메뉴 건너뛰기




Volumn 8, Issue 5-6, 2014, Pages 416-426

Cysteine cathepsins and their potential in clinical therapy and biomarker discovery

Author keywords

Biomarker; Cancer; Cathepsin; Cysteine protease; Proteolysis

Indexed keywords

BALICATIB; BIOLOGICAL MARKER; CATHEPSIN; CATHEPSIN B; CATHEPSIN H; CATHEPSIN K; CATHEPSIN K INHIBITOR; CATHEPSIN L; CATHEPSIN S; CATHEPSIN S INHIBITOR; CATHEPSIN X; CRA 028129; CYSTEINE CATHEPSIN; LOSARTAN; MATRIX METALLOPROTEINASE; MIV 711; ODANACATIB; ONO 5334; RELACATIB; RWJ 445380; UNCLASSIFIED DRUG; VBY 036; VBY 891; CYSTEINE;

EID: 84902081517     PISSN: 18628346     EISSN: 18628354     Source Type: Journal    
DOI: 10.1002/prca.201300085     Document Type: Review
Times cited : (50)

References (126)
  • 1
    • 84859366447 scopus 로고    scopus 로고
    • Protease signalling: the cutting edge
    • Turk, B., Turk, D., Turk, V., Protease signalling: the cutting edge. EMBO J. 2012, 31, 1630-1643.
    • (2012) EMBO J. , vol.31 , pp. 1630-1643
    • Turk, B.1    Turk, D.2    Turk, V.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, 785-799.
    • (2006) Nat. Rev. Drug Discov. , vol.5 , pp. 785-799
    • Turk, B.1
  • 3
    • 77956310878 scopus 로고    scopus 로고
    • Emerging principles in protease-based drug discovery
    • Drag, M., Salvesen, G. S., Emerging principles in protease-based drug discovery. Nat. Rev. Drug Discov. 2010, 9, 690-701.
    • (2010) Nat. Rev. Drug Discov. , vol.9 , pp. 690-701
    • Drag, M.1    Salvesen, G.S.2
  • 4
    • 0036716282 scopus 로고    scopus 로고
    • Strategies for MMP inhibition in cancer: innovations for the post-trial era
    • Overall, C. M., López-Otín, C., Strategies for MMP inhibition in cancer: innovations for the post-trial era. Nat. Rev. Cancer 2002, 2, 657-672.
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 657-672
    • Overall, C.M.1    López-Otín, C.2
  • 5
    • 0037192458 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors and cancer: trials and tribulations
    • Coussens, L. M., Fingleton, B., Matrisian, L. M., Matrix metalloproteinase inhibitors and cancer: trials and tribulations. Science 2002, 295, 2387-2392.
    • (2002) Science , vol.295 , pp. 2387-2392
    • Coussens, L.M.1    Fingleton, B.2    Matrisian, L.M.3
  • 6
    • 84859426282 scopus 로고    scopus 로고
    • MEROPS: the database of proteolytic enzymes, their substrates and inhibitors
    • Rawlings, N. D., Barrett, A. J., Bateman, A., MEROPS: the database of proteolytic enzymes, their substrates and inhibitors. Nucleic Acids Res. 2012, 40, D343-D350.
    • (2012) Nucleic Acids Res. , vol.40
    • Rawlings, N.D.1    Barrett, A.J.2    Bateman, A.3
  • 7
    • 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, 137-147.
    • (1998) Biol. Chem. , vol.379 , pp. 137-147
    • Turk, D.1    Guncar, G.2    Podobnik, M.3    Turk, B.4
  • 8
    • 82755161948 scopus 로고    scopus 로고
    • Cysteine cathepsins: from structure, function and regulation to new frontiers
    • Turk, V., Stoka, V., Vasiljeva, O., Renko, M. et al., Cysteine cathepsins: from structure, function and regulation to new frontiers. Biochim. Biophys. Acta 2012, 1824, 68-88.
    • (2012) Biochim. Biophys. Acta , vol.1824 , pp. 68-88
    • Turk, V.1    Stoka, V.2    Vasiljeva, O.3    Renko, M.4
  • 9
    • 69249227502 scopus 로고    scopus 로고
    • Lysosome biogenesis and lysosomal membrane proteins: trafficking meets function
    • Saftig, P., Klumperman, J., Lysosome biogenesis and lysosomal membrane proteins: trafficking meets function. Nat. Rev. Mol. Cell Biol. 2009, 10, 623-635.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 623-635
    • Saftig, P.1    Klumperman, J.2
  • 10
    • 1942470581 scopus 로고    scopus 로고
    • A cathepsin L isoform that is devoid of a signal peptide localizes to the nucleus in S phase and processes the CDP/Cux transcription factor
    • Goulet, B., Baruch, A., Moon, N. S., Poirier, M. et al., A cathepsin L isoform that is devoid of a signal peptide localizes to the nucleus in S phase and processes the CDP/Cux transcription factor. Mol. Cell 2004, 14, 207-219.
    • (2004) Mol. Cell , vol.14 , pp. 207-219
    • Goulet, B.1    Baruch, A.2    Moon, N.S.3    Poirier, M.4
  • 11
    • 53549094681 scopus 로고    scopus 로고
    • Cathepsin L proteolytically processes histone H3 during mouse embryonic stem cell differentiation
    • Duncan, E. M., Muratore-Schroeder, T. L., Cook, R. G., Garcia, B. A. et al., Cathepsin L proteolytically processes histone H3 during mouse embryonic stem cell differentiation. Cell 2008, 135, 284-294.
    • (2008) Cell , vol.135 , pp. 284-294
    • Duncan, E.M.1    Muratore-Schroeder, T.L.2    Cook, R.G.3    Garcia, B.A.4
  • 13
    • 84868119552 scopus 로고    scopus 로고
    • Structural basis for the recognition and cleavage of histone H3 by cathepsin L
    • Adams-Cioaba, M. A., Krupa, J. C., Xu, C., Mort, J. S., Min, J., Structural basis for the recognition and cleavage of histone H3 by cathepsin L. Nat. Commun. 2011, 2, 197.
    • (2011) Nat. Commun. , vol.2 , pp. 197
    • Adams-Cioaba, M.A.1    Krupa, J.C.2    Xu, C.3    Mort, J.S.4    Min, J.5
  • 14
    • 77951237963 scopus 로고    scopus 로고
    • Stefin B interacts with histones and cathepsin L in the nucleus
    • Ceru, S., Konjar, S., Maher, K., Repnik, U. et al., Stefin B interacts with histones and cathepsin L in the nucleus. J. Biol. Chem. 2010, 285, 10078-10086.
    • (2010) J. Biol. Chem. , vol.285 , pp. 10078-10086
    • Ceru, S.1    Konjar, S.2    Maher, K.3    Repnik, U.4
  • 15
    • 57349176440 scopus 로고    scopus 로고
    • Nuclear cathepsin F regulates activation markers in rat hepatic stellate cells
    • Maubach, G., Lim, M. C., Zhuo, L., Nuclear cathepsin F regulates activation markers in rat hepatic stellate cells. Mol. Biol. Cell 2008, 19, 4238-4248.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4238-4248
    • Maubach, G.1    Lim, M.C.2    Zhuo, L.3
  • 16
    • 77955957035 scopus 로고    scopus 로고
    • Nuclear cysteine cathepsin variants in thyroid carcinoma cells
    • Tedelind, S., Poliakova, K., Valeta, A., Hunegnaw, R. et al., Nuclear cysteine cathepsin variants in thyroid carcinoma cells. Biol. Chem. 2010, 391, 923-935.
    • (2010) Biol. Chem. , vol.391 , pp. 923-935
    • Tedelind, S.1    Poliakova, K.2    Valeta, A.3    Hunegnaw, R.4
  • 17
    • 33846643454 scopus 로고    scopus 로고
    • Cysteine cathepsins and the cutting edge of cancer invasion
    • Gocheva, V., Joyce, J. A., Cysteine cathepsins and the cutting edge of cancer invasion. Cell Cycle 2007, 6, 60-64.
