Cathepsins: Fundamental effectors of endolysosomal proteolysis

Indian Journal of Biochemistry and Biophysics

Volumn 45, Issue 2, 2008, Pages 75-90

  Guha, Sonia ^a   Padh, Harish ^a  

^a B V PATEL PHARMACEUTICAL EDUCATION AND RESEARCH DEVELOPMENT PERD CENTRE   (India)

Author keywords

Cathepsins; Endosome; Intracellular proteolysis

Indexed keywords

CATHEPSIN;

AMINO ACID SEQUENCE; CHEMISTRY; HYDROLYSIS; LYSOSOME; METABOLISM; MOLECULAR GENETICS; SHORT SURVEY;

AMINO ACID SEQUENCE; CATHEPSINS; HYDROLYSIS; LYSOSOMES; MOLECULAR SEQUENCE DATA;

EUKARYOTA;

EID: 84924272105     PISSN: 03011208     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Short Survey

References (157)

1. Conner S D & Schmid S L (2003) Regulated portals of entry into the cell. Nature 422, 37-44
2. Tjelle T E, Brech A, Juvet L K, Griffiths G & Berg T (1996) Isolation and characterization of early endosomes, late endosomes and terminal lysosomes: their role in protein degradation. J Cell Sci 109, 2905-2914
3. Luzio J P, Rous B A, Bright N A, Pryor P R, Mullock B M & Piper R C (2000) Lysosome-endosome fusion and lysosome biogenesis. J Cell Sci 113, 1515-1524
4. Rink J, Ghigo E, Kalaidzidis Y & Zerial M (2005) Rab conversion as a mechanism of progression from early to late endosomes. Cell 122, 735-749
5. Zerial M & McBride H (2001) Rab proteins as membrane organizers. Nat Rev Mol Cell Biol 2, 107-117
6. De Duve C (1963) The lysosome. Sci Am 208, 64-72
7. Ciechanover A (2005) Proteolysis: from the lysosome to ubiquitin and the proteasome. Nat Rev Mol Cell Biol 6, 79-87
8. Mayorek N, Pinson A & Mayer M (1979) Intracellular proteolysis in rat cardiac and skeletal muscle cells in culture. J Cell Physiol 98, 587-595
9. Diment S & Stahl P (1985) Macrophage endosomes contain proteases which degrade endocytosed protein ligands. J Biol Chem 260, 15311-15317
10. Mayorga L S, Diaz R & Stahl P D (1989) Reconstitution of endosomal proteolysis in a cell-free system. Transfer of immune complexes internalized via Fc receptors to an endosomal proteolytic compartment. J Biol Chem 264, 5392-5399
11. Wiley H S, VanNostrand W, McKinley D N & Cunningham D D (1985) Intracellular processing of epidermal growth factor and its effect on ligand-receptor interactions. J Biol Chem 260, 5290-5295
12. Roederer M, Bowser R & Murphy R F (1987) Kinetics and temperature dependence of exposure of endocytosed material to proteolytic enzymes and low pH: evidence for a maturation model for the formation of lysosomes. J Cell Physiol 131, 200-209
13. Schaudies R P, Gorman R M, Savage C R, Jr. & Poretz R D (1987) Proteolytic processing of epidermal growth factor within endosomes. Biochem Biophys Res Commun 143, 710-715
14. Blum J S, Diaz R, Diment S, Fiani M, Mayorga L, Rodman J S & Stahl P D (1989) Proteolytic processing in endosomal vesicles. Cold Spring Harb Symp Quant Biol 54, 287-292
15. Authier F, Mort J S, Bell A W, Posner B I & Bergeron J J (1995) Proteolysis of glucagon within hepatic endosomes by membrane-associated cathepsins B and D. J Biol Chem 270, 15798-15807
16. Doherty J J, 2nd, Kay D G, Lai W H, Posner B I & Bergeron J J (1990) Selective degradation of insulin within rat liver endosomes. J Cell Biol 110, 35-42
17. Blum J S, Fiani M L & Stahl P D (1991) Proteolytic cleavage of ricin A chain in endosomal vesicles. Evidence for the action of endosomal proteases at both neutral and acidic pH. J Biol Chem 266, 22091-22095
18. Merlen C, Fayol-Messaoudi D, Fabrega S, El Hage T, Servin A & Authier F (2005) Proteolytic activation of internalized cholera toxin within hepatic endosomes by cathepsin D. Febs J 272, 4385-4397
19. Blum J S & Cresswell P (1988) Role for intracellular proteases in the processing and transport of class II HLA antigens. Proc Natl Acad Sci (USA) 85, 3975-3979
20. Runquist E A & Havel R J (1991) Acid hydrolases in early and late endosome fractions from rat liver. J Biol Chem 266, 22557-22563
