Cysteine cathepsins and caspases in silicosis

References

Abrahamson, M., Buttle, D.J., Mason, R.W., Hansson, H., Grubb, A., Lilja, H., and Ohlsson, K. (1991a). Regulation of cystatin C activity by serine proteinases. Biomed. Biochim. Acta50, 587–593.Search in Google Scholar

Abrahamson, M., Mason, R.W., Hansson, H., Buttle, D.J., Grubb, A., and Ohlsson, K. (1991b). Human cystatin C. role of the N-terminal segment in the inhibition of human cysteine proteinases and in its inactivation by leucocyte elastase. Biochem. J.273, 621–626.10.1042/bj2730621Search in Google Scholar

Abrahamson, M., Alvarez-Fernandez, M., and Nathanson, C.M. (2003). Cystatins. Biochem. Soc. Symp.70, 179–199.Search in Google Scholar

Barnes, P.J. (1998). New therapies for chronic obstructive pulmonary disease. Thorax53, 137–147.10.1136/thx.53.2.137Search in Google Scholar

Barnes, P.J., Shapiro, S.D., and Pauwels, R.A. (2003). Chronic obstructive pulmonary disease: molecular and cellular mechanisms. Eur. Respir. J.22, 672–688.10.1183/09031936.03.00040703Search in Google Scholar

Borges, V.M., Falcao, H., Leite-Junior, J.H., Alvim, L., Teixeira, G.P., Russo, M., Nobrega, A.F., Lopes, M.F., Rocco, P.M., Davidson, W.F., Linden, R., Yagita, H., Zin, W.A., and DosReis, G.A. (2001). Fas ligand triggers pulmonary silicosis. J. Exp. Med.194, 155–164.10.1084/jem.194.2.155Search in Google Scholar

Borges, V.M., Lopes, M.F., Falcao, H., Leite-Junior, J.H., Rocco, P.R., Davidson, W.F., Linden, R., Zin, W.A., and DosReis, G.A. (2002). Apoptosis underlies immunopathogenic mechanisms in acute silicosis. Am. J. Respir. Cell. Mol. Biol.27, 78–84.10.1165/ajrcmb.27.1.4717Search in Google Scholar

Brain, J.D. (1986). Toxicological aspects of alterations of pulmonary macrophage function. Annu. Rev. Pharmacol. Toxicol.26, 547–565.10.1146/annurev.pa.26.040186.002555Search in Google Scholar

Brasch, F., Ten Brinke, A., Johnen, G., Ochs, M., Kapp, N., Muller, K.M., Beers, M.F., Fehrenbach, H., Richter, J., Batenburg, J.J., and Buhling, F. (2002). Involvement of cathepsin H in the processing of the hydrophobic surfactant-associated protein C in type II pneumocytes. Am. J. Respir. Cell. Mol. Biol.26, 659–670.10.1165/ajrcmb.26.6.4744Search in Google Scholar

Buhling, F., Gerber, A., Ansorge, S., and Welte, T. (1999). Cathepsin cysteine proteinases in the lung. Pneumologie53, 400–407.Search in Google Scholar

Buhling, F., Reisenauer, A., Gerber, A., Kruger, S., Weber, E., Bromme, D., Roessner, A., Ansorge, S., Welte, T., and Rocken, C. (2001). Cathepsin K: a marker of macrophage differentiation? J. Pathol.195, 375–382.10.1002/path.959Search in Google Scholar

Buhling, F., Rocken, C., Brasch, F., Hartig, R., Yasuda, Y., Saftig, P., Bromme, D., and Welte, T. (2004). Pivotal role of cathepsin K in lung fibrosis. Am. J. Pathol.164, 2203–2216.10.1016/S0002-9440(10)63777-7Search in Google Scholar

Buhling, F., Wille, A., Rocken, C., Wiesner, O., Baier, A., Meinecke, I., Welte, T., and Pap, T. (2005). Altered expression of membrane-bound and soluble CD95/Fas contributes to the resistance of fibrotic lung fibroblasts to FasL induced apoptosis. Respir. Res.6, 37.10.1186/1465-9921-6-37Search in Google Scholar PubMed PubMed Central