    • (2007) Cell Cycle , vol.6 , pp. 60-64
    • Gocheva, V.1    Joyce, J.A.2
  • 18
    • 0028618307 scopus 로고
    • Pericellular pH affects distribution and secretion of cathepsin B in malignant cells
    • Rozhin, J., Sameni, M., Ziegler, G., Sloane, B. F., Pericellular pH affects distribution and secretion of cathepsin B in malignant cells. Cancer Res. 1994, 54, 6517-6525.
    • (1994) Cancer Res. , vol.54 , pp. 6517-6525
    • Rozhin, J.1    Sameni, M.2    Ziegler, G.3    Sloane, B.F.4
  • 19
    • 0347683401 scopus 로고    scopus 로고
    • Mutant K-ras regulates cathepsin B localization on the surface of human colorectal carcinoma cells
    • Cavallo-Medved, D., Dosescu, J., Linebaugh, B. E., Sameni, M. et al., Mutant K-ras regulates cathepsin B localization on the surface of human colorectal carcinoma cells. Neoplasia 2003, 5, 507-519.
    • (2003) Neoplasia , vol.5 , pp. 507-519
    • Cavallo-Medved, D.1    Dosescu, J.2    Linebaugh, B.E.3    Sameni, M.4
  • 20
    • 33144488633 scopus 로고    scopus 로고
    • Localization of cysteine protease, cathepsin S, to the surface of vascular smooth muscle cells by association with integrin alphanubeta3
    • Cheng, X. W., Kuzuya, M., Nakamura, K., Di, Q. et al., Localization of cysteine protease, cathepsin S, to the surface of vascular smooth muscle cells by association with integrin alphanubeta3. Am J. Pathol. 2006, 168, 685-694.
    • (2006) Am J. Pathol. , vol.168 , pp. 685-694
    • Cheng, X.W.1    Kuzuya, M.2    Nakamura, K.3    Di, Q.4
  • 21
    • 42149134396 scopus 로고    scopus 로고
    • Cysteine protease cathepsin X modulates immune response via activation of beta2 integrins
    • Obermajer, N., Repnik, U., Jevnikar, Z., Turk, B. et al., Cysteine protease cathepsin X modulates immune response via activation of beta2 integrins. Immunology 2008, 124, 76-88.
    • (2008) Immunology , vol.124 , pp. 76-88
    • Obermajer, N.1    Repnik, U.2    Jevnikar, Z.3    Turk, B.4
  • 22
    • 15844422855 scopus 로고    scopus 로고
    • Cathepsin K, but not cathepsins B, L, or S, is abundantly expressed in human osteoclasts
    • Drake, F. H., Dodds, R. A., James, I. E., Connor, J. R. et al., Cathepsin K, but not cathepsins B, L, or S, is abundantly expressed in human osteoclasts. J. Biol. Chem. 1996, 271, 12511-12516.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12511-12516
    • Drake, F.H.1    Dodds, R.A.2    James, I.E.3    Connor, J.R.4
  • 23
    • 0035127395 scopus 로고    scopus 로고
    • Biosynthesis and processing of cathepsin K in cultured human osteoclasts
    • Rieman, D. J., McClung, H. A., Dodds, R. A., Hwang, S. M. et al., Biosynthesis and processing of cathepsin K in cultured human osteoclasts. Bone 2001, 28, 282-289.
    • (2001) Bone , vol.28 , pp. 282-289
    • Rieman, D.J.1    McClung, H.A.2    Dodds, R.A.3    Hwang, S.M.4
  • 25
    • 19944429298 scopus 로고    scopus 로고
    • HaCaT keratinocytes secrete lysosomal cysteine proteinases during migration
    • Büth, H., Wolters, B., Hartwig, B., Meier-Bornheim, R. et al., HaCaT keratinocytes secrete lysosomal cysteine proteinases during migration. Eur. J. Cell Biol. 2004, 83, 781-795.
    • (2004) Eur. J. Cell Biol. , vol.83 , pp. 781-795
    • Büth, H.1    Wolters, B.2    Hartwig, B.3    Meier-Bornheim, R.4
  • 26
    • 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, 1623-1637.
    • (2002) Curr. Pharm. Des. , vol.8 , pp. 1623-1637
    • Turk, B.1    Turk, D.2    Salvesen, G.S.3
  • 27
    • 33846164404 scopus 로고    scopus 로고
    • Emerging roles of cysteine cathepsins in disease and their potential as drug targets
    • Vasiljeva, O., Reinheckel, T., Peters, C., Turk, D. et al., Emerging roles of cysteine cathepsins in disease and their potential as drug targets. Curr. Pharm. Des. 2007, 13, 387-403.
    • (2007) Curr. Pharm. Des. , vol.13 , pp. 387-403
    • Vasiljeva, O.1    Reinheckel, T.2    Peters, C.3    Turk, D.4
  • 28
    • 77957855881 scopus 로고    scopus 로고
    • Specialized roles for cysteine cathepsins in health and disease
    • Reiser, J., Adair, B., Reinheckel, T., Specialized roles for cysteine cathepsins in health and disease. J. Clin. Invest. 2010, 120, 3421-3431.
    • (2010) J. Clin. Invest. , vol.120 , pp. 3421-3431
    • Reiser, J.1    Adair, B.2    Reinheckel, T.3
  • 29
    • 0029310512 scopus 로고
    • Human cathepsin O2, a novel cysteine protease highly expressed in osteoclastomas and ovary molecular cloning, sequencing and tissue distribution
    • Brömme, D., Okamoto, K., Human cathepsin O2, a novel cysteine protease highly expressed in osteoclastomas and ovary molecular cloning, sequencing and tissue distribution. Biol. Chem. Hoppe. Seyler. 1995, 376, 379-384.
    • (1995) Biol. Chem. Hoppe. Seyler. , vol.376 , pp. 379-384
    • Brömme, D.1    Okamoto, K.2
  • 30
    • 0032080113 scopus 로고    scopus 로고
    • Human cathepsin K cleaves native type I and II collagens at the N-terminal end of the triple helix
    • Kafienah, W., Brömme, D., Buttle, D. J., Croucher, L. J., Hollander, A. P., Human cathepsin K cleaves native type I and II collagens at the N-terminal end of the triple helix. Biochem. J. 1998, 331, 727-732.
    • (1998) Biochem. J. , vol.331 , pp. 727-732
    • Kafienah, W.1    Brömme, D.2    Buttle, D.J.3    Croucher, L.J.4    Hollander, A.P.5
  • 31
    • 0030869303 scopus 로고    scopus 로고
    • Peptide aldehyde inhibitors of cathepsin K inhibit bone resorption both in vitro and in vivo
    • Votta, B. J., Levy, M. A., Badger, A., Bradbeer, J. et al., Peptide aldehyde inhibitors of cathepsin K inhibit bone resorption both in vitro and in vivo. J. Bone Miner. Res. 1997, 12, 1396-1406.
    • (1997) J. Bone Miner. Res. , vol.12 , pp. 1396-1406
    • Votta, B.J.1    Levy, M.A.2    Badger, A.3    Bradbeer, J.4
  • 32
    • 0030984531 scopus 로고    scopus 로고
    • Cathepsin K antisense oligodeoxynucleotide inhibits osteoclastic bone resorption
    • Inui, T., Ishibashi, O., Inaoka, T., Origane, Y. et al., Cathepsin K antisense oligodeoxynucleotide inhibits osteoclastic bone resorption. J. Biol. Chem. 1997, 272, 8109-8112.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8109-8112
    • Inui, T.1    Ishibashi, O.2    Inaoka, T.3    Origane, Y.4
  • 33
    • 0032506007 scopus 로고    scopus 로고
    • Impaired osteoclastic bone resorption leads to osteopetrosis in cathepsin-K-deficient mice
    • Saftig, P., Hunziker, E., Wehmeyer, O., Jones, S. et al., Impaired osteoclastic bone resorption leads to osteopetrosis in cathepsin-K-deficient mice. Proc. Natl. Acad. Sci. USA 1998, 95, 13453-13458.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 13453-13458
    • Saftig, P.1    Hunziker, E.2    Wehmeyer, O.3    Jones, S.4
  • 34
    • 0029809357 scopus 로고    scopus 로고
    • Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency
    • Gelb, B. D., Shi, G. P., Chapman, H. A., Desnick, R. J., Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency. Science 1996, 273, 1236-1238.
