis but not lysis of target cells
    • Simon MM, Hausmann M, Tran T, Ebnet K, Tschopp J, ThaHla R, et al. In vitro- and ex vivo-derived cytolytic leukocytes from granzyme A x B double knockout mice are defective in granule-mediated apoptosis but not lysis of target cells. J Exp Med (1997) 186:1781-6. doi:10.1084/jem.186.10.1781
    • (1997) J Exp Med , vol.186 , pp. 1781-1786
    • Simon, M.M.1    Hausmann, M.2    Tran, T.3    Ebnet, K.4    Tschopp, J.5    ThaHla, R.6
  • 63
    • 33645742877 scopus 로고    scopus 로고
    • Cytotoxic T lymphocyte-induced killing in the absence of granzymes A and B is unique and distinct from both apoptosis and perforin-dependent lysis
    • Waterhouse NJ, Sutton KA, Fau-Sedelies VR, Sedelies A, Fau-Ciccone KA, Ciccone M, et al. Cytotoxic T lymphocyte-induced killing in the absence of granzymes A and B is unique and distinct from both apoptosis and perforin-dependent lysis. J Cell Biol (2006) 173:133-44.
    • (2006) J Cell Biol , vol.173 , pp. 133-144
    • Waterhouse, N.J.1    Sutton, K.A.2    Fau-Sedelies, V.R.3    Sedelies, A.4    Fau-Ciccone, K.A.5    Ciccone, M.6
  • 64
    • 8444249247 scopus 로고    scopus 로고
    • Apoptotic pathways are selectively activated by granzyme A and/or granzyme B in CTL-mediated target cell lysis
    • Pardo J, Bosque A, Brehm R, Wallich R, Naval J, Mullbacher A, et al. Apoptotic pathways are selectively activated by granzyme A and/or granzyme B in CTL-mediated target cell lysis. J Cell Biol (2004) 167:457-68. doi:10.1083/jcb.200406115
    • (2004) J Cell Biol , vol.167 , pp. 457-468
    • Pardo, J.1    Bosque, A.2    Brehm, R.3    Wallich, R.4    Naval, J.5    Mullbacher, A.6
  • 65
    • 55349138368 scopus 로고    scopus 로고
    • Human and mouse granzyme A induce a proinflammatory cytokine response
    • Metkar SS, Menaa C, Pardo J, Wang B, Wallich R, Freudenberg M, et al. Human and mouse granzyme A induce a proinflammatory cytokine response. Immunity (2008) 29:720-33. doi:10.1016/j.immuni.2008.08.014
    • (2008) Immunity , vol.29 , pp. 720-733
    • Metkar, S.S.1    Menaa, C.2    Pardo, J.3    Wang, B.4    Wallich, R.5    Freudenberg, M.6
  • 66
    • 21244505889 scopus 로고    scopus 로고
    • Extracellular matrix remodeling by human granzyme B via cleavage of vitronectin, fibronectin, and laminin
    • Buzza MS, Zamurs L, Sun J, Bird CH, Smith AI, Trapani JA, et al. Extracellular matrix remodeling by human granzyme B via cleavage of vitronectin, fibronectin, and laminin. J Biol Chem (2005) 280:23549-58. doi:10.1074/jbc. M412001200
    • (2005) J Biol Chem , vol.280 , pp. 23549-23558
    • Buzza, M.S.1    Zamurs, L.2    Sun, J.3    Bird, C.H.4    Smith, A.I.5    Trapani, J.A.6
  • 67
    • 33747144028 scopus 로고    scopus 로고
    • Granzyme B is critical for T cell receptor-induced cell death of type 2 helper T cells
    • Devadas S, Das J, Liu C, Zhang L, Roberts AI, Pan Z, et al. Granzyme B is critical for T cell receptor-induced cell death of type 2 helper T cells. Immunity (2006) 25:237-47. doi:10.1016/j.immuni.2006.06.011
    • (2006) Immunity , vol.25 , pp. 237-247
    • Devadas, S.1    Das, J.2    Liu, C.3    Zhang, L.4    Roberts, A.I.5    Pan, Z.6
  • 68
    • 0041969798 scopus 로고    scopus 로고
    • A novel domain in adenovirus L4-100K is required for stable binding and efficient inhibition of human granzyme B: possible interaction with a species-specific exosite
    • Andrade F, Casciola-Rosen LA, Rosen A. A novel domain in adenovirus L4-100K is required for stable binding and efficient inhibition of human granzyme B: possible interaction with a species-specific exosite. Mol Cell Biol (2003) 23:6315-26. doi:10.1128/MCB.23.17.6315-6326.2003
    • (2003) Mol Cell Biol , vol.23 , pp. 6315-6326
    • Andrade, F.1    Casciola-Rosen, L.A.2    Rosen, A.3
  • 69
    • 84875529000 scopus 로고    scopus 로고
    • Control of human viral infections by natural killer cells
    • Jost S, Altfeld M. Control of human viral infections by natural killer cells. Annu Rev Immunol (2013) 31:163-94. doi:10.1146/annurev-immunol-032712-100001
    • (2013) Annu Rev Immunol , vol.31 , pp. 163-194
    • Jost, S.1    Altfeld, M.2
  • 70
    • 0036831613 scopus 로고    scopus 로고
    • New aspects of natural-killer-cell surveillance and therapy of cancer
    • Smyth MJ, Hayakawa Y, Takeda K, Yagita H. New aspects of natural-killer-cell surveillance and therapy of cancer. Nat Rev Cancer (2002) 2:850-61. doi:10.1038/nrc928
    • (2002) Nat Rev Cancer , vol.2 , pp. 850-861
    • Smyth, M.J.1    Hayakawa, Y.2    Takeda, K.3    Yagita, H.4
  • 71
    • 84876134219 scopus 로고    scopus 로고
    • Granule exocytosis mediates immune surveillance of senescent cells
    • Sagiv A, Biran A, Yon M, Simon J, Lowe SW, Krizhanovsky V. Granule exocytosis mediates immune surveillance of senescent cells. Oncogene (2013) 32:1971-7. doi:10.1038/onc.2012.206