21. Claus V, Jahraus A, Tjelle T, Berg T, Kirschke H, Faulstich H & Griffiths G (1998) Lysosomal enzyme trafficking between phagosomes, endosomes, and lysosomes in J774 macrophages. Enrichment of cathepsin H in early endosomes. J Biol Chem 273, 9842-9851
22. Authier F, Metioui M, Bell A W & Mort J S (1999) Negative regulation of epidermal growth factor signaling by selective proteolytic mechanisms in the endosome mediated by cathepsin B. J Biol Chem 274, 33723-33731
23. Authier F, Metioui M, Fabrega S, Kouach M & Briand G (2002) Endosomal proteolysis of internalized insulin at the C-terminal region of the B chain by cathepsin D. J Biol Chem 277, 9437-9446
24. Authier F, Kouach M & Briand G (2005) Endosomal proteolysis of insulin-like growth factor-I at its C-terminal D-domain by cathepsin B. FEBS Lett 579, 4309-4316
25. Pillay C S, Elliott E & Dennison C (2002) Endolysosomal proteolysis and its regulation. Biochem J 363, 417-419
26. Takio K, Towatari T, Katunuma N, Teller D C & Titani K (1983) Homology of amino acid sequences of rat liver cathepsins B and H with that of papain. Proc Natl Acad Sci (USA) 80, 3666-3670
27. Lee X, Ahmed F R, Hirama T, Huber C P, Rose D R, To R, Hasnain S, Tarn A & Mort J S (1990) Crystallization of recombinant rat cathepsin B. J Biol Chem 265, 5950-5951
28. Sol-Church K, Frenck J, Bertenshaw G & Mason R W (2000) Characterization of mouse cathepsin R, a new member of a family of placentally expressed cysteine proteases. Biochim Biophys Acta 1492, 488-492
29. Sol-Church K, Frenck J & Mason R W (2000) Mouse cathepsin M, a placenta-specific lysosomal cysteine protease related to cathepsins L and P. Biochim Biophys Acta 1491, 289-294
30. McGrath M E (1999) The lysosomal cysteine proteases. Annu Rev Biophys Biomol Struct 28, 181-204
31. Turk V, Turk B & Turk D (2001) Lysosomal cysteine proteases: facts and opportunities. Embo J 20, 4629-4633
32. Turk V, Turk B, Guncar G, Turk D & Kos J (2002) Lysosomal cathepsins: structure, role in antigen processing and presentation, and cancer. Adv Enzyme Regul 42, 285-303
33. Turk D, Turk B & Turk V (2003) Papain-like lysosomal cysteine proteases and their inhibitors: drug discovery targets? Biochem Soc Symp 70, 15-30
34. van der Drift A C, van Noort J M & Kruse J (1990) Catheptic processing of protein antigens: enzymic and molecular aspects. Semin Immunol 2, 255-271
35. Collette J, Bocock J P, Ahn K, Chapman R L, Godbold G, Yeyeodu S & Erickson A H (2004) Biosynthesis and alternate targeting of the lysosomal cysteine protease cathepsin L. Int Rev Cytol 241, 1-51
36. Brocklehurst K (1994) A sound basis for pH-dependent kinetic studies on enzymes. Protein Eng 7, 291-299
37. Turk B, Turk V & Turk D (1997) Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors. Biol Chem 378, 141-150
38. Ostermann N, Gerhartz B, Worpenberg S, Trappe J & Eder J (2004) Crystal structure of an activation intermediate of cathepsin E. J Mol Biol 342, 889-899
39. Liuzzo J P, Petanceska S S, Moscatelli D & Devi L A (1999) Inflammatory mediators regulate cathepsin S in macrophages and microglia: A role in attenuating heparan sulfate interactions. Mol Med 5, 320-333
40. Schwarz G, Boehncke W H, Braun M, Schroter C J, Burster T, Flad T, Dressel D, Weber E, Schmid H & Kalbacher H (2002) Cathepsin S activity is detectable in human keratinocytes and is selectively upregulated upon stimulation with interferon-gamma. J Invest Dermatol 119, 44-49
41. Storm van's Gravesande K, Layne M D, Ye Q, Le L, Baron R M, Perrella M A, Santambrogio L, Silverman E S & Riese R J (2002) IFN regulatory factor-1 regulates IFN-gamma-dependent cathepsin S expression. J Immunol 168, 4488-4494
42. Beers C, Honey K, Fink S, Forbush K & Rudensky A (2003) Differential regulation of cathepsin S and cathepsin L in interferon gamma-treated macrophages. J Exp Med 197, 169-179