Buttle, D.J., Abrahamson, M., Burnett, D., Mort, J.S., Barrett, A.J., Dando, P.M., and Hill, S.L. (1991). Human sputum cathepsin B degrades proteoglycan, is inhibited by α2-macroglobulin and is modulated by neutrophil elastase cleavage of cathepsin B precursor and cystatin C. Biochem. J.276, 325–331.10.1042/bj2760325Search in Google Scholar

Castranova, V. and Vallyathan, V. (2000). Silicosis and coal workers' pneumoconiosis. Environ. Health Perspect.108 (Suppl. 4), 675–684.Search in Google Scholar

Chang, J.C., Lesser, M., Yoo, O.H., and Orlowski, M. (1986). Increased cathepsin B-like activity in alveolar macrophages and bronchoalveolar lavage fluid from smokers. Am. Rev. Respir. Dis.134, 538–541.Search in Google Scholar

Chao, S.K., Hamilton, R.F., Pfau, J.C., and Holian, A. (2001). Cell surface regulation of silica-induced apoptosis by the SR-A scavenger receptor in a murine lung macrophage cell line (MH-S). Toxicol. Appl. Pharmacol.174, 10–16.10.1006/taap.2001.9190Search in Google Scholar

Chapman, H.A. Jr. and Shi, G.P. (2000). Protease injury in the development of COPD. Chest117, 295S–299S.10.1378/chest.117.5_suppl_1.295SSearch in Google Scholar

Chapman, H.A., Riese, R.J., and Shi, G.P. (1997). Emerging roles for cysteine proteases in human biology. Annu. Rev. Physiol.59, 63–88.10.1146/annurev.physiol.59.1.63Search in Google Scholar

Davidson, J.M. (1990). Biochemistry and turnover of lung interstitium. Eur. Respir. J.3, 1048–1063.10.1183/09031936.93.03091048Search in Google Scholar

Denault, J.B. and Salvesen, G.S. (2002). Caspases: keys in the ignition of cell death. Chem. Rev.102, 4489–4500.10.1021/cr010183nSearch in Google Scholar

DosReis, G.A., Borges, V.M., and Zin, W.A. (2004). The central role of Fas-ligand cell signaling in inflammatory lung diseases. J. Cell. Mol. Med.8, 285–293.10.1111/j.1582-4934.2004.tb00318.xSearch in Google Scholar

Everts, V., van der Zee, E., Creemers, L., and Beertsen, W. (1996). Phagocytosis and intracellular digestion of collagen, its role in turnover and remodelling. Histochem. J.28, 229–245.10.1007/BF02409011Search in Google Scholar

Feng, G.H., Bailin, T., Oh, J., and Spritz, R.A. (1997). Mouse pale ear (ep) is homologous to human Hermansky-Pudlak syndrome and contains a rare ‘AT-AC’ intron. Hum. Mol. Genet.6, 793–697.10.1093/hmg/6.5.793Search in Google Scholar

Ferri, K.F. and Kroemer, G. (2001). Organelle-specific initiation of cell death pathways. Nat. Cell Biol.3, 255–263.10.1038/ncb1101-e255Search in Google Scholar

Fubini, B. and Hubbard, A. (2003). Reactive oxygen species (ROS) and reactive nitrogen species (RNS) generation by silica in inflammation and fibrosis. Free Radic. Biol. Med.34, 1507–1516.10.1016/S0891-5849(03)00149-7Search in Google Scholar

Fuentes-Prior, P. and Salvesen, G.S. (2004). The protein structures that shape caspase activity, specificity, activation and inhibition. Biochem. J.384, 201–232.10.1042/BJ20041142Search in Google Scholar

Garnero, P., Borel, O., Byrjalsen, I., Ferreras, M., Drake, F.H., McQueney, M.S., Foged, N.T., Delmas, P.D., and Delaisse, J.M. (1998). The collagenolytic activity of cathepsin K is unique among mammalian proteinases. J. Biol. Chem.273, 32347–32352.10.1074/jbc.273.48.32347Search in Google Scholar