    • (2013) Oncogene , vol.32 , pp. 1971-1977
    • Sagiv, A.1    Biran, A.2    Yon, M.3    Simon, J.4    Lowe, S.W.5    Krizhanovsky, V.6
  • 72
    • 50949124847 scopus 로고    scopus 로고
    • Human natural killer cells
    • Caligiuri MA. Human natural killer cells. Blood (2008) 112:461-9. doi:10.1182/blood-2007-09-077438
    • (2008) Blood , vol.112 , pp. 461-469
    • Caligiuri, M.A.1
  • 73
    • 79551666576 scopus 로고    scopus 로고
    • Revisiting human natural killer cell subset function revealed cytolytic CD56(dim)CD16+ NK cells as rapid producers of abundant IFN-gamma on activation
    • De Maria A, Bozzano F, Cantoni C, Moretta L. Revisiting human natural killer cell subset function revealed cytolytic CD56(dim)CD16+ NK cells as rapid producers of abundant IFN-gamma on activation. Proc Natl Acad Sci U S A (2011) 108:728-32. doi:10.1073/pnas.1012356108
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 728-732
    • De Maria, A.1    Bozzano, F.2    Cantoni, C.3    Moretta, L.4
  • 74
    • 0029962753 scopus 로고    scopus 로고
    • Immune regulation: a critical link between NK cells and CTLs
    • Kos FJ, Engleman EG. Immune regulation: a critical link between NK cells and CTLs. Immunol Today (1996) 17:174-6. doi:10.1016/0167-5699(96)80616-5
    • (1996) Immunol Today , vol.17 , pp. 174-176
    • Kos, F.J.1    Engleman, E.G.2
  • 75
    • 42449088897 scopus 로고    scopus 로고
    • Natural killer cell recognition of missing self
    • Karre K. Natural killer cell recognition of missing self. Nat Immunol (2008) 9:477-80. doi:10.1038/ni0508-477
    • (2008) Nat Immunol , vol.9 , pp. 477-480
    • Karre, K.1
  • 76
    • 0025300414 scopus 로고
    • In search of the 'missing self': MHC molecules and NK cell recognition
    • Ljunggren HG, Karre K. In search of the 'missing self': MHC molecules and NK cell recognition. Immunol Today (1990) 11:237-44. doi:10.1016/0167-5699(90)90097-S
    • (1990) Immunol Today , vol.11 , pp. 237-244
    • Ljunggren, H.G.1    Karre, K.2
  • 77
    • 1542380606 scopus 로고    scopus 로고
    • Unravelling natural killer cell function: triggering and inhibitory human NK receptors
    • Moretta L, Moretta A. Unravelling natural killer cell function: triggering and inhibitory human NK receptors. EMBO J (2004) 23:255-9. doi:10.1038/sj.emboj.7600019
    • (2004) EMBO J , vol.23 , pp. 255-259
    • Moretta, L.1    Moretta, A.2
  • 78
    • 42449102990 scopus 로고    scopus 로고
    • Up on the tightrope: natural killer cell activation and inhibition
    • Lanier LL. Up on the tightrope: natural killer cell activation and inhibition. Nat Immunol (2008) 9:495-502. doi:10.1038/ni1581
    • (2008) Nat Immunol , vol.9 , pp. 495-502
    • Lanier, L.L.1
  • 79
    • 84875528678 scopus 로고    scopus 로고
    • Controlling natural killer cell responses: integration of signals for activation and inhibition
    • Long EO, Kim HS, Liu D, Peterson ME, Rajagopalan S. Controlling natural killer cell responses: integration of signals for activation and inhibition. Annu Rev Immunol (2013) 31:227-58. doi:10.1146/annurev-immunol-020711-075005
    • (2013) Annu Rev Immunol , vol.31 , pp. 227-258
    • Long, E.O.1    Kim, H.S.2    Liu, D.3    Peterson, M.E.4    Rajagopalan, S.5
  • 80
    • 51149108034 scopus 로고    scopus 로고
    • The killer's kiss: the many functions of NK cell immunological synapses
    • Krzewski K, Strominger JL. The killer's kiss: the many functions of NK cell immunological synapses. Curr Opin Cell Biol (2008) 20:597-605. doi:10.1016/j.ceb.2008.05.006
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 597-605
    • Krzewski, K.1    Strominger, J.L.2
  • 81
    • 33750686595 scopus 로고    scopus 로고
    • Human natural killer cell development
    • Freud AG, Caligiuri MA. Human natural killer cell development. Immunol Rev (2006) 214:56-72. doi:10.1111/j.1600-065X.2006.00451.x
    • (2006) Immunol Rev , vol.214 , pp. 56-72
    • Freud, A.G.1    Caligiuri, M.A.2
  • 82
    • 33845252269 scopus 로고    scopus 로고
    • Coordinated acquisition of inhibitory and activating receptors and functional properties by developing human natural killer cells
    • Grzywacz B, Kataria N, Sikora M, Oostendorp RA, Dzierzak EA, Blazar BR, et al. Coordinated acquisition of inhibitory and activating receptors and functional properties by developing human natural killer cells. Blood (2006) 108:3824-33. doi:10.1182/blood-2006-04-020198
    • (2006) Blood , vol.108 , pp. 3824-3833
    • Grzywacz, B.1    Kataria, N.2    Sikora, M.3    Oostendorp, R.A.4    Dzierzak, E.A.5    Blazar, B.R.6
  • 83
    • 26844581032 scopus 로고    scopus 로고
    • Natural-killer cells and dendritic cells: "l'union fait la force"
    • Walzer T, Dalod M, Robbins SH, Zitvogel L, Vivier E. Natural-killer cells and dendritic cells: "l'union fait la force". Blood (2005) 106:2252-8. doi:10.1182/blood-2005-03-1154