43. Wang Y, Baron R M, Zhu G, Joo M, Christman J W, Silverman E S, Perrella M A, Riese R J & Cernadas M (2006) PU.1 regulates cathepsin S expression in professional APCs. J Immunol 176, 275-283
44. Watari M, Watari H, Nachamkin I & Strauss J F (2000) Lipopolysaccharide induces expression of genes encoding pro-inflammatory cytokines and the elastin-degrading enzyme, cathepsin S, in human cervical smooth-muscle cells. J Soc Gynecol Investig 7, 190-198
45. Rozman J, Stojan J, Kuhelj R, Turk V & Turk B (1999) Autocatalytic processing of recombinant human procathepsin B is a bimolecular process. FEBS Lett 459, 358-362
46. Jerala R, Zerovnik E, Kidric J & Turk V (1998) pH-induced conformational transitions of the propeptide of human cathepsin L. A role for a molten globule state in zymogen activation. J Biol Chem 273, 11498-11504
47. Laurent-Matha V, Derocq D, Prebois C, Katunuma N & Liaudet-Coopman E (2006) Processing of human cathepsin d is independent of its catalytic function and auto-activation: involvement of cathepsins L and B. J Biochem (Tokyo) 139, 363-371
48. Turk B, Dolenc I, Lenarcic B, Krizaj I, Turk V, Bieth J G & Bjork I (1999) Acidic pH as a physiological regulator of human cathepsin L activity. Eur J Biochem 259, 926-932
49. Turk B, Turk D & Salvesen G S (2002) Regulating cysteine protease activity: essential role of protease inhibitors as guardians and regulators. Curr Pharm Des 8, 1623-1637
50. Turk B & Fritz H (2003) Vito Turk-30 years of research on cysteine proteases and their inhibitors. Biol Chem 384, 833-836
51. Lautwein A, Kraus M, Reich M, Burster T, Brandenburg J, Overkleeft H S, Schwarz G, Kammer W, Weber E, Kalbacher H, Nordheim A & Driessen C (2004) Human B lymphoblastoid cells contain distinct patterns of cathepsin activity in endocytic compartments and regulate MHC class II transport in a cathepsin S-independent manner. J Leukoc Biol 75, 844-855
52. Lautwein A, Burster T, Lennon-Dumenil A M, Overkleeft H S, Weber E, Kalbacher H & Driessen C (2002) Inflammatory stimuli recruit cathepsin activity to late endosomal compartments in human dendritic cells. Eur J Immunol 32, 3348-3357
53. Jane D T, Morvay L, Dasilva L, Cavallo-Medved D, Sloane B F & Dufresne M J (2006) Cathepsin B localizes to plasma membrane caveolae of differentiating myoblasts and is secreted in an active form at physiological pH. Biol cell 387, 223-234
54. Stachowiak K, Tokmina M, Karpinska A, Sosnowska R & Wiczk W (2004) Fluorogenic peptide substrates for carboxydipeptidase activity of cathepsin B. Acta Biochim Pol 51, 81-92
55. Nagler D K, Storer A C, Portaro F C, Carmona E, Juliano L & Menard R (1997) Major increase in endopeptidase activity of human cathepsin B upon removal of occluding loop contacts. Biochemistry 36, 12608-12615
56. Blum J S, Fiani M L & Stahl P D (1991) Localization of cathepsin D in endosomes: characterization and biological importance. Adv Exp Med Biol 306, 281-287
57. Creemers L B, Hoeben K A, Jansen D C, Buttle D J, Beertsen W & Everts V (1998) Participation of intracellular cysteine proteinases, in particular cathepsin B, in degradation of collagen in periosteal tissue explants. Matrix Biol 16, 575-584
58. Almeida P C, Oliveira V, Chagas J R, Meldal M, Juliano M A & Juliano L (2000) Hydrolysis by cathepsin B of fluorescent peptides derived from human prorenin. Hypertension 35, 1278-1283
59. Shiba H, Uchida D, Kobayashi H & Natori M (2001) Involvement of cathepsin B- and L-like proteinases in silk gland histolysis during metamorphosis of Bombyx mori. Arch Biochem Biophys 390, 28-34
60. Raldua D, Fabra M, Bozzo M G, Weber E & Cerda J (2006) Cathepsin B-mediated yolk protein degradation during killifish oocyte maturation is blocked by an H+-ATPase inhibitor: effects on the hydration mechanism. Am J Physiol Regul Integr Comp Physiol 290, R 456-466
61. Shompole S & Jasmer D P (2001) Cathepsin B-like cysteine proteases confer intestinal cysteine protease activity in Haemonchus contortus. J Biol Chem 276, 2928-2934