Guicciardi, M.E., Deussing, J., Miyoshi, H., Bronk, S.F., Svingen, P.A., Peters, C., Kaufmann, S.H., and Gores, G.J. (2000). Cathepsin B contributes to TNF-α-mediated hepatocyte apoptosis by promoting mitochondrial release of cytochrome c. J. Clin. Invest.106, 1127–1137.10.1172/JCI9914Search in Google Scholar

Guttentag, S., Robinson, L., Zhang, P., Brasch, F., Buhling, F., and Beers, M. (2003). Cysteine protease activity is required for surfactant protein B processing and lamellar body genesis. Am. J. Respir. Cell. Mol. Biol.28, 69–79.10.1165/rcmb.2002-0111OCSearch in Google Scholar

Hannothiaux, M.H., Scharfman, A., Wastiaux, A., Cornu, L., van Brussel, E., Lafitte, J.J., Sebastien, P., and Roussel, P. (1991). An attempt to evaluate lung aggression in monkey silicosis: hydrolases, peroxidase and antiproteases activities in serial bronchoalveolar lavages. Eur. Respir. J.4, 191–204.10.1183/09031936.93.04020191Search in Google Scholar

Heidtmann, H.H., Salge, U., Havemann, K., Kirschke, H., and Wiederanders, B. (1993). Secretion of a latent, acid activatable cathepsin L precursor by human non-small cell lung cancer cell lines. Oncol. Res.5, 441–451.Search in Google Scholar

Henskens, Y.M., Veerman, E.C., and Nieuw Amerongen, A.V. (1996). Cystatins in health and disease. Biol. Chem. Hoppe-Seyler377, 71–86.Search in Google Scholar

Hermansky, F. and Pudlak, P. (1959). Albinism associated with hemorrhagic diathesis and unusual pigmented reticular cells in the bone marrow: report of two cases with histochemical studies. Blood14, 162–169.10.1182/blood.V14.2.162.162Search in Google Scholar

Ishii, Y., Hashizume, Y., Watanabe, T., Waguri, S., Sato, N., Yamamoto, M., Hasegawa, S., Kominami, E., and Uchiyama, Y. (1991). Cysteine proteinases in bronchoalveolar epithelial cells and lavage fluid of rat lung. J. Histochem. Cytochem.39, 461–468.10.1177/39.4.2005374Search in Google Scholar

Ivy, G.O., Kanai, S., Ohta, M., Smith, G., Sato, Y., Kobayashi, M., and Kitani, K. (1989). Lipofuscin-like substances accumulate rapidly in brain, retina and internal organs with cysteine protease inhibition. Adv. Exp. Med. Biol.266, 31–45.Search in Google Scholar

Iyer, R. and Holian, A. (1997). Involvement of the ICE family of proteases in silica-induced apoptosis in human alveolar macrophages. Am. J. Physiol.273, L760–767.10.1152/ajplung.1997.273.4.L760Search in Google Scholar

Iyer, R., Hamilton, R.F., Li, L., and Holian, A. (1996). Silica-induced apoptosis mediated via scavenger receptor in human alveolar macrophages. Toxicol. Appl. Pharmacol.141, 84–92.10.1016/S0041-008X(96)80012-3Search in Google Scholar

Johnson, D.A., Barrett, A.J., and Mason, R.W. (1986). Cathepsin L inactivates a1-proteinase inhibitor by cleavage in the reactive site region. J. Biol. Chem.261, 14748–14751.10.1016/S0021-9258(18)66935-2Search in Google Scholar

Langley, R.J., Kalra, R., Mishra, N.C., Hahn, F.F., Razani-Boroujerdi, S., Singh, S.P., Benson, J.M., Pena-Philippides, J.C., Barr, E.B., and Sopori, M.L. (2004). A biphasic response to silica: I. Immunostimulation is restricted to the early stage of silicosis in Lewis rats. Am. J. Respir. Cell. Mol. Biol.30, 823–829.Search in Google Scholar

Lecaille, F., Kaleta, J., and Bromme, D. (2002). Human and parasitic papain-like cysteine proteases: their role in physiology and pathology and recent developments in inhibitor design. Chem. Rev.102, 4459–4488.10.1021/cr0101656Search in Google Scholar PubMed