    • (2005) Blood , vol.106 , pp. 2252-2258
    • Walzer, T.1    Dalod, M.2    Robbins, S.H.3    Zitvogel, L.4    Vivier, E.5
  • 84
    • 0347994957 scopus 로고    scopus 로고
    • NK cells regulate CD8+ T cell effector function in response to an intracellular pathogen
    • Vankayalapati R, Klucar P, Wizel B, Weis SE, Samten B, SafiH, et al. NK cells regulate CD8+ T cell effector function in response to an intracellular pathogen. J Immunol (2004) 172:130-7. doi:10.4049/jimmunol.172.1.130
    • (2004) J Immunol , vol.172 , pp. 130-137
    • Vankayalapati, R.1    Klucar, P.2    Wizel, B.3    Weis, S.E.4    Samten, B.5    Safi, H.6
  • 85
    • 77955376568 scopus 로고    scopus 로고
    • Increased lysis of stem cells but not their differentiated cells by natural killer cells; de-differentiation or reprogramming activates NK cells
    • Tseng HC, Arasteh A, Paranjpe A, Teruel A, Yang W, Behel A, et al. Increased lysis of stem cells but not their differentiated cells by natural killer cells; de-differentiation or reprogramming activates NK cells. PLoS One (2010) 5:e11590. doi:10.1371/journal.pone.0011590
    • (2010) PLoS One , vol.5 , pp. e11590
    • Tseng, H.C.1    Arasteh, A.2    Paranjpe, A.3    Teruel, A.4    Yang, W.5    Behel, A.6
  • 86
    • 84911476031 scopus 로고    scopus 로고
    • Natural killer cells as effectors of selection and differentiation of stem cells: role in resolution of inflammation
    • Jewett A, Man YG, Cacalano N, Kos J, Tseng HC. Natural killer cells as effectors of selection and differentiation of stem cells: role in resolution of inflammation. J Immunotoxicol (2014) 11:297-307. doi:10.3109/1547691X.2013.877104
    • (2014) J Immunotoxicol , vol.11 , pp. 297-307
    • Jewett, A.1    Man, Y.G.2    Cacalano, N.3    Kos, J.4    Tseng, H.C.5
  • 87
    • 33645812129 scopus 로고    scopus 로고
    • Regulatory CD56(bright) natural killer cells mediate immunomodulatory effects of IL-2Ralpha-targeted therapy (daclizumab) in multiple sclerosis
    • Bielekova B, Catalfamo M, Reichert-Scrivner S, Packer A, Cerna M, Waldmann TA, et al. Regulatory CD56(bright) natural killer cells mediate immunomodulatory effects of IL-2Ralpha-targeted therapy (daclizumab) in multiple sclerosis. Proc Natl Acad Sci U S A (2006) 103:5941-6. doi:10.1073/pnas.0601335103
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 5941-5946
    • Bielekova, B.1    Catalfamo, M.2    Reichert-Scrivner, S.3    Packer, A.4    Cerna, M.5    Waldmann, T.A.6
  • 88
    • 0037378748 scopus 로고    scopus 로고
    • Activated, but not resting T cells can be recognized and killed by syngeneic NK cells
    • Rabinovich BA, Li J, Shannon J, Hurren R, Chalupny J, Cosman D, et al. Activated, but not resting, T cells can be recognized and killed by syngeneic NK cells. J Immunol (2003) 170:3572-6. doi:10.4049/jimmunol.170.7.3572
    • (2003) J Immunol , vol.170 , pp. 3572-3576
    • Rabinovich, B.A.1    Li, J.2    Shannon, J.3    Hurren, R.4    Chalupny, J.5    Cosman, D.6
  • 89
    • 50249184550 scopus 로고    scopus 로고
    • Formation and function of the lytic NK-cell immunological synapse
    • Orange JS. Formation and function of the lytic NK-cell immunological synapse. Nat Rev Immunol (2008) 8:713-25. doi:10.1038/nri2381
    • (2008) Nat Rev Immunol , vol.8 , pp. 713-725
    • Orange, J.S.1
  • 90
    • 79960547202 scopus 로고    scopus 로고
    • Unexpected role for granzyme K in CD56bright NK cell-mediated immunoregulation of multiple sclerosis
    • Jiang W, Chai NR, Maric D, Bielekova B. Unexpected role for granzyme K in CD56bright NK cell-mediated immunoregulation of multiple sclerosis. J Immunol (2011) 187:781-90. doi:10.4049/jimmunol.1100789
    • (2011) J Immunol , vol.187 , pp. 781-790
    • Jiang, W.1    Chai, N.R.2    Maric, D.3    Bielekova, B.4
  • 91
    • 59049094662 scopus 로고    scopus 로고
    • Adaptive immune features of natural killer cells
    • Sun JC, Beilke JN, Lanier LL. Adaptive immune features of natural killer cells. Nature (2009) 457:557-61. doi:10.1038/nature07665
    • (2009) Nature , vol.457 , pp. 557-561
    • Sun, J.C.1    Beilke, J.N.2    Lanier, L.L.3
  • 93
    • 84863338121 scopus 로고    scopus 로고
    • Cytomegalovirus reactivation after allogeneic transplantation promotes a lasting increase in educated NKG2C+ natural killer cells with potent function
    • Foley B, Cooley S, Verneris MR, Pitt M, Curtsinger J, Luo X, et al. Cytomegalovirus reactivation after allogeneic transplantation promotes a lasting increase in educated NKG2C+ natural killer cells with potent function. Blood (2012) 119:2665-74. doi:10.1182/blood-2011-10-386995
    • (2012) Blood , vol.119 , pp. 2665-2674
    • Foley, B.1    Cooley, S.2    Verneris, M.R.3    Pitt, M.4    Curtsinger, J.5    Luo, X.6
  • 94
    • 80052602721 scopus 로고    scopus 로고