    • (1996) Science , vol.273 , pp. 1236-1238
    • Gelb, B.D.1    Shi, G.P.2    Chapman, H.A.3    Desnick, R.J.4
  • 35
    • 84887618813 scopus 로고    scopus 로고
    • Osteoporosis-a current view of pharmacological prevention and treatment
    • Das, S., Crockett, J. C., Osteoporosis-a current view of pharmacological prevention and treatment. Drug Des. Devel. Ther. 2013, 7, 435-448.
    • (2013) Drug Des. Devel. Ther. , vol.7 , pp. 435-448
    • Das, S.1    Crockett, J.C.2
  • 36
    • 0026507880 scopus 로고
    • Proteoglycans: many forms and many functions
    • Hardingham, T. E., Fosang, A. J., Proteoglycans: many forms and many functions. FASEB J. 1992, 6, 861-870.
    • (1992) FASEB J. , vol.6 , pp. 861-870
    • Hardingham, T.E.1    Fosang, A.J.2
  • 37
    • 1042267249 scopus 로고    scopus 로고
    • Osteoarthritis: is it a disease of cartilage or bone
    • Felson, D. T., Neogi, T., Osteoarthritis: is it a disease of cartilage or bone? Arthritis Rheum. 2004, 50, 341-344.
    • (2004) Arthritis Rheum. , vol.50 , pp. 341-344
    • Felson, D.T.1    Neogi, T.2
  • 38
    • 40349087284 scopus 로고    scopus 로고
    • Reappraising metalloproteinases in rheumatoid arthritis and osteoarthritis: destruction or repair
    • Murphy, G., Nagase, H., Reappraising metalloproteinases in rheumatoid arthritis and osteoarthritis: destruction or repair? Nat. Clin. Pract. Rheumatol. 2008, 4, 128-135.
    • (2008) Nat. Clin. Pract. Rheumatol. , vol.4 , pp. 128-135
    • Murphy, G.1    Nagase, H.2
  • 39
    • 0029091894 scopus 로고
    • Control of matrix synthesis in isolated bovine chondrocytes by extracellular and intracellular pH
    • Wilkins, R. J., Hall, A. C., Control of matrix synthesis in isolated bovine chondrocytes by extracellular and intracellular pH. J. Cell Physiol. 1995, 164, 474-481.
    • (1995) J. Cell Physiol. , vol.164 , pp. 474-481
    • Wilkins, R.J.1    Hall, A.C.2
  • 40
    • 0036226928 scopus 로고    scopus 로고
    • Acidic cysteine endoproteinase cathepsin K in the degeneration of the superficial articular hyaline cartilage in osteoarthritis
    • Konttinen, Y. T., Mandelin, J., Li, T. F., Salo, J. et al., Acidic cysteine endoproteinase cathepsin K in the degeneration of the superficial articular hyaline cartilage in osteoarthritis. Arthritis Rheum. 2002, 46, 953-960.
    • (2002) Arthritis Rheum. , vol.46 , pp. 953-960
    • Konttinen, Y.T.1    Mandelin, J.2    Li, T.F.3    Salo, J.4
  • 41
    • 3442875303 scopus 로고    scopus 로고
    • Pathogenesis of bone and cartilage destruction in rheumatoid arthritis
    • ii11-iii6
    • Goldring, S. R., Pathogenesis of bone and cartilage destruction in rheumatoid arthritis. Rheumatology 2003, 42(Suppl 2), ii11-ii6.
    • (2003) Rheumatology , vol.42 , Issue.SUPPL. 2
    • Goldring, S.R.1
  • 42
    • 0023886162 scopus 로고
    • Human cathepsin B and cysteine-proteinase inhibitors (CPIs) in inflamatory and metabolic join diseases
    • Lenarčič, B., Gabrijelčič, D., Rozman, B., Drobnič-Košorok, M., Turk, V., Human cathepsin B and cysteine-proteinase inhibitors (CPIs) in inflamatory and metabolic join diseases. Biol. Chem. Hoppe Seyler 1988, 369, 257-261.
    • (1988) Biol. Chem. Hoppe Seyler , vol.369 , pp. 257-261
    • Lenarčič, B.1    Gabrijelčič, D.2    Rozman, B.3    Drobnič-Košorok, M.4    Turk, V.5
  • 43
    • 0025220324 scopus 로고
    • Determination of cathepsins B and H in sera and synovial fluids of patients with different joint diseases
    • Gabrijelcic, D., Annan-Prah, A., Rodic, B., Rozman, B. et al., Determination of cathepsins B and H in sera and synovial fluids of patients with different joint diseases. J. Clin. Chem. Clin. Biochem. 1990, 28, 149-153.
    • (1990) J. Clin. Chem. Clin. Biochem. , vol.28 , pp. 149-153
    • Gabrijelcic, D.1    Annan-Prah, A.2    Rodic, B.3    Rozman, B.4
  • 44
    • 0030837038 scopus 로고    scopus 로고
    • Selective induction of the secretion of cathepsins B and L by cytokines in synovial fibroblast-like cells
    • Lemaire, R., Huet, G., Zerimech, F., Grard, G. et al., Selective induction of the secretion of cathepsins B and L by cytokines in synovial fibroblast-like cells. Br. J. Rheumatol. 1997, 36, 735-743.
    • (1997) Br. J. Rheumatol. , vol.36 , pp. 735-743
    • Lemaire, R.1    Huet, G.2    Zerimech, F.3    Grard, G.4
  • 45
    • 0034096934 scopus 로고    scopus 로고
    • Cathepsin B and its endogenous inhibitor cystetin C in rheumatoid arthritis synovium
    • Hansen, T., Petrow, P. K., Gaumann, A., Keyzser, G. M. et al., Cathepsin B and its endogenous inhibitor cystetin C in rheumatoid arthritis synovium. J. Rheumatol. 2000, 27, 859-865.
    • (2000) J. Rheumatol. , vol.27 , pp. 859-865
    • Hansen, T.1    Petrow, P.K.2    Gaumann, A.3    Keyzser, G.M.4
  • 46
    • 77952798828 scopus 로고    scopus 로고
    • Expression and activity profiling of selected cysteine proteases and matrix metalloproteinases in synovial fluids from patients with rheumatoid arthritis and osteoarthritis
    • Požgan, U., Caglič, D., Rozman, B., Nagase, H. et al., Expression and activity profiling of selected cysteine proteases and matrix metalloproteinases in synovial fluids from patients with rheumatoid arthritis and osteoarthritis. Biol. Chem. 2010, 391, 571-579.
    • (2010) Biol. Chem. , vol.391 , pp. 571-579
    • Požgan, U.1    Caglič, D.2    Rozman, B.3    Nagase, H.4
  • 47
    • 0028901908 scopus 로고
    • Cathepsin B in osteoarthritis: cytochemical and histochemical analysis of human femoral head cartilage
    • Baici, A., Lang, A., Horler, D., Kissling, R., Merlin, C., Cathepsin B in osteoarthritis: cytochemical and histochemical analysis of human femoral head cartilage. Ann. Rheum. Dis. 1995, 54, 289-297.
    • (1995) Ann. Rheum. Dis. , vol.54 , pp. 289-297
    • Baici, A.1    Lang, A.2    Horler, D.3    Kissling, R.4    Merlin, C.5
  • 48
    • 0028907722 scopus 로고
    • Cathepsin B in osteoarthritis: zonal variation of enzyme activity in human femoral head cartilage
    • Baici, A., Horler, D., Lang, A., Merlin, C., Kissling, R., Cathepsin B in osteoarthritis: zonal variation of enzyme activity in human femoral head cartilage. Ann. Rheum. Dis. 1995, 54, 281-288.
    • (1995) Ann. Rheum. Dis. , vol.54 , pp. 281-288
    • Baici, A.1    Horler, D.2    Lang, A.3    Merlin, C.4    Kissling, R.5
  • 49
    • 1342304427 scopus 로고    scopus 로고
    • Early diagnosis of osteoarthritis using cathepsin B sensitive near-infrared fluorescent probes
    • Lai, W. F., Chang, C. H., Tang, Y., Bronson, R., Tung, C. H., Early diagnosis of osteoarthritis using cathepsin B sensitive near-infrared fluorescent probes. Osteoarthr. Cartil. 2004, 12, 239-244.