Lesser, M., Padilla, M.L., and Cardozo, C. (1992). Induction of emphysema in hamsters by intratracheal instillation of cathepsin B. Am. Rev. Respir. Dis.145, 661–668.10.1164/ajrccm/145.3.661Search in Google Scholar

Luthgens, K., Ebert, W., Trefz, G., Gabrijelcic, D., Turk, V., and Lah, T. (1993). Cathepsin B and cysteine proteinase inhibitors in bronchoalveolar lavage fluid of lung cancer patients. Cancer Detect. Prev.17, 387–397.Search in Google Scholar

Majerle, A. and Jerala, R. (2003). Protein inhibitors form complexes with procathepsin L and augment cleavage of the propeptide. Arch. Biochem. Biophys.417, 53–58.10.1016/S0003-9861(03)00319-9Search in Google Scholar

Mossman, B.T. and Churg, A. (1998). Mechanisms in the pathogenesis of asbestosis and silicosis. Am. J. Respir. Crit. Care Med.157, 1666–1680.10.1164/ajrccm.157.5.9707141Search in Google Scholar

Oh, J., Bailin, T., Fukai, K., Feng, G.H., Ho, L., Mao, J.I., Frenk, E., Tamura, N., and Spritz, R.A. (1996). Positional cloning of a gene for Hermansky-Pudlak syndrome, a disorder of cytoplasmic organelles. Nat. Genet.14, 300–306.10.1038/ng1196-300Search in Google Scholar

Ohashi, K., Naruto, M., Nakaki, T., and Sano, E. (2003). Identification of interleukin-8 converting enzyme as cathepsin L. Biochim. Biophys. Acta1649, 30–39.10.1016/S1570-9639(03)00152-3Search in Google Scholar

Owen, C.A. and Campbell, E.J. (1999a). The cell biology of leukocyte-mediated proteolysis. J. Leukoc. Biol.65, 137–150.10.1002/jlb.65.2.137Search in Google Scholar

Owen, C.A. and Campbell, E.J. (1999b). Extracellular proteolysis: new paradigms for an old paradox. J. Lab. Clin. Med.134, 341–351.10.1016/S0022-2143(99)90148-8Search in Google Scholar

Perdereau, C., Godat, E., Maurel, M.C., Hazouard, E., Diot, E., and Lalmanach, G. (2006). Cysteine cathepsins in human silicotic bronchoalveolar lavage fluids. Biochim. Biophys. Acta1762, 351–356.10.1016/j.bbadis.2005.10.005Search in Google Scholar

Perez-Ramos, J., de Lourdes Segura-Valdez, M., Vanda, B., Selman, M., and Pardo, A. (1999). Matrix metalloproteinases 2, 9, and 13, and tissue inhibitors of metalloproteinases 1 and 2 in experimental lung silicosis. Am. J. Respir. Crit. Care Med.160, 1274–1282.10.1164/ajrccm.160.4.9808006Search in Google Scholar

Pettus, B.J., Chalfant, C.E., and Hannun, Y.A. (2002). Ceramide in apoptosis: an overview and current perspectives. Biochim. Biophys. Acta1585, 114–125.10.1016/S1388-1981(02)00331-1Search in Google Scholar

Porter, D.W., Ye, J., Ma, J., Barger, M., Robinson, V.A., Ramsey, D., McLaurin, J., Khan, A., Landsittel, D., Teass, A., and Castranova, V. (2002). Time course of pulmonary response of rats to inhalation of crystalline silica: NF-κB activation, inflammation, cytokine production, and damage. Inhal. Toxicol.14, 349–367.10.1080/08958370252870998Search in Google Scholar

Punturieri, A., Filippov, S., Allen, E., Caras, I., Murray, R., Reddy, V., and Weiss, S.J. (2000). Regulation of elastinolytic cysteine proteinase activity in normal and cathepsin K-deficient human macrophages. J. Exp. Med.192, 789–799.10.1084/jem.192.6.789Search in Google Scholar