    • Expansion of a unique CD57(+)NKG2Chi natural killer cell subset during acute human cytomegalovirus infection
    • Lopez-Verges S, Milush JM, Schwartz BS, Pando MJ, Jarjoura J, York VA, et al. Expansion of a unique CD57(+)NKG2Chi natural killer cell subset during acute human cytomegalovirus infection. Proc Natl Acad Sci U S A (2011) 108:14725-32. doi:10.1073/pnas.1110900108
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 14725-14732
    • Lopez-Verges, S.1    Milush, J.M.2    Schwartz, B.S.3    Pando, M.J.4    Jarjoura, J.5    York, V.A.6
  • 95
    • 39749157121 scopus 로고    scopus 로고
    • Expression of T-cell receptor genes during early T-cell development
    • Abbey JL, O'Neill HC. Expression of T-cell receptor genes during early T-cell development. Immunol Cell Biol (2008) 86:166-74. doi:10.1038/sj.icb.7100120
    • (2008) Immunol Cell Biol , vol.86 , pp. 166-174
    • Abbey, J.L.1    O'Neill, H.C.2
  • 96
    • 0025175087 scopus 로고
    • The activation of resting lymphocytes is accompanied by the biogenesis of lysosomal organelles
    • Olsen I, Bou-Gharios G, Abraham D. The activation of resting lymphocytes is accompanied by the biogenesis of lysosomal organelles. Eur J Immunol (1990) 20:2161-70. doi:10.1002/eji.1830201003
    • (1990) Eur J Immunol , vol.20 , pp. 2161-2170
    • Olsen, I.1    Bou-Gharios, G.2    Abraham, D.3
  • 97
    • 0023952461 scopus 로고
    • Ultrastructural localization of a lysosomal enzyme in resin-embedded lymphocytes
    • Bou-Gharios G, Moss J, Olsen I, Partridge T. Ultrastructural localization of a lysosomal enzyme in resin-embedded lymphocytes. Histochemistry (1988) 89:69-74. doi:10.1007/BF00496587
    • (1988) Histochemistry , vol.89 , pp. 69-74
    • Bou-Gharios, G.1    Moss, J.2    Olsen, I.3    Partridge, T.4
  • 98
    • 0025885771 scopus 로고
    • T-cell effector functions: mechanisms for delivery of cytotoxicity and help
    • Podack ER, Kupfer A. T-cell effector functions: mechanisms for delivery of cytotoxicity and help. Annu Rev Cell Biol (1991) 7:479-504. doi:10.1146/annurev.cellbio.7.1.479
    • (1991) Annu Rev Cell Biol , vol.7 , pp. 479-504
    • Podack, E.R.1    Kupfer, A.2
  • 99
    • 0036229026 scopus 로고    scopus 로고
    • Structural basis of T cell recognition of peptides bound to MHC molecules
    • Wang JH, Reinherz EL. Structural basis of T cell recognition of peptides bound to MHC molecules. Mol Immunol (2002) 38:1039-49. doi:10.1016/S0161-5890(02)00033-0
    • (2002) Mol Immunol , vol.38 , pp. 1039-1049
    • Wang, J.H.1    Reinherz, E.L.2
  • 100
    • 0036200757 scopus 로고    scopus 로고
    • CD28 function: a balance of costimulatory and regulatory signals
    • Bour-Jordan H, Blueston JA. CD28 function: a balance of costimulatory and regulatory signals. J Clin Immunol (2002) 22:1-7. doi:10.1023/A:1014256417651
    • (2002) J Clin Immunol , vol.22 , pp. 1-7
    • Bour-Jordan, H.1    Blueston, J.A.2
  • 101
    • 38449096740 scopus 로고    scopus 로고
    • Secretory mechanisms in cell-mediated cytotoxicity
    • Stinchcombe JC, Griffiths GM. Secretory mechanisms in cell-mediated cytotoxicity. Annu Rev Cell Dev Biol (2007) 23:495-517. doi:10.1146/annurev.cellbio.23.090506.123521
    • (2007) Annu Rev Cell Dev Biol , vol.23 , pp. 495-517
    • Stinchcombe, J.C.1    Griffiths, G.M.2
  • 102
    • 0028914352 scopus 로고
    • Serial killing by cytotoxic T lymphocytes: T cell receptor triggers degranulation, re-filling of the lytic granules and secretion of lytic proteins via a non-granule pathway
    • Isaaz S, Baetz K, Olsen K, Podack E, Griffiths GM. Serial killing by cytotoxic T lymphocytes: T cell receptor triggers degranulation, re-filling of the lytic granules and secretion of lytic proteins via a non-granule pathway. Eur J Immunol (1995) 25:1071-9. doi:10.1002/eji.1830250432
    • (1995) Eur J Immunol , vol.25 , pp. 1071-1079
    • Isaaz, S.1    Baetz, K.2    Olsen, K.3    Podack, E.4    Griffiths, G.M.5
  • 103
    • 5644302161 scopus 로고    scopus 로고
    • Human T regulatory cells can use the perforin pathway to cause autologous target cell death
    • Grossman WJ, Verbsky JW, Barchet W, Colonna M, Atkinson JP, Ley TJ. Human T regulatory cells can use the perforin pathway to cause autologous target cell death. Immunity (2004) 21:589-601. doi:10.1016/j.immuni.2004.09.002
    • (2004) Immunity , vol.21 , pp. 589-601
    • Grossman, W.J.1    Verbsky, J.W.2    Barchet, W.3    Colonna, M.4    Atkinson, J.P.5    Ley, T.J.6
  • 104
    • 13544271161 scopus 로고    scopus 로고
    • Cutting edge: contact-mediated suppression by CD4+CD25+ regulatory cells involves a granzyme B-dependent, perforin-independent mechanism
    • Gondek DC, Lu LF, Quezada SA, Sakaguchi S, Noelle RJ. Cutting edge: contact-mediated suppression by CD4+CD25+ regulatory cells involves a granzyme B-dependent, perforin-independent mechanism. J Immunol (2005) 174:1783-6. doi:10.4049/jimmunol.174.4.1783