    • (2004) Osteoarthr. Cartil. , vol.12 , pp. 239-244
    • Lai, W.F.1    Chang, C.H.2    Tang, Y.3    Bronson, R.4    Tung, C.H.5
  • 50
    • 0036185401 scopus 로고    scopus 로고
    • Comparison of cathepsins K and S expression within the rheumatoid and osteoarthritic synovium
    • Hou, W. S., Li, W., Keyszer, G., Comparison of cathepsins K and S expression within the rheumatoid and osteoarthritic synovium. Arthritis Rheum. 2002, 46, 663-674.
    • (2002) Arthritis Rheum. , vol.46 , pp. 663-674
    • Hou, W.S.1    Li, W.2    Keyszer, G.3
  • 51
    • 0035185895 scopus 로고    scopus 로고
    • Cathepsin K is a critical protease in synovial fibroblast mediated collagen degradation
    • Hou, W. S., Li, Z., Gordon, R. E., Chan, K. et al., Cathepsin K is a critical protease in synovial fibroblast mediated collagen degradation. Am J Pathol 2001, 159, 2167-2177.
    • (2001) Am J Pathol , vol.159 , pp. 2167-2177
    • Hou, W.S.1    Li, Z.2    Gordon, R.E.3    Chan, K.4
  • 52
    • 0038486755 scopus 로고    scopus 로고
    • Cleavage site specificity of cathepsin K toward cartilage proteoglycans and protease complex formation
    • Hou, W. S., Li, Z., Buttner, F. H., Bartnik, E., Bromme, D., Cleavage site specificity of cathepsin K toward cartilage proteoglycans and protease complex formation. Biol. Chem. 2003, 384, 891-897.
    • (2003) Biol. Chem. , vol.384 , pp. 891-897
    • Hou, W.S.1    Li, Z.2    Buttner, F.H.3    Bartnik, E.4    Bromme, D.5
  • 53
    • 84859061110 scopus 로고    scopus 로고
    • Role for cysteine protease cathepsins in heart disease: focus on biology and mechanisms with clinical implication
    • Cheng, X. W., Shi, G. P., Kuzuya, M., Sasaki, T. et al., Role for cysteine protease cathepsins in heart disease: focus on biology and mechanisms with clinical implication. Circulation 2012, 125, 1551-1562.
    • (2012) Circulation , vol.125 , pp. 1551-1562
    • Cheng, X.W.1    Shi, G.P.2    Kuzuya, M.3    Sasaki, T.4
  • 54
    • 33750246799 scopus 로고    scopus 로고
    • Elastolytic cathepsin induction/activation system exists in myocardium and is upregulated in hypertension heart failure
    • Cheng, X. W., Obata, K., Kuzuya, M., Izawa, H. et al., Elastolytic cathepsin induction/activation system exists in myocardium and is upregulated in hypertension heart failure. Hypertension 2006, 48, 979-987.
    • (2006) Hypertension , vol.48 , pp. 979-987
    • Cheng, X.W.1    Obata, K.2    Kuzuya, M.3    Izawa, H.4
  • 55
    • 18344376711 scopus 로고    scopus 로고
    • Dilated cardiomyopathy in mice deficient for the lysosomal cysteine peptidase cathepsin L
    • Stypmann, J., Glaser, K., Roth, W., Tobin, D. J. et al., Dilated cardiomyopathy in mice deficient for the lysosomal cysteine peptidase cathepsin L. Proc. Natl. Acad. Sci. USA 2002, 99, 6234-6239.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 6234-6239
    • Stypmann, J.1    Glaser, K.2    Roth, W.3    Tobin, D.J.4
  • 56
    • 33845652579 scopus 로고    scopus 로고
    • Lysosomal, cytosceletal and metabolic alterations in cardiomyopathy of cathepsin L knockout mice
    • Petermann, I., Mayer, C., Stypmann, J., Biniossek, M. L. et al., Lysosomal, cytosceletal and metabolic alterations in cardiomyopathy of cathepsin L knockout mice. FASEB J. 2006, 20, 1266-1268.
    • (2006) FASEB J. , vol.20 , pp. 1266-1268
    • Petermann, I.1    Mayer, C.2    Stypmann, J.3    Biniossek, M.L.4
  • 57
    • 60549104999 scopus 로고    scopus 로고
    • Lysosomal cysteine peptidase cathepsin L protects against cardiac hyperthrophy through blocking AKT/GSK3beta signaling
    • Tang, Q., Cai, J., Shen, D., Bian, Z. et al., Lysosomal cysteine peptidase cathepsin L protects against cardiac hyperthrophy through blocking AKT/GSK3beta signaling. J. Mol. Med. 2006, 87, 249-260.
    • (2006) J. Mol. Med. , vol.87 , pp. 249-260
    • Tang, Q.1    Cai, J.2    Shen, D.3    Bian, Z.4
  • 58
    • 20044373820 scopus 로고    scopus 로고
    • Cathepsin L is required for endothelial progenitor cell induced neovascularisation
    • Urbich, C., Heeschen, C., Aicher, A., Sasaki, K. et al., Cathepsin L is required for endothelial progenitor cell induced neovascularisation. Nat. Med. 2005, 11, 206-213.
    • (2005) Nat. Med. , vol.11 , pp. 206-213
    • Urbich, C.1    Heeschen, C.2    Aicher, A.3    Sasaki, K.4
  • 59
    • 78751469546 scopus 로고    scopus 로고
    • Cathepsin L contributes to cardiac repair and remodeling post-infarction
    • Sun, M, Chen, M., Liu, Y., Fukuoka, M. et al., Cathepsin L contributes to cardiac repair and remodeling post-infarction. Cardiovasc. Res. 2010, 89, 374-383.
    • (2010) Cardiovasc. Res. , vol.89 , pp. 374-383
    • Sun, M.1    Chen, M.2    Liu, Y.3    Fukuoka, M.4
  • 60
    • 78751469546 scopus 로고    scopus 로고
    • Cathepsin-L contributes to cardiac repair and remodelling post-infarction
    • Sun, M., Chen, M., Liu, Y., Fukuoka, M. et al., Cathepsin-L contributes to cardiac repair and remodelling post-infarction. Cardiovasc. Res. 2011, 89, 374-383.
    • (2011) Cardiovasc. Res. , vol.89 , pp. 374-383
    • Sun, M.1    Chen, M.2    Liu, Y.3    Fukuoka, M.4
  • 61
    • 33746834187 scopus 로고    scopus 로고
    • Increased expression of elastolytic cathepsins S, K and V and their inhibitor cystatin C in stenotic aortic valves
    • Helske, S., Syvaranta, S., Lindstedt, K. A., Lappalainen, J. et al., Increased expression of elastolytic cathepsins S, K and V and their inhibitor cystatin C in stenotic aortic valves. Arterioscler. Thromb. Vasc. Biol. 2006, 26, 1791-1798.
    • (2006) Arterioscler. Thromb. Vasc. Biol. , vol.26 , pp. 1791-1798
    • Helske, S.1    Syvaranta, S.2    Lindstedt, K.A.3    Lappalainen, J.4
  • 62
    • 64049108554 scopus 로고    scopus 로고
    • Elevated cyclic stretch alters matrix remodeling in aortic valve cusps: implications for degenerative aortic valve disease
    • Balachandran, K., Sucosky, P., Jo, H., Yoganathan, A. P., Elevated cyclic stretch alters matrix remodeling in aortic valve cusps: implications for degenerative aortic valve disease. Am. J. Physiol. Heart Circ. Physiol. 2009, 296, H756-H764.
    • (2009) Am. J. Physiol. Heart Circ. Physiol. , vol.296
    • Balachandran, K.1    Sucosky, P.2    Jo, H.3    Yoganathan, A.P.4
  • 63
    • 77954568359 scopus 로고    scopus 로고
    • Elevated cyclic stretch induces aortic valve calcification in a bone morphogenic protein dependant manner
    • Balachandran, K., Sucosky, P., Jo, H., Yoganathan, A. P., Elevated cyclic stretch induces aortic valve calcification in a bone morphogenic protein dependant manner. Am. J. Pathol. 2010, 177, 49-57.