Reddy, V.Y., Zhang, Q.Y., and Weiss, S.J. (1995). Pericellular mobilization of the tissue-destructive cysteine proteinases, cathepsins B, L, and S, by human monocyte-derived macrophages. Proc. Natl. Acad. Sci. USA92, 3849–3853.10.1073/pnas.92.9.3849Search in Google Scholar

Reilly, J.J. Jr., Chen, P., Sailor, L.Z., Wilcox, D., Mason, R.W., and Chapman, H.A. Jr. (1991). Cigarette smoking induces an elastolytic cysteine proteinase in macrophages distinct from cathepsin L. Am. J. Physiol.261, L41–88.10.1152/ajplung.1991.261.2.L41Search in Google Scholar

Rosenman, K.D., Moore-Fuller, M., and Reilly, M.J. (1999). Connective tissue disease and silicosis. Am. J. Ind. Med.35, 375–381.10.1002/(SICI)1097-0274(199904)35:4<375::AID-AJIM8>3.0.CO;2-ISearch in Google Scholar

Salvesen, G.S. and Abrams, J.M. (2004). Caspase activation-stepping on the gas or releasing the brakes? Lessons from humans and flies. Oncogene23, 2774–2784.10.1038/sj.onc.1207522Search in Google Scholar

Sarih, M., Souvannavong, V., Brown, S.C., and Adam, A. (1993). Silica induces apoptosis in macrophages and the release of interleukin-1α and interleukin-1β. J. Leukoc. Biol.54, 407–413.10.1002/jlb.54.5.407Search in Google Scholar

Scabilloni, J.F., Wang, L., Antonini, J.M., Roberts, J.R., Castranova, V., and Mercer, R.R. (2005). Matrix metalloproteinase induction in fibrosis and fibrotic nodule formation due to silica inhalation. Am. J. Physiol. Lung Cell. Mol. Physiol.288, L709–L717.10.1152/ajplung.00034.2004Search in Google Scholar

Serveau-Avesque, C., Ferrer-Di Martino, M., Herve-Grepinet, V., Hazouard, E., Gauthier, F., Diot, E., and Lalmanach, G. (2006). Active cathepsins B, H, K, L and S in human inflammatory bronchoalveolar lavage fluids. Biol. Cell98, 15–22.10.1042/BC20040512Search in Google Scholar

Shangary, S., Lerner, E.C., Zhan, Q., Corey, S.J., Smithgall, T.E., and Baskaran, R. (2003). Lyn regulates the cell death response to ultraviolet radiation through c-Jun N terminal kinase-dependent Fas ligand activation. Exp. Cell. Res.289, 67–76.10.1016/S0014-4827(03)00234-9Search in Google Scholar

Shapiro, S.D. (2002). Proteinases in chronic obstructive pulmonary disease. Biochem. Soc. Trans.30, 98–102.10.1042/bst0300098Search in Google Scholar

Shen, H.M., Zhang, Z., Zhang, Q.F., and Ong, C.N. (2001). Reactive oxygen species and caspase activation mediate silica-induced apoptosis in alveolar macrophages. Am. J. Physiol. Lung Cell. Mol. Physiol.280, L10–L17.10.1152/ajplung.2001.280.1.L10Search in Google Scholar

Shi, G.P., Bryant, R.A., Riese, R., Verhelst, S., Driessen, C., Li, Z., Bromme, D., Ploegh, H.L., and Chapman, H.A. (2000). Role for cathepsin F in invariant chain processing and major histocompatibility complex class II peptide loading by macrophages. J. Exp. Med.191, 1177–1186.10.1084/jem.191.7.1177Search in Google Scholar

Steenland, K. and Goldsmith, D.F. (1995). Silica exposure and autoimmune diseases. Am. J. Ind. Med.28, 603–608.10.1002/ajim.4700280505Search in Google Scholar

Stockley, R.A. (1999). Neutrophils and protease/antiprotease imbalance. Am. J. Respir. Crit. Care Med.160, S49–S52.10.1164/ajrccm.160.supplement_1.13Search in Google Scholar