    • (2005) J Immunol , vol.174 , pp. 1783-1786
    • Gondek, D.C.1    Lu, L.F.2    Quezada, S.A.3    Sakaguchi, S.4    Noelle, R.J.5
  • 105
    • 33646567156 scopus 로고    scopus 로고
    • Activated CD4+CD25+ T cells selectively kill B lymphocytes
    • Zhao DM, Thornton AM, DiPaolo RJ, Shevach EM. Activated CD4+CD25+ T cells selectively kill B lymphocytes. Blood (2006) 107:3925-32. doi:10.1182/blood-2005-11-4502
    • (2006) Blood , vol.107 , pp. 3925-3932
    • Zhao, D.M.1    Thornton, A.M.2    DiPaolo, R.J.3    Shevach, E.M.4
  • 106
    • 14844340568 scopus 로고    scopus 로고
    • Differential lysosomal proteolysis in antigen-presenting cells determines antigen fate
    • Delamarre L, Pack M, Chang H, Mellman I, Trombetta ES. Differential lysosomal proteolysis in antigen-presenting cells determines antigen fate. Science (2005) 307:1630-4. doi:10.1126/science.1108003
    • (2005) Science , vol.307 , pp. 1630-1634
    • Delamarre, L.1    Pack, M.2    Chang, H.3    Mellman, I.4    Trombetta, E.S.5
  • 107
    • 0030897071 scopus 로고    scopus 로고
    • Human dipeptidyl-peptidase I. Gene characterization, localization, and expression
    • Rao NV, Rao GV, Hoidal JR. Human dipeptidyl-peptidase I. Gene characterization, localization, and expression. J Biol Chem (1997) 272:10260-5. doi:10.1074/jbc.272.15.10260
    • (1997) J Biol Chem , vol.272 , pp. 10260-10265
    • Rao, N.V.1    Rao, G.V.2    Hoidal, J.R.3
  • 108
    • 0032546934 scopus 로고    scopus 로고
    • Regulated expression, processing, and secretion of dog mast cell dipeptidyl peptidase I
    • Wolters PJ, Raymond WW, Blount JL, Caughey GH. Regulated expression, processing, and secretion of dog mast cell dipeptidyl peptidase I. J Biol Chem (1998) 273:15514-20. doi:10.1074/jbc.273.25.15514
    • (1998) J Biol Chem , vol.273 , pp. 15514-15520
    • Wolters, P.J.1    Raymond, W.W.2    Blount, J.L.3    Caughey, G.H.4
  • 109
    • 0034930012 scopus 로고    scopus 로고
    • Immunochemical localisation of cathepsin S, cathepsin L and MHC class II-associated p41 isoform of invariant chain in human lymph node tissue
    • Zavasnik-Bergant V, Sekirnik A, Golouh R, Turk V, Kos J. Immunochemical localisation of cathepsin S, cathepsin L and MHC class II-associated p41 isoform of invariant chain in human lymph node tissue. Biol Chem (2001) 382:799-804.
    • (2001) Biol Chem , vol.382 , pp. 799-804
    • Zavasnik-Bergant, V.1    Sekirnik, A.2    Golouh, R.3    Turk, V.4    Kos, J.5
  • 110
    • 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) 37:266-75. doi:10.1016/j.exphem.2008.10.011
    • (2009) Exp Hematol , vol.37 , pp. 266-275
    • Stoeckle, C.1    Gouttefangeas, C.2    Hammer, M.3    Weber, E.4    Melms, A.5    Tolosa, E.6
  • 111
    • 0037454948 scopus 로고    scopus 로고
    • Differential regulation of cathepsin S and cathepsin L in interferon gamma-treated macrophages
    • Beers C, Honey K, Fink S, Forbush K, Rudensky A. Differential regulation of cathepsin S and cathepsin L in interferon gamma-treated macrophages. J Exp Med (2003) 197:169-79. doi:10.1084/jem.20020978
    • (2003) J Exp Med , vol.197 , pp. 169-179
    • Beers, C.1    Honey, K.2    Fink, S.3    Forbush, K.4    Rudensky, A.5
  • 112
    • 0033083688 scopus 로고    scopus 로고
    • Cathepsin S required for normal MHC class II peptide loading and germinal center development
    • Shi GP, Villadangos JA, DranoffG, Small C, Gu L, Haley KJ, et al. Cathepsin S required for normal MHC class II peptide loading and germinal center development. Immunity (1999) 10:197-206. doi:10.1016/S1074-7613(00)80020-5
    • (1999) Immunity , vol.10 , pp. 197-206
    • Shi, G.P.1    Villadangos, J.A.2    Dranoff, G.3    Small, C.4    Gu, L.5    Haley, K.J.6
  • 113
    • 21044440422 scopus 로고    scopus 로고
    • Carboxypeptidases cathepsins X and B display distinct protein profile in human cells and tissues
    • Kos J, Sekirnik A, Premzl A, Zavasnik-Bergant V, Langerholc T, Turk B, et al. Carboxypeptidases cathepsins X and B display distinct protein profile in human cells and tissues. Exp Cell Res (2005) 306:103-13. doi:10.1016/j.yexcr.2004.12.006
    • (2005) Exp Cell Res , vol.306 , pp. 103-113
    • Kos, J.1    Sekirnik, A.2    Premzl, A.3    Zavasnik-Bergant, V.4    Langerholc, T.5    Turk, B.6
  • 114
    • 84896549845 scopus 로고    scopus 로고
    • Cysteine cathepsins in neurological disorders
    • Pislar A, Kos J. Cysteine cathepsins in neurological disorders. Mol Neurobiol (2014) 49:1017-30. doi:10.1007/s12035-013-8576-6
    • (2014) Mol Neurobiol , vol.49 , pp. 1017-1030
    • Pislar, A.1    Kos, J.2
  • 115
    • 33745824230 scopus 로고    scopus 로고
    • Carboxypeptidase cathepsin X mediates beta2-integrin-dependent adhesion of differentiated U-937 cells