    • (2010) Am. J. Pathol. , vol.177 , pp. 49-57
    • Balachandran, K.1    Sucosky, P.2    Jo, H.3    Yoganathan, A.P.4
  • 64
    • 65349154635 scopus 로고    scopus 로고
    • Arterial and aortic valve calcification abolished by elastolytic cathepsin S deficiency in chronic renal disease
    • Aikawa, E., Aikawa, M., Libby, P., Figueiredo, J. L. et al., Arterial and aortic valve calcification abolished by elastolytic cathepsin S deficiency in chronic renal disease. Circulation 2009, 119, 1785-1794.
    • (2009) Circulation , vol.119 , pp. 1785-1794
    • Aikawa, E.1    Aikawa, M.2    Libby, P.3    Figueiredo, J.L.4
  • 65
    • 0032145836 scopus 로고    scopus 로고
    • Expression of elastinolytic cathepsins S and K in human atheroma and regulation of their production in smooth muscle cells
    • Sukhova, G. K., Shi, G. P., Simon, D. I., Chapman, H. A., Libby, P., Expression of elastinolytic cathepsins S and K in human atheroma and regulation of their production in smooth muscle cells. J. Clin. Invest. 1998, 102, 576-583.
    • (1998) J. Clin. Invest. , vol.102 , pp. 576-583
    • Sukhova, G.K.1    Shi, G.P.2    Simon, D.I.3    Chapman, H.A.4    Libby, P.5
  • 66
    • 0036735233 scopus 로고    scopus 로고
    • Differential expression of cysteine and aspartic proteases during progression of atherosclerosis in apolipoprotein E-defficient mice
    • Jormsjo, S., Wuttge, D. M., Sirsjo, A., Whatling, C. et al., Differential expression of cysteine and aspartic proteases during progression of atherosclerosis in apolipoprotein E-defficient mice. Am. J. Pathol. 2002, 161, 939-946.
    • (2002) Am. J. Pathol. , vol.161 , pp. 939-946
    • Jormsjo, S.1    Wuttge, D.M.2    Sirsjo, A.3    Whatling, C.4
  • 67
    • 0029007093 scopus 로고
    • Pericellular mobilization of the tissue-destructive cysteine proteinases, cathepsins B, L, and S, by human monocyte-derived macrophages
    • Reddy, V. Y., Zhang, Q. Y., Weiss, S. J., Pericellular mobilization of the tissue-destructive cysteine proteinases, cathepsins B, L, and S, by human monocyte-derived macrophages. Proc. Natl. Acad Sci. USA 1995, 92, 3849-3853.
    • (1995) Proc. Natl. Acad Sci. USA , vol.92 , pp. 3849-3853
    • Reddy, V.Y.1    Zhang, Q.Y.2    Weiss, S.J.3
  • 69
    • 33644865170 scopus 로고    scopus 로고
    • Disruption of the cathepsin K gene reduces atherosclerosis progression and induces plaque fibrosis but accelerates macrophage foam cell formation
    • Lutgens, E., Lutgens, S. P., Faber, B. C., Heeneman, S. et al., Disruption of the cathepsin K gene reduces atherosclerosis progression and induces plaque fibrosis but accelerates macrophage foam cell formation. Circulation 2006, 113, 98-107.
    • (2006) Circulation , vol.113 , pp. 98-107
    • Lutgens, E.1    Lutgens, S.P.2    Faber, B.C.3    Heeneman, S.4
  • 70
    • 33646449061 scopus 로고    scopus 로고
    • Inflammation and cellular immune responses in abdominal aortic aneurysms
    • Shimizu, K., Mitchell, R. N., Libby, P., Inflammation and cellular immune responses in abdominal aortic aneurysms. Arterioscler. Thromb. Vasc. Biol. 2006, 26, 987-994.
    • (2006) Arterioscler. Thromb. Vasc. Biol. , vol.26 , pp. 987-994
    • Shimizu, K.1    Mitchell, R.N.2    Libby, P.3
  • 71
    • 0032718590 scopus 로고    scopus 로고
    • Cystatin C deficiency in human atherosclerosis and aortic aneurysms
    • Shi, G. P., Sukhova, G. K., Grubb, A., Ducharme, A. et al., Cystatin C deficiency in human atherosclerosis and aortic aneurysms. J. Clin. Invest. 1999, 104, 1191-1197.
    • (1999) J. Clin. Invest. , vol.104 , pp. 1191-1197
    • Shi, G.P.1    Sukhova, G.K.2    Grubb, A.3    Ducharme, A.4
  • 72
    • 30044445997 scopus 로고    scopus 로고
    • Cathepsin L expression and regulation in human abdominal aortic aneurysm, atherosclerosis, and vascular cells
    • Liu, J., Sukhova, G. K., Yang, J. T., Sun, J. et al., Cathepsin L expression and regulation in human abdominal aortic aneurysm, atherosclerosis, and vascular cells. Atherosclerosis 2006, 184, 302-311.
    • (2006) Atherosclerosis , vol.184 , pp. 302-311
    • Liu, J.1    Sukhova, G.K.2    Yang, J.T.3    Sun, J.4
  • 73
    • 52449101897 scopus 로고    scopus 로고
    • Cathepsin B, K, and S are expressed in cerebral aneurysms and promote the progression of cerebral aneurysms
    • Aoki, T., Kataoka, H., Ishibashi, R., Nozaki, K., Hashimoto, N., Cathepsin B, K, and S are expressed in cerebral aneurysms and promote the progression of cerebral aneurysms. Stroke 2008, 39, 2603-2610.
    • (2008) Stroke , vol.39 , pp. 2603-2610
    • Aoki, T.1    Kataoka, H.2    Ishibashi, R.3    Nozaki, K.4    Hashimoto, N.5
  • 74
    • 48749085788 scopus 로고    scopus 로고
    • Superoxide-dependent cathepsin activation is associated with hypertensive myocardial remodeling and represents a target for angiotensin II type 1 receptor blocker treatment
    • Cheng, X. W., Murohara, T., Kuzuya, M., Izawa, H. et al., Superoxide-dependent cathepsin activation is associated with hypertensive myocardial remodeling and represents a target for angiotensin II type 1 receptor blocker treatment. Am. J. Pathol. 2008, 173, 358-369.
    • (2008) Am. J. Pathol. , vol.173 , pp. 358-369
    • Cheng, X.W.1    Murohara, T.2    Kuzuya, M.3    Izawa, H.4
  • 76
    • 34547624086 scopus 로고    scopus 로고
    • Angiotensin inhibition decreases progression of advanced atherosclerosis and stabilizes established atherosclerotic plaques
    • Suganuma, E., Babaev, V. R., Motojima, M., Zuo, Y. et al., Angiotensin inhibition decreases progression of advanced atherosclerosis and stabilizes established atherosclerotic plaques. J. Am. Soc. Nephrol. 2007, 18, 2311-2319.
    • (2007) J. Am. Soc. Nephrol. , vol.18 , pp. 2311-2319
    • Suganuma, E.1    Babaev, V.R.2    Motojima, M.3    Zuo, Y.4
  • 77
    • 0019797924 scopus 로고
    • Lysosomal cathepsin B: correlation with metastatic potential
    • Sloane, B. F., Dunn, J. R., Honn, K. V., Lysosomal cathepsin B: correlation with metastatic potential. Science 1981, 212, 1151-1153.
    • (1981) Science , vol.212 , pp. 1151-1153
    • Sloane, B.F.1    Dunn, J.R.2    Honn, K.V.3
  • 78
    • 1542604677 scopus 로고    scopus 로고
    • Cysteine proteases as disease markers
    • Berdowska, I., Cysteine proteases as disease markers. Clin. Chim. Acta 2004, 342, 41-69.