62. Lindkvist B, Fajardo I, Pejler G & Borgstrom A (2006) Cathepsin B Activates Human Trypsinogen 1 but Not Proelastase 2 or Procarboxypeptidase B. Pancreatology 6, 224-231
63. Van Acker G J, Saluja A K, Bhagat L, Singh V P, Song A M & Steer M L (2002) Cathepsin B inhibition prevents trypsinogen activation and reduces pancreatitis severity. Am J Physiol Gastrointest Liver Physiol 283, G794-800
64. Ge J, Zhao G, Chen R, Li S, Wang S, Zhang X, Zhuang Y, Du J, Yu X, Li G & Yang Y (2006) Enhanced myocardial cathepsin B expression in patients with dilated cardiomyopathy. Eur J Heart Fail 8, 284-289
65. Baici A, Lang A, Zwicky R & Muntener K (2005) Cathepsin B in osteoarthritis: uncontrolled proteolysis in the wrong place. Semin Arthritis Rheum 34, 24-28
66. Ebert M P, Kruger S, Fogeron M L, Lamer S, Chen J, Pross M, Schulz H U, Lage H, Heim S, Roessner A, Malfertheiner P & Rocken C (2005) Overexpression of cathepsin B in gastric cancer identified by proteome analysis. Proteomics 5, 1693-1704
67. Wickramasinghe N S, Nagaraj N S, Vigneswaran N & Zacharias W (2005) Cathepsin B promotes both motility and invasiveness of oral carcinoma cells. Arch Biochem Biophys 436, 187-195
68. Guzinska-Ustymowicz K, Zalewski B, Kasacka I, Piotrowski Z & Skrzydlewska E (2004) Activity of cathepsin B and D in colorectal cancer: relationships with tumour budding. Anticancer Res 24, 2847-2851
69. Nishikawa H, Ozaki Y, Nakanishi T, Blomgren K, Tada T, Arakawa A & Suzumori K (2004) The role of cathepsin B and cystatin C in the mechanisms of invasion by ovarian cancer. Gynecol Oncol 92, 881-886
70. Podgorski I & Sloane B F (2003) Cathepsin B and its role(s) in cancer progression. Biochem Soc Symp 70, 263-276
71. Haraguchi C M, Ishido K, Kominami E & Yokota S (2003) Expression of cathepsin H in differentiating rat spermatids: immunoelectron microscopic study. Histochem Cell Biol 120, 63-71
72. Guncar G, Podobnik M, Pungercar J, Strukelj B, Turk V & Turk D (1998) 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 6, 51-61
73. Vasiljeva O, Dolinar M, Turk V & Turk B (2003) Recombinant human cathepsin H lacking the mini chain is an endopeptidase. Biochemistry 42, 13522-13528
74. Dodt J & Reichwein J (2003) Human cathepsin H: deletion of the mini-chain switches substrate specificity from aminopeptidase to endopeptidase. Biol Chem 384, 1327-1332
75. Horn M, Doleckova-Maresova L, Rulisek L, Masa M, Vasiljeva O, Turk B, Gan-Erdene T, Baudys M & Mares M (2005) Activation processing of cathepsin H impairs recognition by its propeptide. Biol Chem 386, 941-947
76. Brguljan P M, Turk V, Nina C, Brzin J, Krizaj I & Popovic T (2003) Human brain cathepsin H as a neuropeptide and bradykinin metabolizing enzyme. Peptides 24, 1977-1984
77. Brasch F, Ten Brinke A, Johnen G, Ochs M, Kapp N, Muller K M, Beers M F, Fehrenbach H, Richter J, Batenburg J J & 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
78. Chornaya V & Lyannaya O (2004) Some physicochemical properties of cathepsin H from human meningioma. Exp Oncol 26, 278-281
79. Schweiger A, Christensen I J, Nielsen H J, Sorensen S, Brunner N & Kos J (2004) Serum cathepsin H as a potential prognostic marker in patients with colorectal cancer. Int J Biol Markers 19, 289-294
80. Taubert H, Riemann D, Kehlen A, Meye A, Bartel F, John V, Brandt J, Bache M, Wurl P, Schmidt H & Weber E (2002) Expression of cathepsin B, D and L protein in juvenile idiopathic arthritis. Autoimmunity 35, 221-224
81. Waghray A, Keppler D, Sloane B F, Schuger L & Chen Y Q (2002) Analysis of a truncated form of cathepsin H in human prostate tumor cells. J Biol Chem 277, 11533-11538
82. Schweiger A, Staib A, Werle B, Krasovec M, Lah T T, Ebert W, Turk V & Kos J (2000) Cysteine proteinase cathepsin H in tumours and sera of lung cancer patients: relation to prognosis and cigarette smoking. Br J Cancer 82, 782-788