    • Obermajer N, Premzl A, Zavasnik-Bergant T, Turk B, Kos J. Carboxypeptidase cathepsin X mediates beta2-integrin-dependent adhesion of differentiated U-937 cells. Exp Cell Res (2006) 312:2515-27. doi:10.1016/j.yexcr.2006.04.019
    • (2006) Exp Cell Res , vol.312 , pp. 2515-2527
    • Obermajer, N.1    Premzl, A.2    Zavasnik-Bergant, T.3    Turk, B.4    Kos, J.5
  • 116
    • 55549089642 scopus 로고    scopus 로고
    • Maturation of dendritic cells depends on proteolytic cleavage by cathepsin X
    • Obermajer N, SVajger U, Bogyo M, Jeras M, Kos J. Maturation of dendritic cells depends on proteolytic cleavage by cathepsin X. J Leukoc Biol (2008) 84:1306-15. doi:10.1189/jlb.0508285
    • (2008) J Leukoc Biol , vol.84 , pp. 1306-1315
    • Obermajer, N.1    Svajger, U.2    Bogyo, M.3    Jeras, M.4    Kos, J.5
  • 117
    • 0032479144 scopus 로고    scopus 로고
    • Cathepsin Z, a novel human cysteine proteinase with a short propeptide domain and a unique chromosomal location
    • Santamaria I, Velasco G, Pendas AM, Fueyo A, Lopez-Otin C. Cathepsin Z, a novel human cysteine proteinase with a short propeptide domain and a unique chromosomal location. J Biol Chem (1998) 273:16816-23. doi:10.1074/jbc.273.27.16816
    • (1998) J Biol Chem , vol.273 , pp. 16816-16823
    • Santamaria, I.1    Velasco, G.2    Pendas, A.M.3    Fueyo, A.4    Lopez-Otin, C.5
  • 118
    • 0040234054 scopus 로고    scopus 로고
    • Human cathepsin X: a novel cysteine protease of the papain family with a very short proregion and unique insertions
    • Nagler DK, Menard R. Human cathepsin X: a novel cysteine protease of the papain family with a very short proregion and unique insertions. FEBS Lett (1998) 434:135-9. doi:10.1016/S0014-5793(98)00964-8
    • (1998) FEBS Lett , vol.434 , pp. 135-139
    • Nagler, D.K.1    Menard, R.2
  • 119
    • 33845986378 scopus 로고    scopus 로고
    • RGD-dependent binding of procathepsin X to integrin alphavbeta3 mediates cell-adhesive properties
    • Lechner AM, Assfalg-Machleidt I, Zahler S, Stoeckelhuber M, Machleidt W, Jochum M, et al. RGD-dependent binding of procathepsin X to integrin alphavbeta3 mediates cell-adhesive properties. J Biol Chem (2006) 281:39588-97. doi:10.1074/jbc. M513439200
    • (2006) J Biol Chem , vol.281 , pp. 39588-39597
    • Lechner, A.M.1    Assfalg-Machleidt, I.2    Zahler, S.3    Stoeckelhuber, M.4    Machleidt, W.5    Jochum, M.6
  • 120
    • 79959840888 scopus 로고    scopus 로고
    • Cathepsin X cleavage of the beta2 integrin regulates talin-binding and LFA-1 affinity in T cells
    • Jevnikar Z, Obermajer N, Doljak B, Turk S, Gobec S, Svajger U, et al. Cathepsin X cleavage of the beta2 integrin regulates talin-binding and LFA-1 affinity in T cells. J Leukoc Biol (2011) 90:99-109. doi:10.1189/jlb.1110622
    • (2011) J Leukoc Biol , vol.90 , pp. 99-109
    • Jevnikar, Z.1    Obermajer, N.2    Doljak, B.3    Turk, S.4    Gobec, S.5    Svajger, U.6
  • 121
    • 80052086902 scopus 로고    scopus 로고
    • LFA-1 fine-tuning by cathepsin X
    • Jevnikar Z, Obermajer N, Kos J. LFA-1 fine-tuning by cathepsin X. IUBMB Life (2011) 63:686-93. doi:10.1002/iub.505
    • (2011) IUBMB Life , vol.63 , pp. 686-693
    • Jevnikar, Z.1    Obermajer, N.2    Kos, J.3
  • 122
    • 69949133985 scopus 로고    scopus 로고
    • Intra- versus extracellular effects of microglia-derived cysteine proteases in a conditioned medium transfer model
    • Wendt W, Schulten R, Stichel CC, Lubbert H. Intra- versus extracellular effects of microglia-derived cysteine proteases in a conditioned medium transfer model. J Neurochem (2009) 110:1931-41. doi:10.1111/j.1471-4159.2009.06283.x
    • (2009) J Neurochem , vol.110 , pp. 1931-1941
    • Wendt, W.1    Schulten, R.2    Stichel, C.C.3    Lubbert, H.4
  • 123
    • 33845768784 scopus 로고    scopus 로고
    • Microglia-mediated neurotoxicity: uncovering the molecular mechanisms
    • Block ML, Zecca L, Hong JS. Microglia-mediated neurotoxicity: uncovering the molecular mechanisms. Nat Rev Neurosci (2007) 8:57-69. doi:10.1038/nrn2038
    • (2007) Nat Rev Neurosci , vol.8 , pp. 57-69
    • Block, M.L.1    Zecca, L.2    Hong, J.S.3
  • 124
    • 0036168150 scopus 로고    scopus 로고
    • Dipeptidyl peptidase I activates neutrophil-derived serine proteases and regulates the development of acute experimental arthritis
    • Adkison AM, Raptis SZ, Kelley DG, Pham CT. Dipeptidyl peptidase I activates neutrophil-derived serine proteases and regulates the development of acute experimental arthritis. J Clin Invest (2002) 109:363-71. doi:10.1172/JCI13462
    • (2002) J Clin Invest , vol.109 , pp. 363-371
    • Adkison, A.M.1    Raptis, S.Z.2    Kelley, D.G.3    Pham, C.T.4
  • 125
    • 10344234724 scopus 로고    scopus 로고
    • Papillon-Lefevre syndrome: correlating the molecular, cellular, and clinical consequences of cathepsin C/dipeptidyl peptidase I deficiency in humans