Stoka, V., Turk, B., Schendel, S.L., Kim, T.H., Cirman, T., Snipas, S.J., Ellerby, L.M., Bredesen, D., Freeze, H., Abrahamson, M., et al. (2001). Lysosomal protease pathways to apoptosis. Cleavage of bid, not pro-caspases, is the most likely route. J. Biol. Chem.276, 3149–3157.10.1074/jbc.M008944200Search in Google Scholar

Taggart, C., Cervantes-Laurean, D., Kim, G., McElvaney, N.G., Wehr, N., Moss, J., and Levine, R.L. (2000). Oxidation of either methionine 351 or methionine 358 in α1-antitrypsin causes loss of anti-neutrophil elastase activity. J. Biol. Chem.275, 27258–27265.10.1016/S0021-9258(19)61505-XSearch in Google Scholar

Taggart, C.C., Lowe, G.J., Greene, C.M., Mulgrew, A.T., O'Neill, S.J., Levine, R.L., and McElvaney, N.G. (2001). Cathepsin B, L, and S cleave and inactivate secretory leucoprotease inhibitor. J. Biol. Chem.276, 33345–33352.10.1074/jbc.M103220200Search in Google Scholar PubMed

Taggart, C.C., Greene, C.M., Smith, S.G., Levine, R.L., McCray, P.B. Jr., O'Neill, S., and McElvaney, N.G. (2003). Inactivation of human b-defensins 2 and 3 by elastolytic cathepsins. J. Immunol.171, 931–937.10.4049/jimmunol.171.2.931Search in Google Scholar PubMed

Takahashi, H., Ishidoh, K., Muno, D., Ohwada, A., Nukiwa, T., Kominami, E., and Kira, S. (1993). Cathepsin L activity is increased in alveolar macrophages and bronchoalveolar lavage fluid of smokers. Am. Rev. Respir. Dis.147, 1562–1568.10.1164/ajrccm/147.6_Pt_1.1562Search in Google Scholar PubMed

Takeyabu, K., Betsuyaku, T., Nishimura, M., Yoshioka, A., Tanino, M., Miyamoto, K., and Kawakami, Y. (1998). Cysteine proteinases and cystatin C in bronchoalveolar lavage fluid from subjects with subclinical emphysema. Eur. Respir. J.12, 1033–1039.10.1183/09031936.98.12051033Search in Google Scholar

Thibodeau, M., Giardina, C., and Hubbard, A.K. (2003). Silica-induced caspase activation in mouse alveolar macrophages is dependent upon mitochondrial integrity and aspartic proteolysis. Toxicol. Sci.76, 91–101.10.1093/toxsci/kfg178Search in Google Scholar

Thibodeau, M.S., Giardina, C., Knecht, D.A., Helble, J., and Hubbard, A.K. (2004). Silica-induced apoptosis in mouse alveolar macrophages is initiated by lysosomal enzyme activity. Toxicol. Sci.80, 34–48.10.1093/toxsci/kfh121Search in Google Scholar

Thome, M. and Tschopp, J. (2001). Regulation of lymphocyte proliferation and death by FLIP. Nat. Rev. Immunol.1, 50–58.10.1038/35095508Search in Google Scholar

Thornberry, N.A., Bull, H.G., Calaycay, J.R., Chapman, K.T., Howard, A.D., Kostura, M.J., Miller, D.K., Molineaux, S.M., Weidner, J.R., Aunins, J., et al. (1992). A novel heterodimeric cysteine protease is required for interleukin-1β processing in monocytes. Nature356, 768–774.10.1038/356768a0Search in Google Scholar

Tomita, K., Caramori, G., Lim, S., Ito, K., Hanazawa, T., Oates, T., Chiselita, I., Jazrawi, E., Chung, K.F., Barnes, P.J., and Adcock, I.M. (2002). Increased p21(CIP1/WAF1) and B cell lymphoma leukemia-x(L) expression and reduced apoptosis in alveolar macrophages from smokers. Am. J. Respir. Crit. Care Med.166, 724–731.10.1164/rccm.2104010Search in Google Scholar