83. Ryvnyak V V, Ryvnyak E I & Tudos R V (2004) Electron histochemical localization of cathepsin L in the liver. Bull Exp Biol Med 137, 90-91
84. Robker R L, Russell D L, Espey L L, Lydon J P, O'Malley B W & Richards J S (2000) Progesterone-regulated genes in the ovulation process: ADAMTS-1 and cathepsin L proteases. Proc Natl Acad Sci (USA) 97, 4689-4694
85. Collins P R, Stack C M, O'Neill S M, Doyle S, Ryan T, Brennan G P, Mousley A, Stewart M, Maule A G, Dalton J P & Donnelly S (2004) Cathepsin L1, the major protease involved in liver fluke (Fasciola hepatica) virulence: propetide cleavage sites and autoactivation of the zymogen secreted from gastrodermal cells. J Biol Chem 279, 17038-17046
86. Lennon-Dumenil A M, Roberts R A, Valentijn K, Driessen C, Overkleeft H S, Erickson A, Peters P J, Bikoff E, Ploegh H L & Wolf Bryant P (2001) The p41 isoform of invariant chain is a chaperone for cathepsin L. Embo J 20, 4055-4064
87. Craft W W, Jr., Patch J & Dutch R E (2006) A mature and fusogenic form of the Nipah virus fusion protein requires proteolytic processing by cathepsin L. Virology 346, 251-257
88. Pager C T & Dutch R E (2005) Cathepsin L is involved in proteolytic processing of the Hendra virus fusion protein. J Virol 79, 12714-12720
89. Hsieh C S, deRoos P, Honey K, Beers C & Rudensky A Y (2002) A role for cathepsin L and cathepsin S in peptide generation for MHC class II presentation. J Immunol 168, 2618-2625
90. Yasothornsrikul S, Greenbaum D, Medzihradszky K F, Toneff T, Bundey R, Miller R, Schilling B, Petermann I, Dehnert J, Logvinova A, Goldsmith P, Neveu J M, Lane W S, Gibson B, Reinheckel T, Peters C, Bogyo M & Hook V (2003) Cathepsin L in secretory vesicles functions as a prohormone-processing enzyme for production of the enkephalin peptide neurotransmitter. Proc Natl Acad Sci (USA) 100, 9590-9595
91. Yoshiyama Y, Arai K, Oki T & Hattori T (2000) Expression of invariant chain and pro-cathepsin L in Alzheimer's brain. Neurosci Lett 290, 125-128
92. Kirschke H, Eerola R, Hopsu-Havu V K, Bromme D & Vuorio E (2000) Antisense RNA inhibition of cathepsin L expression reduces tumorigenicity of malignant cells. Eur J Cancer 36, 787-795
93. Nasu K, Kai K, Fujisawa K, Takai N, Nishida Y & Miyakawa I (2001) Expression of cathepsin L in normal endometrium and endometrial cancer. Eur J Obstet Gynecol Reprod Biol 99, 102-105
94. Niedergethmann M, Wostbrock B, Sturm J W, Willeke F, Post S & Hildenbrand R (2004) Prognostic impact of cysteine proteases cathepsin B and cathepsin L in pancreatic adenocarcinoma. Pancreas 29, 204-211
95. Bylaite M, Moussali H, Marciukaitiene I, Ruzicka T & Walz M (2006) Expression of cathepsin L and its inhibitor hurpin in inflammatory and neoplastic skin diseases. Exp Dermatol 15, 110-118
96. Wille A, Gerber A, Heimburg A, Reisenauer A, Peters C, Saftig P, Reinheckel T, Welte T & Buhling F (2004) Cathepsin L is involved in cathepsin D. processing and regulation of apoptosis in A549 human lung epithelial cells. Biol Chem 385, 665-670
97. Maehr R, Mintern J D, Herman A E, Lennon-Dumenil A M, Mathis D, Benoist C & Ploegh H L (2005) Cathepsin L is essential for onset of autoimmune diabetes in NOD mice. J Clin Invest 115, 2934-2943
98. Diment S, Leech M S & Stahl P D (1988) Cathepsin D is membrane-associated in macrophage endosomes. J Biol Chem 263, 6901-6907
99. Ryvnyak V V, Gudumak V S & Dulgieru O F (2003) Electron-histochemical location of cathepsin D and elastase in the uterus. Bull Exp Biol Med 136, 199-201
100. Hasilik A, von Figura K, Conzelmann E, Nehrkorn H & Sandhoff K (1982) Lysosomal enzyme precursors in human fibroblasts. Activation of cathepsin D precursor in vitro and activity of beta-hexosaminidase A precursor towards ganglioside GM2. Eur J Biochem 125, 317-321
101. Fusek M & Vetvicka V (2005) Dual role of cathepsin D: ligand and protease. Biomed Pap Med Fac Univ Palacky Olomouc Czech Repub 149, 43-50