    • Pham CT, Ivanovich JL, Raptis SZ, Zehnbauer B, Ley TJ. Papillon-Lefevre syndrome: correlating the molecular, cellular, and clinical consequences of cathepsin C/dipeptidyl peptidase I deficiency in humans. J Immunol (2004) 173:7277-81. doi:10.4049/jimmunol.173.12.7277
    • (2004) J Immunol , vol.173 , pp. 7277-7281
    • Pham, C.T.1    Ivanovich, J.L.2    Raptis, S.Z.3    Zehnbauer, B.4    Ley, T.J.5
  • 126
    • 4444343709 scopus 로고    scopus 로고
    • Loss-of-function mutations in cathepsin C in two families with Papillon-Lefevre syndrome are associated with deficiency of serine proteinases in PMNs
    • de Haar SF, Jansen DC, Schoenmaker T, De Vree H, Everts V, Beertsen W. Loss-of-function mutations in cathepsin C in two families with Papillon-Lefevre syndrome are associated with deficiency of serine proteinases in PMNs. Hum Mutat (2004) 23:524. doi:10.1002/humu.9243
    • (2004) Hum Mutat , vol.23 , pp. 524
    • de Haar, S.F.1    Jansen, D.C.2    Schoenmaker, T.3    De Vree, H.4    Everts, V.5    Beertsen, W.6
  • 127
    • 0035947568 scopus 로고    scopus 로고
    • Dipeptidyl peptidase I is essential for activation of mast cell chymases, but not tryptases, in mice
    • Wolters PJ, Pham CT, Muilenburg DJ, Ley TJ, Caughey GH. Dipeptidyl peptidase I is essential for activation of mast cell chymases, but not tryptases, in mice. J Biol Chem (2001) 276:18551-6. doi:10.1074/jbc. M100223200
    • (2001) J Biol Chem , vol.276 , pp. 18551-18556
    • Wolters, P.J.1    Pham, C.T.2    Muilenburg, D.J.3    Ley, T.J.4    Caughey, G.H.5
  • 128
    • 0035881830 scopus 로고    scopus 로고
    • Human cathepsin W, a cysteine protease predominantly expressed in NK cells, is mainly localized in the endoplasmic reticulum
    • Wex T, Buhling F, Wex H, Gunther D, Malfertheiner P, Weber E, et al. Human cathepsin W, a cysteine protease predominantly expressed in NK cells, is mainly localized in the endoplasmic reticulum. J Immunol (2001) 167:2172-8. doi:10.4049/jimmunol.167.4.2172
    • (2001) J Immunol , vol.167 , pp. 2172-2178
    • Wex, T.1    Buhling, F.2    Wex, H.3    Gunther, D.4    Malfertheiner, P.5    Weber, E.6
  • 129
    • 0037136311 scopus 로고    scopus 로고
    • Surface cathepsin B protects cytotoxic lymphocytes from self-destruction after degranulation
    • Balaji KN, Schaschke N, Machleidt W, Catalfamo M, Henkart PA. Surface cathepsin B protects cytotoxic lymphocytes from self-destruction after degranulation. J Exp Med (2002) 196:493-503. doi:10.1084/jem.20011836
    • (2002) J Exp Med , vol.196 , pp. 493-503
    • Balaji, K.N.1    Schaschke, N.2    Machleidt, W.3    Catalfamo, M.4    Henkart, P.A.5
  • 130
    • 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 PI, Villadangos JA, et al. 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) 281:30485-91. doi:10.1074/jbc. M602007200
    • (2006) J Biol Chem , vol.281 , pp. 30485-30491
    • Baran, K.1    Ciccone, A.2    Peters, C.3    Yagita, H.4    Bird, P.I.5    Villadangos, J.A.6
  • 131
    • 0033802292 scopus 로고    scopus 로고
    • Regulation of elastinolytic cysteine proteinase activity in normal and cathepsin K-deficient human macrophages
    • Punturieri A, Filippov S, Allen E, Caras I, Murray R, Reddy V, et al. Regulation of elastinolytic cysteine proteinase activity in normal and cathepsin K-deficient human macrophages. J Exp Med (2000) 192:789-99. doi:10.1084/jem.192.6.789
    • (2000) J Exp Med , vol.192 , pp. 789-799
    • Punturieri, A.1    Filippov, S.2    Allen, E.3    Caras, I.4    Murray, R.5    Reddy, V.6
  • 132
    • 79957931329 scopus 로고    scopus 로고
    • The unexpected link between osteoclasts and the immune system
    • Takayanagi H. The unexpected link between osteoclasts and the immune system. Adv Exp Med Biol (2010) 658:61-8. doi:10.1007/978-1-4419-1050-9_7
    • (2010) Adv Exp Med Biol , vol.658 , pp. 61-68
    • Takayanagi, H.1
  • 133
    • 77955935962 scopus 로고    scopus 로고
    • Human and mouse perforin are processed in part through cleavage by the lysosomal cysteine proteinase cathepsin L
    • Konjar S, Sutton VR, Hoves S, Repnik U, Yagita H, Reinheckel T, et al. Human and mouse perforin are processed in part through cleavage by the lysosomal cysteine proteinase cathepsin L. Immunology (2010) 131:257-67. doi:10.1111/j.1365-2567.2010.03299.x
    • (2010) Immunology , vol.131 , pp. 257-267
    • Konjar, S.1    Sutton, V.R.2    Hoves, S.3    Repnik, U.4    Yagita, H.5    Reinheckel, T.6
  • 134
    • 0027159814 scopus 로고
    • Dipeptidyl peptidase I is enriched in granules of in vitro- and in vivo-activated cytotoxic T lymphocytes
    • Brown GR, McGuire MJ, Thiele DL. Dipeptidyl peptidase I is enriched in granules of in vitro- and in vivo-activated cytotoxic T lymphocytes. J Immunol (1993) 150:4733-42.