Travis, J. and Salvesen, G.S. (1983). Human plasma proteinase inhibitors. Annu. Rev. Biochem.52, 655–709.10.1146/annurev.bi.52.070183.003255Search in Google Scholar

Turk, V. and Bode, W. (1991). The cystatins: protein inhibitors of cysteine proteinases. FEBS Lett.285, 213–219.10.1016/0014-5793(91)80804-CSearch in Google Scholar

Turk, B., Turk, D., and Turk, V. (2000). Lysosomal cysteine proteases: more than scavengers. Biochim. Biophys. Acta1477, 98–111.10.1016/S0167-4838(99)00263-0Search in Google Scholar

Turk, V., Turk, B., and Turk, D. (2001). Lysosomal cysteine proteases: facts and opportunities. EMBO J.20, 4629–4633.10.1093/emboj/20.17.4629Search in Google Scholar PubMed PubMed Central

Ueki, A., Isozaki, Y., and Kusaka, M. (2005). Anti-caspase-8 autoantibody response in silicosis patients is associated with HLA-DRB1, DQB1 and DPB1 alleles. J. Occup. Health47, 61–67.10.1539/joh.47.61Search in Google Scholar PubMed

Ulbricht, B., Hagmann, W., Ebert, W., and Spiess, E. (1996). Differential secretion of cathepsins B and L from normal and tumor human lung cells stimulated by 12(S)-hydroxy-eicosatetraenoic acid. Exp. Cell. Res.226, 255–263.10.1006/excr.1996.0226Search in Google Scholar PubMed

Van den Brule, S., Misson, P., Buhling, F., Lison, D., and Huaux, F. (2005). Overexpression of cathepsin K during silica-induced lung fibrosis and control by TGF-β. Respir. Res.6, 84.10.1186/1465-9921-6-84Search in Google Scholar PubMed PubMed Central

Vanhee, D., Gosset, P., Boitelle, A., Wallaert, B., and Tonnel, A.B. (1995). Cytokines and cytokine network in silicosis and coal workers' pneumoconiosis. Eur. Respir. J.8, 834–842.10.1183/09031936.95.08050834Search in Google Scholar

Wang, Z., Zheng, T., Zhu, Z., Homer, R.J., Riese, R.J., Chapman, H.A. Jr., Shapiro, S.D., and Elias, J.A. (2000). Interferon γ induction of pulmonary emphysema in the adult murine lung. J. Exp. Med.192, 1587–1600.10.1084/jem.192.11.1587Search in Google Scholar PubMed PubMed Central

Wolters, P.J. and Chapman, H.A. (2000). Importance of lysosomal cysteine proteases in lung disease. Respir. Res.1, 170–177.10.1186/rr29Search in Google Scholar PubMed PubMed Central

Yasuda, Y., Li, Z., Greenbaum, D., Bogyo, M., Weber, E., and Bromme, D. (2004). Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages. J. Biol. Chem.279, 36761–36770.10.1074/jbc.M403986200Search in Google Scholar PubMed

Yayoi, Y., Ohsawa, Y., Koike, M., Zhang, G., Kominami, E., and Uchiyama, Y. (2001). Specific localization of lysosomal aminopeptidases in type II alveolar epithelial cells of the rat lung. Arch. Histol. Cytol.64, 89–97.10.1679/aohc.64.89Search in Google Scholar PubMed

Yoshioka, Y., Kumasaka, T., Ishidoh, K., Kominami, E., Mitani, K., Hosokawa, Y., and Fukuchi, Y. (2004). Inflammatory response and cathepsins in silica-exposed Hermansky-Pudlak syndrome model pale ear mice. Pathol. Int.54, 322–331.10.1111/j.1440-1827.2004.01626.xSearch in Google Scholar PubMed

Zheng, T., Zhu, Z., Wang, Z., Homer, R.J., Ma, B., Riese, R.J. Jr., Chapman, H.A. Jr., Shapiro, S.D., and Elias, J.A. (2000). Inducible targeting of IL-13 to the adult lung causes matrix metalloproteinase- and cathepsin-dependent emphysema. J. Clin. Invest.106, 1081–1093.10.1172/JCI10458Search in Google Scholar PubMed PubMed Central