    • (2004) Clin. Chim. Acta , vol.342 , pp. 41-69
    • Berdowska, I.1
  • 79
    • 33749017931 scopus 로고    scopus 로고
    • Cysteine cathepsins: multifunctional enzymes in cancer
    • Mohamed, M. M., Sloane, B. F., Cysteine cathepsins: multifunctional enzymes in cancer. Nat. Rev. Cancer 2006, 6, 764-775.
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 764-775
    • Mohamed, M.M.1    Sloane, B.F.2
  • 80
    • 2342603891 scopus 로고    scopus 로고
    • Cathepsin cysteine proteases are effectors of invasive growth and angiogenesis during multistage tumorigenesis
    • Joyce, J. A., Baruch, A., Chehade, K., Meyer-Morse, N. et al., Cathepsin cysteine proteases are effectors of invasive growth and angiogenesis during multistage tumorigenesis. Cancer Cell 2004, 5, 443-453.
    • (2004) Cancer Cell , vol.5 , pp. 443-453
    • Joyce, J.A.1    Baruch, A.2    Chehade, K.3    Meyer-Morse, N.4
  • 81
    • 80052587306 scopus 로고    scopus 로고
    • Ferri-liposomes as an MRI-visible drug-delivery system for targeting tumours and their microenvironment
    • Mikhaylov, G., Mikac, U., Magaeva, A. A., Itin, V. I. et al., Ferri-liposomes as an MRI-visible drug-delivery system for targeting tumours and their microenvironment. Nat. Nanotechnol. 2011, 6, 594-602.
    • (2011) Nat. Nanotechnol. , vol.6 , pp. 594-602
    • Mikhaylov, G.1    Mikac, U.2    Magaeva, A.A.3    Itin, V.I.4
  • 82
    • 33744917827 scopus 로고    scopus 로고
    • Tumor cell-derived and macrophage-derived cathepsin B promotes progression and lung metastasis of mammary cancer
    • Vasiljeva, O., Papazoglou, A., Krüger, A., Brodoefel, H. et al., Tumor cell-derived and macrophage-derived cathepsin B promotes progression and lung metastasis of mammary cancer. Cancer Res. 2006, 66, 5242-5250.
    • (2006) Cancer Res. , vol.66 , pp. 5242-5250
    • Vasiljeva, O.1    Papazoglou, A.2    Krüger, A.3    Brodoefel, H.4
  • 83
    • 47049095033 scopus 로고    scopus 로고
    • Reduced tumour cell proliferation and delayed development of high-grade mammary carcinomas in cathepsin B-deficient mice
    • Vasiljeva, O., Korovin, M., Gajda, M., Brodoefel, H. et al., Reduced tumour cell proliferation and delayed development of high-grade mammary carcinomas in cathepsin B-deficient mice. Oncogene 2008, 27, 4191-4199.
    • (2008) Oncogene , vol.27 , pp. 4191-4199
    • Vasiljeva, O.1    Korovin, M.2    Gajda, M.3    Brodoefel, H.4
  • 84
    • 33644784910 scopus 로고    scopus 로고
    • Distinct roles for cysteine cathepsin genes in multistage tumorigenesis
    • Gocheva, V., Zeng, W., Ke, D., Klimstra, D. et al., Distinct roles for cysteine cathepsin genes in multistage tumorigenesis. Genes Dev. 2006, 20, 543-556.
    • (2006) Genes Dev. , vol.20 , pp. 543-556
    • Gocheva, V.1    Zeng, W.2    Ke, D.3    Klimstra, D.4
  • 85
    • 77249161680 scopus 로고    scopus 로고
    • Synergistic antitumor effects of combined cathepsin B and cathepsin Z deficiencies on breast cancer progression and metastasis in mice
    • Sevenich, L., Schurigt, U., Sachse, K., Gajda, M. et al., Synergistic antitumor effects of combined cathepsin B and cathepsin Z deficiencies on breast cancer progression and metastasis in mice. Proc. Natl. Acad. Sci. USA 2010, 107, 2497-2502.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 2497-2502
    • Sevenich, L.1    Schurigt, U.2    Sachse, K.3    Gajda, M.4
  • 86
    • 38649084746 scopus 로고    scopus 로고
    • Dual contrasting roles of cysteine cathepsins in cancer progression: apoptosis versus tumour invasion
    • Vasiljeva, O., Turk, B., Dual contrasting roles of cysteine cathepsins in cancer progression: apoptosis versus tumour invasion. Biochimie 2008, 90, 380-386.
    • (2008) Biochimie , vol.90 , pp. 380-386
    • Vasiljeva, O.1    Turk, B.2
  • 87
    • 0033986761 scopus 로고    scopus 로고
    • Causes and consequences of tumour acidity and implications for treatment
    • Stubbs, M., McSheehy, P. M., Griffiths, J. R., Bashford, C. L., Causes and consequences of tumour acidity and implications for treatment. Mol. Med. Today 2000, 6, 15-9.
    • (2000) Mol. Med. Today , vol.6 , pp. 15-19
    • Stubbs, M.1    McSheehy, P.M.2    Griffiths, J.R.3    Bashford, C.L.4
  • 88
    • 79953163995 scopus 로고    scopus 로고
    • Proteolytic networks in cancer
    • Mason, S. D., Joyce, J. A., Proteolytic networks in cancer. Trends Cell Biol. 2011, 21, 228-237.
    • (2011) Trends Cell Biol. , vol.21 , pp. 228-237
    • Mason, S.D.1    Joyce, J.A.2
  • 89
  • 90
    • 1642535587 scopus 로고    scopus 로고
    • Inhibition of tumorigenicity and metastasis of human melanoma cells by anti-cathepsin L single chain variable fragment
    • Rousselet, N., Mills, L., Jean, D., Tellez, C. et al., Inhibition of tumorigenicity and metastasis of human melanoma cells by anti-cathepsin L single chain variable fragment. Cancer Res. 2004, 64, 146-151.
    • (2004) Cancer Res. , vol.64 , pp. 146-151
    • Rousselet, N.1    Mills, L.2    Jean, D.3    Tellez, C.4
  • 91
    • 0037192819 scopus 로고    scopus 로고
    • Analysis of a truncated form of cathepsin H in human prostate tumor cells
    • Waghray, A., Keppler, D., Sloane, B. F., Schuger, L., Chen, Y. Q., Analysis of a truncated form of cathepsin H in human prostate tumor cells. J. Biol. Chem. 2002, 277, 11533-11538.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11533-11538
    • Waghray, A.1    Keppler, D.2    Sloane, B.F.3    Schuger, L.4    Chen, Y.Q.5
  • 92
    • 0037969805 scopus 로고    scopus 로고
    • The clinical significance of cathepsin S expression in human astrocytomas
    • Flannery, T., Gibson, D., Mirakhur, M., McQuaid, S. et al., The clinical significance of cathepsin S expression in human astrocytomas. Am. J. Pathol. 2003, 163, 175-182.
    • (2003) Am. J. Pathol. , vol.163 , pp. 175-182
    • Flannery, T.1    Gibson, D.2    Mirakhur, M.3    McQuaid, S.4
  • 94
    • 0041737535 scopus 로고    scopus 로고
    • Molecular mechanisms of glioma invasiveness: the role of proteases
    • Rao, J. S., Molecular mechanisms of glioma invasiveness: the role of proteases. Nat. Rev. Cancer 2003, 3, 489-501.
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 489-501
    • Rao, J.S.1
  • 95
    • 0027329828 scopus 로고
    • In vitro" study of basement membrane degradation by the cysteine proteinases, cathepsins B, B-like and L. Digestion of collagen IV, laminin, fibronectin, and release of gelatinase activities from basement membrane fibronectin
    • Guinec, N., Dalet-Fumeron, V., Pagano, M., "In vitro" study of basement membrane degradation by the cysteine proteinases, cathepsins B, B-like and L. Digestion of collagen IV, laminin, fibronectin, and release of gelatinase activities from basement membrane fibronectin. Biol. Chem. Hoppe Seyler 1993, 374, 1135-1146.