    • (1993) J Immunol , vol.150 , pp. 4733-4742
    • Brown, G.R.1    McGuire, M.J.2    Thiele, D.L.3
  • 135
    • 33846990905 scopus 로고    scopus 로고
    • Residual active granzyme B in cathepsin C-null lymphocytes is sufficient for perforin-dependent target cell apoptosis
    • Sutton VR, Waterhouse NJ, Browne KA, Sedelies K, Ciccone A, Anthony D, et al. Residual active granzyme B in cathepsin C-null lymphocytes is sufficient for perforin-dependent target cell apoptosis. J Cell Biol (2007) 176:425-33. doi:10.1083/jcb.200609077
    • (2007) J Cell Biol , vol.176 , pp. 425-433
    • Sutton, V.R.1    Waterhouse, N.J.2    Browne, K.A.3    Sedelies, K.4    Ciccone, A.5    Anthony, D.6
  • 136
    • 0028132819 scopus 로고
    • Identification of acid cysteine proteinase inhibitor (cystatin A) in the human thymus
    • Soderstrom KO, Rinne R, Hopsu-Havu VK, Jarvinen M, Rinne A. Identification of acid cysteine proteinase inhibitor (cystatin A) in the human thymus. Anat Rec (1994) 240:115-9. doi:10.1002/ar.1092400111
    • (1994) Anat Rec , vol.240 , pp. 115-119
    • Soderstrom, K.O.1    Rinne, R.2    Hopsu-Havu, V.K.3    Jarvinen, M.4    Rinne, A.5
  • 137
    • 0343745748 scopus 로고
    • Human cystatins in normal and diseased tissues - a review
    • Jarvinen M, Rinne A, Hopsu-Havu VK. Human cystatins in normal and diseased tissues - a review. Acta Histochem (1987) 82:5-18. doi:10.1016/S0065-1281(87)80043-0
    • (1987) Acta Histochem , vol.82 , pp. 5-18
    • Jarvinen, M.1    Rinne, A.2    Hopsu-Havu, V.K.3
  • 138
    • 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) 272:1535-45. doi:10.1111/j.1742-4658.2005.04594.x
    • (2005) FEBS J , vol.272 , pp. 1535-1545
    • Langerholc, T.1    Zavasnik-Bergant, V.2    Turk, B.3    Turk, V.4    Abrahamson, M.5    Kos, J.6
  • 139
    • 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) 297:607-18. doi:10.1016/j.yexcr.2004.03.048
    • (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
  • 140
    • 84906267525 scopus 로고    scopus 로고
    • Cystatin F regulates proteinase activity in IL-2-activated natural killer cells
    • Maher K, Konjar S, Watts C, Turk B, Kopitar-Jerala N. Cystatin F regulates proteinase activity in IL-2-activated natural killer cells. Protein Pept Lett (2014) 21:957-65. doi:10.2174/0929866521666140403124146
    • (2014) Protein Pept Lett , vol.21 , pp. 957-965
    • Maher, K.1    Konjar, S.2    Watts, C.3    Turk, B.4    Kopitar-Jerala, N.5
  • 141
    • 38949174026 scopus 로고    scopus 로고
    • Cystatin F is a cathepsin C-directed protease inhibitor regulated by proteolysis
    • Hamilton G, Colbert JD, Schuettelkopf AW, Watts C. Cystatin F is a cathepsin C-directed protease inhibitor regulated by proteolysis. EMBO J (2008) 27:499-508. doi:10.1038/sj.emboj.7601979
    • (2008) EMBO J , vol.27 , pp. 499-508
    • Hamilton, G.1    Colbert, J.D.2    Schuettelkopf, A.W.3    Watts, C.4
  • 142
    • 0032569023 scopus 로고    scopus 로고
    • Leukocystatin, a new class II cystatin expressed selectively by hematopoietic cells
    • Halfon S, Ford J, Foster J, Dowling L, Lucian L, Sterling M, et al. Leukocystatin, a new class II cystatin expressed selectively by hematopoietic cells. J Biol Chem (1998) 273:16400-8. doi:10.1074/jbc.273.26.16400
    • (1998) J Biol Chem , vol.273 , pp. 16400-16408
    • Halfon, S.1    Ford, J.2    Foster, J.3    Dowling, L.4    Lucian, L.5    Sterling, M.6
  • 143
    • 0032544743 scopus 로고    scopus 로고
    • Cystatin F is a glycosylated human low molecular weight cysteine proteinase inhibitor
    • Ni J, Fernandez MA, Danielsson L, Chillakuru RA, Zhang J, Grubb A, et al. Cystatin F is a glycosylated human low molecular weight cysteine proteinase inhibitor. J Biol Chem (1998) 273:24797-804. doi:10.1074/jbc.273.38.24797
    • (1998) J Biol Chem , vol.273 , pp. 24797-24804
    • Ni, J.1    Fernandez, M.A.2    Danielsson, L.3    Chillakuru, R.A.4    Zhang, J.5    Grubb, A.6
  • 144
    • 84857788537 scopus 로고    scopus 로고
    • Regulation of cathepsins S and L by cystatin F during maturation of dendritic cells
    • Magister S, Obermajer N, Mirkovic B, Svajger U, Renko M, Softic A, et al. Regulation of cathepsins S and L by cystatin F during maturation of dendritic cells. Eur J Cell Biol (2012) 91:391-401. doi:10.1016/j.ejcb.2012.01.001
    • (2012) Eur J Cell Biol , vol.91 , pp. 391-401
    • Magister, S.1    Obermajer, N.2    Mirkovic, B.3    Svajger, U.4    Renko, M.5    Softic, A.6


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