102. Lkhider M, Castino R, Bouguyon E, Isidore C & Ollivier-Bousquet M (2004) Cathepsin D released by lactating rat mammary epithelial cells is involved in prolactin cleavage under physiological conditions. J Cell Sci 117, 5155-5164
103. Beaujouin M, Baghdiguian S, Glondu-Lassis M, Berchem G & Liaudet-Coopman E (2006) Overexpression of both catalytically active and -inactive cathepsin D by cancer cells enhances apoptosis-dependent chemo-sensitivity. Oncogene 25, 1967-1973
104. Bidere N, Lorenzo H K, Carmona S, Laforge M, Harper F, Dumont C & Senik A (2003) Cathepsin D triggers Bax activation, resulting in selective apoptosis-inducing factor (AIF) relocation in T lymphocytes entering the early commitment phase to apoptosis. J Biol Chem 278, 31401-31411
105. Kirschke H, Barrett A J & Rawlings N D (1995) Proteinases 1: lysosomal cysteine proteinases. Protein Profile 2, 1581-1643
106. Kirschke H & Wiederanders B (1994) Cathepsin S and related lysosomal endopeptidases. Methods Enzymol 244, 500-511
107. Shi G P, Munger J S, Meara J P, Rich D H & Chapman H A (1992) Molecular cloning and expression of human alveolar macrophage cathepsin S, an elastinolytic cysteine protease. J Biol Chem 267, 7258-7262
108. Cheng X W, Kuzuya M, Nakamura K, Di Q, Liu Z, Sasaki T, Kanda S, Jin H, Shi G P, Murohara T, Yokota M & Iguchi A (2006) Localization of cysteine protease, cathepsin S, to the surface of vascular smooth muscle cells by association with integrin alphanubeta3. Am J Pathol 168, 685-694
109. Shi G P, Webb A C, Foster K E, Knoll J H, Lemere C A, Munger J S & Chapman H A (1994) Human cathepsin S: chromosomal localization, gene structure, and tissue distribution. J Biol Chem 269, 11530-11536
110. Liuzzo J P, Petanceska S S & Devi L A (1999) Neurotrophic factors regulate cathepsin S in macrophages and microglia: A role in the degradation of myelin basic protein and amyloid beta peptide. Mol Med 5, 334-343
111. Driessen C, Bryant R A, Lennon-Dumenil A M, Villadangos J A, Bryant P W, Shi G P, Chapman H A & Ploegh H L (1999) Cathepsin S controls the trafficking and maturation of MHC class II molecules in dendritic cells. J Cell Biol 147, 775-790
112. Liu W & Spero D M (2004) Cysteine protease cathepsin S as a key step in antigen presentation. Drug News Perspect 17, 357-363
113. Beers C, Burich A, Kleijmeer M J, Griffith J M, Wong P & Rudensky A Y (2005) Cathepsin S controls MHC class II-mediated antigen presentation by epithelial cells in vivo. J Immunol 174, 1205-1212
114. Boes M, van der Wel N, Peperzak V, Kim Y M, Peters P J & Ploegh H (2005) In vivo control of endosomal architecture by class Il-associated invariant chain and cathepsin S. Eur J Immunol 35, 2552-2562
115. Shi G P, Sukhova G K, Kuzuya M, Ye Q, Du J, Zhang Y, Pan J H, Lu M L, Cheng X W, Iguchi A, Perrey S, Lee A M, Chapman H A & Libby P (2003) Deficiency of the cysteine protease cathepsin S impairs microvessel growth. Circ Res 92, 493-500
116. Wang B, Sun J, Kitamoto S, Yang M, Grubb A, Chapman H A, Kalluri R & Shi G P (2006) Cathepsin S controls angiogenesis and tumor growth via matrix-derived angiogenic factors. J Biol Chem 281, 6020-6029
117. Beck H, Schwarz G, Schroter C J, Deeg M, Baier D, Stevanovic S, Weber E, Driessen C & Kalbacher H (2001) Cathepsin S and an asparagine-specific endoprotease dominate the proteolytic processing of human myelin basic protein in vitro. Eur J Immunol 31, 3726-3736
118. Liu J, Ma L, Yang J, Ren A, Sun Z, Yan G, Sun J, Fu H, Xu W, Hu C & Shi G P (2005) Increased serum cathepsin S in patients with atherosclerosis and diabetes. Atherosclerosis 186, 411-419
119. Flannery T, McQuaid S, McGoohan C, McConnell R S, McGregor G, Mirakhur M, Hamilton P, Diamond J, Cran G, Walker B, Scott C, Martin L, Ellison D, Patel C, Nicholson C, Mendelow D, McCormick D & Johnston P G (2006) Cathepsin S expression: An independent prognostic factor in glioblastoma tumours-a pilot study. Int J Cancer 119, 854-860