    • (1993) Biol. Chem. Hoppe Seyler , vol.374 , pp. 1135-1146
    • Guinec, N.1    Dalet-Fumeron, V.2    Pagano, M.3
  • 96
    • 0036754586 scopus 로고    scopus 로고
    • Degradation of extracellular matrix protein tenascin-C by cathepsin B: an interaction involved in the progression of gliomas
    • Mai, J., Sameni, M., Mikkelsen, T., Sloane, B. F., Degradation of extracellular matrix protein tenascin-C by cathepsin B: an interaction involved in the progression of gliomas. Biol. Chem. 2002, 383, 1407-1413.
    • (2002) Biol. Chem. , vol.383 , pp. 1407-1413
    • Mai, J.1    Sameni, M.2    Mikkelsen, T.3    Sloane, B.F.4
  • 97
    • 84873858791 scopus 로고    scopus 로고
    • Cathepsin H mediates the processing of talin and regulates migration of prostate cancer cells
    • Jevnikar, Z., Rojnik, M., Jamnik, P., Doljak, B. et al., Cathepsin H mediates the processing of talin and regulates migration of prostate cancer cells. J. Biol. Chem. 2013, 288, 2201-2209.
    • (2013) J. Biol. Chem. , vol.288 , pp. 2201-2209
    • Jevnikar, Z.1    Rojnik, M.2    Jamnik, P.3    Doljak, B.4
  • 98
    • 84872233476 scopus 로고    scopus 로고
    • Profilin 1 as a target for cathepsin X activity in tumor cells
    • Pečar Fonović, U., Jevnikar, Z., Rojnik, M., Doljak, B. et al., Profilin 1 as a target for cathepsin X activity in tumor cells. PLoS One 2013, 8, e53918.
    • (2013) PLoS One , vol.8
    • Pečar Fonović, U.1    Jevnikar, Z.2    Rojnik, M.3    Doljak, B.4
  • 99
    • 0035793580 scopus 로고    scopus 로고
    • Lysosomal protease pathways to apoptosis. Cleavage of bid, not pro-caspases, is the most likely route
    • Stoka, V., Turk, B., Schendel, S. L., Kim, T. H. et al., Lysosomal protease pathways to apoptosis. Cleavage of bid, not pro-caspases, is the most likely route. J. Biol. Chem. 2001, 276, 3149-3157.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3149-3157
    • Stoka, V.1    Turk, B.2    Schendel, S.L.3    Kim, T.H.4
  • 100
    • 82955189189 scopus 로고    scopus 로고
    • Macrophages and cathepsin proteases blunt chemotherapeutic response in breast cancer
    • Shree, T., Olson, O. C., Elie, B. T., Kester, J. C. et al., Macrophages and cathepsin proteases blunt chemotherapeutic response in breast cancer. Genes Dev. 2011, 25, 2465-2479.
    • (2011) Genes Dev. , vol.25 , pp. 2465-2479
    • Shree, T.1    Olson, O.C.2    Elie, B.T.3    Kester, J.C.4
  • 101
    • 37549070672 scopus 로고    scopus 로고
    • Cysteine cathepsin proteases as pharmacological targets in cancer
    • Palermo, C., Joyce, J. A., Cysteine cathepsin proteases as pharmacological targets in cancer. Trends. Pharmacol. Sci. 2008, 29, 22-28.
    • (2008) Trends. Pharmacol. Sci. , vol.29 , pp. 22-28
    • Palermo, C.1    Joyce, J.A.2
  • 102
    • 0003083706 scopus 로고    scopus 로고
    • The expression of lysosomal proteinases and their inhibitors in breast cancer: possible relationship to prognosis of the disease
    • Lah, T. T., Kos, J., Blejec, A., Frkovic-Georgio, S. et al., The expression of lysosomal proteinases and their inhibitors in breast cancer: possible relationship to prognosis of the disease. Pathol. Oncol. Res. 1997, 3, 89-99.
    • (1997) Pathol. Oncol. Res. , vol.3 , pp. 89-99
    • Lah, T.T.1    Kos, J.2    Blejec, A.3    Frkovic-Georgio, S.4
  • 103
    • 0031887693 scopus 로고    scopus 로고
    • Prognostic significance of cathepsins B and L in primary human breast cancer
    • Foekens, J. A., Kos, J., Peters, H. A., Krasovec, M. et al., Prognostic significance of cathepsins B and L in primary human breast cancer. J. Clin. Oncol. 1998, 16, 1013-1021.
    • (1998) J. Clin. Oncol. , vol.16 , pp. 1013-1021
    • Foekens, J.A.1    Kos, J.2    Peters, H.A.3    Krasovec, M.4
  • 104
    • 78650727555 scopus 로고    scopus 로고
    • Cathepsin B: a potential prognostic marker for inflammatory breast cancer
    • Nouh, M. A., Mohamed, M. M., El-Shinawi, M., Shaalan, M. A. et al., Cathepsin B: a potential prognostic marker for inflammatory breast cancer. J. Transl. Med. 2011, 9, 1.
    • (2011) J. Transl. Med. , vol.9 , pp. 1
    • Nouh, M.A.1    Mohamed, M.M.2    El-Shinawi, M.3    Shaalan, M.A.4
  • 105
    • 0034128337 scopus 로고    scopus 로고
    • Cysteine proteinases and their inhibitors in extracellular fluids: markers for diagnosis and prognosis in cancer
    • Kos, J., Werle, B., Lah, T., Brunner, N., Cysteine proteinases and their inhibitors in extracellular fluids: markers for diagnosis and prognosis in cancer. Int. J. Biol. Markers 2000, 15, 84-89.
    • (2000) Int. J. Biol. Markers , vol.15 , pp. 84-89
    • Kos, J.1    Werle, B.2    Lah, T.3    Brunner, N.4
  • 106
    • 80054723111 scopus 로고    scopus 로고
    • Clinical value of combined detection of serum matrix metalloproteinase-9, heparanase, and cathepsin for determining ovarian cancer invasion and metastasis
    • Zhang, W., Yang, H. C., Wang, Q., Yang, Z. J. et al., Clinical value of combined detection of serum matrix metalloproteinase-9, heparanase, and cathepsin for determining ovarian cancer invasion and metastasis. Anticancer Res. 2011, 31, 3423-3428.
    • (2011) Anticancer Res. , vol.31 , pp. 3423-3428
    • Zhang, W.1    Yang, H.C.2    Wang, Q.3    Yang, Z.J.4
  • 107
    • 0035914268 scopus 로고    scopus 로고
    • Cathepsin S in tumours, regional lymph nodes and sera of patients with lung cancer: relation to prognosis
    • Kos, J., Sekirnik, A., Kopitar, G., Cimerman, N. et al., Cathepsin S in tumours, regional lymph nodes and sera of patients with lung cancer: relation to prognosis. Br. J. Cancer 2001, 85, 1193-1200.
    • (2001) Br. J. Cancer , vol.85 , pp. 1193-1200
    • Kos, J.1    Sekirnik, A.2    Kopitar, G.3    Cimerman, N.4
  • 108
    • 78549293229 scopus 로고    scopus 로고
    • Cathepsins B and L in peripheral blood mononuclear cells of pediatric acute myeloid leukemia: potential poor prognostic markers
    • Jain, M., Bakhshi, S., Shukla, A. A., Chauhan, S. S., Cathepsins B and L in peripheral blood mononuclear cells of pediatric acute myeloid leukemia: potential poor prognostic markers. Ann. Hematol. 2010, 89, 1223-1232.
    • (2010) Ann. Hematol. , vol.89 , pp. 1223-1232
    • Jain, M.1    Bakhshi, S.2    Shukla, A.A.3    Chauhan, S.S.4
  • 109
    • 12344325808 scopus 로고    scopus 로고
    • Serum cathepsin H as a potential prognostic marker in patients with colorectal cancer
    • Schweiger, A., Christensen, I. J., Nielsen, H. J., Sørensen, S. et al., Serum cathepsin H as a potential prognostic marker in patients with colorectal cancer. Int. J. Biol. Markers 2004, 19, 289-294.
    • (2004) Int. J. Biol. Markers , vol.19 , pp. 289-294
    • Schweiger, A.1    Christensen, I.J.2    Nielsen, H.J.3    Sørensen, S.4
  • 110
    • 84867296995 scopus 로고    scopus 로고
    • Cathepsin X in serum from patients with colorectal cancer: relation to prognosis
    • Vizin, T., Christensen, I. J., Nielsen, H. J., Kos, J., Cathepsin X in serum from patients with colorectal cancer: relation to prognosis. Radiol. Oncol. 2012, 46, 207-212.
    • (2012) Radiol. Oncol , vol.46 , pp. 207-212
    • Vizin, T.1    Christensen, I.J.2    Nielsen, H.J.3    Kos, J.4
  • 111
    • 33646518541 scopus 로고    scopus 로고
    • Increased serum cathepsin S in patients with atherosclerosis and diabetes
    • Liu, J., Ma, L., Yang, J., Ren, A. et al., Increased serum cathepsin S in patients with atherosclerosis and diabetes. Atherosclerosis 2006, 186, 411-419.
    • (2006) Atherosclerosis , vol.186 , pp. 411-419
    • Liu, J.1    Ma, L.2    Yang, J.3    Ren, A.4
  • 112
    • 59049103199 scopus 로고    scopus 로고
    • Usefulness of serum cathepsin L as an independent biomarker in patients with coronary heart disease
    • Liu, Y., Li, X., Peng, D., Tan, Z. et al., Usefulness of serum cathepsin L as an independent biomarker in patients with coronary heart disease. Am. J. Cardiol. 2009, 103, 476-481.
    • (2009) Am. J. Cardiol. , vol.103 , pp. 476-481
    • Liu, Y.1    Li, X.2    Peng, D.3    Tan, Z.4
  • 113
    • 66249143728 scopus 로고    scopus 로고
    • Cystatin C and NT-proBNP, a powerful combination of biomarkers for predicting cardiovascular mortality in elderly patients with heart failure: results from a 10-year study in primary care
    • Alehagen, U., Dahlström, U., Lindahl, T. L., Cystatin C and NT-proBNP, a powerful combination of biomarkers for predicting cardiovascular mortality in elderly patients with heart failure: results from a 10-year study in primary care. Eur. J. Heart Fail. 2009, 11, 354-360.
    • (2009) Eur. J. Heart Fail , vol.11 , pp. 354-360
    • Alehagen, U.1    Dahlström, U.2    Lindahl, T.L.3
  • 114
    • 84881222169 scopus 로고    scopus 로고
    • Identification, prioritization, and evaluation of glycoproteins for aggressive prostate cancer using quantitative glycoproteomics and antibody-based assays on tissue specimens
    • Chen, J., Xi, J., Tian, Y., Bova, G. S., Zhang, H., Identification, prioritization, and evaluation of glycoproteins for aggressive prostate cancer using quantitative glycoproteomics and antibody-based assays on tissue specimens. Proteomics 2013, 13, 2268-2277.
    • (2013) Proteomics , vol.13 , pp. 2268-2277
    • Chen, J.1    Xi, J.2    Tian, Y.3    Bova, G.S.4    Zhang, H.5
  • 115
    • 33846167705 scopus 로고    scopus 로고
    • Activity based probes for proteases: applications to biomarker discovery, molecular imaging and drug screening
    • Fonović, M., Bogyo, M., Activity based probes for proteases: applications to biomarker discovery, molecular imaging and drug screening. Curr. Pharm. Des. 2007, 13, 253-261.
    • (2007) Curr. Pharm. Des. , vol.13 , pp. 253-261
    • Fonović, M.1    Bogyo, M.2
  • 116
    • 84862873324 scopus 로고    scopus 로고
    • Activity-based probes for the study of proteases: recent advances and developments
    • Serim, S., Haedke, U., Verhelst, S. H., Activity-based probes for the study of proteases: recent advances and developments. Chem. Med. Chem. 2012, 7, 1146-1159.
    • (2012) Chem. Med. Chem. , vol.7 , pp. 1146-1159
    • Serim, S.1    Haedke, U.2    Verhelst, S.H.3
  • 118
    • 43749107913 scopus 로고    scopus 로고
    • Application of activity-based probes to the study of enzymes involved in cancer progression
    • Paulick, M. G., Bogyo, M., Application of activity-based probes to the study of enzymes involved in cancer progression. Curr. Opin. Genet. Dev. 2008, 18, 97-106.
    • (2008) Curr. Opin. Genet. Dev. , vol.18 , pp. 97-106
    • Paulick, M.G.1    Bogyo, M.2
  • 119
    • 79551503110 scopus 로고    scopus 로고
    • Functional in vivo imaging of cysteine cathepsin activity in murine model of inflammation
    • Caglič, D., Globisch, A., Kindermann, M., Lim, N. H. et al., Functional in vivo imaging of cysteine cathepsin activity in murine model of inflammation. Bioorg. Med. Chem. 2011, 19, 1055-1061.
    • (2011) Bioorg. Med. Chem. , vol.19 , pp. 1055-1061
    • Caglič, D.1    Globisch, A.2    Kindermann, M.3    Lim, N.H.4
  • 120
    • 33846821908 scopus 로고    scopus 로고
    • Proteomic discovery of protease substrates
    • Schilling, O., Overall, C. M., Proteomic discovery of protease substrates. Curr. Opin. Chem. Biol. 2007, 11, 36-45.
    • (2007) Curr. Opin. Chem. Biol. , vol.11 , pp. 36-45
    • Schilling, O.1    Overall, C.M.2
  • 121
    • 84858969517 scopus 로고    scopus 로고
    • Functional protease profiling for diagnosis of malignant disease
    • Findeisen, P., Neumaier, M., Functional protease profiling for diagnosis of malignant disease. Proteomics Clin. Appl. 2012, 6, 60-78.
    • (2012) Proteomics Clin. Appl. , vol.6 , pp. 60-78
    • Findeisen, P.1    Neumaier, M.2
  • 122
    • 27144473929 scopus 로고    scopus 로고
    • Caspase-specific and nonspecific in vivo protein processing during Fas-induced apoptosis
    • Van Damme, P., Martens, L., Van Damme, J., Hugelier, K. et al., Caspase-specific and nonspecific in vivo protein processing during Fas-induced apoptosis. Nat. Methods 2005, 2, 771-777.
    • (2005) Nat. Methods , vol.2 , pp. 771-777
    • Van Damme, P.1    Martens, L.2    Van Damme, J.3    Hugelier, K.4
  • 123
    • 33847276695 scopus 로고    scopus 로고
    • In search of partners: linking extracellular proteases to substrates
    • Overall, C. M., Blobel, C. P., In search of partners: linking extracellular proteases to substrates. Nat. Rev. Mol. Cell Biol. 2007, 8, 245-257.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 245-257
    • Overall, C.M.1    Blobel, C.P.2
  • 124
    • 0038333588 scopus 로고    scopus 로고
    • Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides
    • Gevaert, K., Goethals, M., Martens, L., Van Damme, J. et al., Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat. Biotechnol. 2003, 21, 566-569.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 566-569
    • Gevaert, K.1    Goethals, M.2    Martens, L.3    Van Damme, J.4
  • 125
    • 82755164012 scopus 로고    scopus 로고
    • Proteomic identification of protease cleavage sites characterizes prime and non-prime specificity of cysteine cathepsins B, L, and S
    • Biniossek, M. L., Nägler, D. K., Becker-Pauly, C., Schilling, O., Proteomic identification of protease cleavage sites characterizes prime and non-prime specificity of cysteine cathepsins B, L, and S. J. Proteome Res. 2011, 10, 5363-5373.
    • (2011) J. Proteome Res. , vol.10 , pp. 5363-5373
    • Biniossek, M.L.1    Nägler, D.K.2    Becker-Pauly, C.3    Schilling, O.4
  • 126
    • 84893850175 scopus 로고    scopus 로고
    • Double deficiency of cathepsins B and L results in massive secretome alterations and suggests a degradative cathepsin-MMP axis
    • Tholen, S., Biniossek, M. L., Gansz, M., Ahrens, T. D. et al., Double deficiency of cathepsins B and L results in massive secretome alterations and suggests a degradative cathepsin-MMP axis. Cell Mol. Life Sci. 2013, 71, 899-916.
    • (2013) Cell Mol. Life Sci. , vol.71 , pp. 899-916
    • Tholen, S.1    Biniossek, M.L.2    Gansz, M.3    Ahrens, T.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.