120. Saegusa K, Ishimaru N, Yanagi K, Arakaki R, Ogawa K, Saito I, Katunuma N & Hayashi Y (2002) Cathepsin S inhibitor prevents autoantigen presentation and autoimmunity. J Clin Invest 110, 361-369
121. Tezuka K, Tezuka Y, Maejima A, Sato T, Neraoto K, Kamioka H, Hakeda Y & Kumegawa M (1994) Molecular cloning of a possible cysteine proteinase predominantly expressed in osteoclasts. J Biol Chem 269, 1106-1109
122. Inaoka T, Bilbe G, Ishibashi O, Tezuka K, Kumegawa M & Kokubo T (1995) Molecular cloning of human cDNA for cathepsin K: novel cysteine proteinase predominantly expressed in bone. Biochem Biophys Res Commun 206, 89-96
123. Buhling F, Gerber A, Hackel C, Kruger S, Kohnlein T, Bromme D, Reinhold D, Ansorge S & Welte T (1999) Expression of cathepsin K in lung epithelial cells. Am J Respir Cell Mol Biol 20, 612-619
124. Mandelin J, Hukkanen M, Li T F, Korhonen M, Liljestrom M, Sillat T, Hanemaaijer R, Salo J, Santavirta S & Konttinen Y T (2005) Human osteoblasts produce cathepsin K. Bone 38,769-777
125. Dodds R A (2003) A cytochemical assay for osteoclast cathepsin K activity. Cell Biochem Fund 21, 231-234
126. Kafienah W, Bromme D, Buttle D J, Croucher L J & Hollander A P (1998) Human cathepsin K cleaves native type I and II collagens at the N-terminal end of the triple helix. Biochem J 331, 727-732
127. Buhling F, Waldburg N, Gerber A, Hackel C, Kruger S, Reinhold D, Bromme D, Weber E, Ansorge S & Welte T (2000) Cathepsin K expression in human lung. Adv Exp Med Biol 477,281-286
128. Atley L M, Mort J S, Lalumiere M & Eyre D R (2000) Proteolysis of human bone collagen by cathepsin K: characterization of the cleavage sites generating by cross-linked N-telopeptide neoepitope. Bone 26, 241-247
129. Buhling F, Rocken C, Brasch F, Hartig R, Yasuda Y, Saftig P, Bromme D & Welte T (2004) Pivotal role of cathepsin K in lung fibrosis. Am J Pathol 164, 2203-2216
130. Troen B R (2004) The role of cathepsin K in normal bone resorption. Drug News Perspect 17,19-28
131. Motyckova G & Fisher D E (2002) Pycnodysostosis: role and regulation of cathepsin K in osteoclast function and human disease. Curr Mol Med 2,407-421
132. Everts V, Hou W S, Rialland X, Tigchelaar W, Saftig P, Bromme D, Gelb B D & Beertsen W (2003) Cathepsin K deficiency in pycnodysostosis results in accumulation of non-digested phagocytosed collagen in fibroblasts. Calcif Tissue Int 73, 380-386
133. Godat E, Lecaille F, Desmazes C, Duchene S, Weidauer E, Saftig P, Bromme D, Vandier C & Lalmanach G (2004) Cathepsin K: a cysteine protease with unique kinin-degrading properties. Biochem J 383, 501-506
134. Lutgens E, Lutgens S P, Faber B C, Heeneman S, Gijbels M M, de Winther M P, Frederik P, van der Made I, Daugherty A, Sijbers A M, Fisher A, Long C J, Saftig P, Black D, Daemen M J & Cleutjens K B (2006) Disruption of the cathepsin K gene reduces atherosclerosis progression and induces plaque fibrosis but accelerates macrophage foam cell formation. Circulation 113, 98-107
135. Morko J P, Soderstrom M, Saamanen A M, Salminen H J & Vuorio EI (2004) Up regulation of cathepsin K expression in articular chondrocytes in a transgenic mouse model for osteoarthritis. Ann Rheum Dis 63, 649-655
136. Deaton D N & Kumar S (2004) 6. Cathepsin K inhibitors: their potential as anti-osteoporosis agents. Prog Med Chem 42,245-375
137. Wang D, Li W, Pechar M, Kopeckova P, Bromme D & Kopecek J (2004) Cathepsin K inhibitor-polymer conjugates: potential drugs for the treatment of osteoporosis and rheumatoid arthritis. Int J Pharm 211, 13-19
138. Lindeman J H, Hanemaaijer R, Mulder A, Dijkstra P D, Szuhai K, Bromme D, Verheijen J H & Hogendoorn P C (2004) Cathepsin K is the principal protease in giant cell tumor of bone. Am J Pathol 165, 593-600
139. McGuire M J, Lipsky P E & Thiele D L (1997) Cloning and characterization of the cDNA encoding mouse dipeptidyl peptidase I (cathepsin C). Biochim Biophys Acta 1351, 267-273
140. Sastradipura D F, Nakanishi H, Tsukuba T, Nishishita K, Sakai H, Kato Y, Gotow T, Uchiyama Y & Yamamoto K (1998) Identification of cellular compartments involved in processing of cathepsin E in primary cultures of rat microglia. J Neurochem 70, 2045-2056
141. Chain B M, Free P, Medd P, Swetman C, Tabor A B & Terrazzini N (2005) The expression and function of cathepsin E in dendritic cells. J Immunol 174, 1791-1800
142. Athauda S B & Takahashi K (2002) Distinct cleavage specificity of human cathepsin E at neutral pH with special preference for Arg-Arg bonds. Protein Pept Lett 9, 15-22
143. Santamaria I, Velasco G, Pendas A M, Paz A & Lopez-Otin C (1999) Molecular cloning and structural and functional characterization of human cathepsin F, a new cysteine proteinase of the papain family with a long propeptide domain. J Biol Chem 274, 13800-13809
144. Wang B, Shi G P, Yao P M, Li Z, Chapman H A & Bromme D (1998) Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization. J Biol Chem 273, 32000-32008
145. Tisljar K, Deussing J & Peters C (1999) Cathepsin J, a novel murine cysteine protease of the papain family with a placenta-restricted expression. FEBS Lett 459, 299-304
146. Bode S, Peters C & Deussing J M (2005) Placental cathepsin M is alternatively spliced and exclusively expressed in the spongiotrophoblast layer. Biochim Biophys Acta 1731, 160-167
147. Santamaria I, Pendas A M, Velasco G & Lopez-Otin C (1998) Genomic structure and chromosomal localization of the human cathepsin O gene (CTSO). Genomics 53,231-234
148. Sol-Church K, Frenck J & Mason R W (2000) Cathepsin Q, a novel lysosomal cysteine protease highly expressed in placenta. Biochem Biophys Res Commun 267, 791-795
149. Bromme D, Li Z, Barnes M & Mehler E (1999) Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization. Biochemistry 38, 2377-2385
150. Tolosa E, Li W, Yasuda Y, Wienhold W, Denzin L K, Lautwein A, Driessen C, Schnorrer P, Weber E, Stevanovic S, Kurek R, Melms A & Bromme D (2003) Cathepsin V is involved in the degradation of invariant chain in human thymus and is overexpressed in myasthenia gravis. J Clin Invest 112, 517-526
151. Ondr J K & Pham C T (2004) Characterization of murine cathepsin W and its role in cell-mediated cytotoxicity. J Biol Chem 279, 27525-27533
152. Wex T, Levy B, Smeekens S P, Ansorge S, Desnick R J & Bromine D (1998) Genomic structure, chromosomal localization, and expression of human cathepsin W. Biochem Biophys Res Commun 248, 255-261
153. Klemencic I, Carmona A K, Cezari M H, Juliano M A, Juliano L, Guncar G, Turk D, Krizaj I, Turk V & Turk B (2000) Biochemical characterization of human cathepsin X revealed that the enzyme is an exopeptidase, acting as carboxymonopeptidase or carboxydipeptidase. Eur J Biochem 267, 5404-5412
154. Guncar G, Klemencic I, Turk B, Turk V, Karaoglanovic-Carmona A, Juliano L & Turk D (2000) Crystal structure of cathepsin X: a flip-flop of the ring of His23 allows carboxy-monopeptidase and carboxy-dipeptidase activity of the protease. Structure 8, 305-313
155. Turk D, Podobnik M, Kuhelj R, Dolinar M & Turk V (1996) Crystal structures of human procathepsin B at 3.2 and 3.3 Angstroms resolution reveal an interaction motif between a papain-like cysteine protease and its propeptide. FEBS Lett 384, 211-214
156. Greenspan P D, Clark K L, Tommasi R A, Cowen S D, McQuire L W, Farley D L, van Duzer J H, Goldberg R L, Zhou H, Du Z, Fitt J J, Coppa D E, Fang Z, Macchia W, Zhu L, Capparelli M P, Goldstein R, Wigg A M, Doughty J R, Bohacek R S & Knap A K (2001) Identification of dipeptidyl nitriles as potent and selective inhibitors of cathepsin B through structure-based drug design. J Med Chem 44, 4524-4534
157. Baldwin E T, Bhat T N, Gulnik S, Hosur M V, Sowder R C, 2nd, Cachau R E, Collins J, Silva A M & Erickson J W (1993) Crystal structures of native and inhibited forms of human cathepsin D: implications for lysosomal targeting and drug design. Proc Natl Acad Sci (USA) 90, 6796-6800