Degradation of type I collagen and pathogenesis of infectious diseases

Type I Collagen: Biological Functions, Synthesis and Medicinal Applications

Volumn , Issue , 2012, Pages 45-70

  Motta, Flávia Nader ^a   Azevedo, Clênia ^a   de Araújo, Carla Nunes ^a   Santana, Jaime M ^a   Bastos, Izabela M D ^a  

^a UNIVERSITY OF BRASILIA   (Brazil)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 84895408486     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter

References (172)

1. Abad, A., Fernández-Molina, J. V., Bikandi, J., Ramírez, A., Margareto, J., Sendino, J., Hernando, F. L., Pontón, J., Garaizar, J., and Rementeria, A. (2010). What makes Aspergillus fumigatus a successful pathogen? Genes and molecules involved in invasive aspergillosis. Rev. Iberoam. Micol. 27, 155-182.
2. Abrahamson, D. R. (1986). Recent studies on the structure and pathology of basement membranes. J. Pathol. 149, 257-278.
3. Ahsan, M. M., Kimura, T., Karita, S., Sakka, K., and Ohmiya, K. (1996). Cloning, D. N. A. sequencing, and expression of the gene encoding Clostridium thermocellum cellulase CelJ, the largest catalytic component of the cellulosome. J. Bacteriol. 178, 5732-5740.
4. Andrews, S. J. (1999). The life cicle of Fasciola hepatica. Oxford, U. K.: C. A. B. I. edn.
5. Ankri, S., Stolarsky, T., Bracha, R., Padilla-Vaca, F., and Mirelman, D. (1999). Antisense inhibition of expression of cysteine proteinases affects Entamoeba histolytica-induced formation of liver abscess in hamsters. Infect. Immun. 67, 421-422.
6. Arhets, P., Olivo, J. C., Gounon, P., Sansonetti, P., and Guillén, N. (1998). Virulence and functions of myosin II are inhibited by overexpression of light meromyosin in Entamoeba histolytica. Mol. Biol. Cell 9, 1537-1547.
7. Armstrong, D. G., and Jude, E. B. (2002). The role of matrix metalloproteinases in wound healing. J. Am. Podiatr. Med. Assoc. 92, 12-18.
8. Arnold, L. H., Butt, L. E., Prior, S. H., Read, C. M., Fields, G. B., and Pickford, A. R. (2011). The interface between catalytic and hemopexin domains in matrix metalloproteinase-1 conceals a collagen binding exosite. J. Biol. Chem. 286, 45073-45082.
9. Atley, L. M., Mort, J. S., Lalumiere, M., and 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.
10. Balloy, V., and Chignard, M. (2009). The innate immune response to Aspergillus fumigatus. Microbes Infect. 11, 919-927.
11. Baronas-Lowell, D., Lauer-Fields, J. L., and Fields, G. B. (2004). Induction of endothelial cell activation by a triple helical alpha2beta integrin ligand, derived from type I collagen alpha1(I)496-507. J. Biol. Chem. 279, 952-962.
12. Bastos, I. M., Grellier, P., Martins, N. F., Cadavid-Restrepo, G., de Souza-Ault, M. R., Augustyns, K., Teixeira, A. R., Schrével, J., Maigret, B., da Silveira, J. F., et al. (2005). Molecular, functional and structural properties of the prolyl oligopeptidase of Trypanosoma cruzi (POP Tc80), which is required for parasite entry into mammalian cells. Biochem. J. 388, 29-38.
13. Bastos, I. M., Motta, F. N., Charneau, S., Santana, J. M., Dubost, L., Augustyns, K., and Grellier, P. (2010). Prolyl oligopeptidase of Trypanosoma brucei hydrolyzes native collagen, peptide hormones and is active in the plasma of infected mice. Microbes Infect. 12, 457-466.
14. Bauvois, B., Sancéau, J., and Wietzerbin, J. (1992). Human U937 cell surface peptidase activities: characterization and degradative effect on tumor necrosis factor-alpha. Eur. J. Immunol. 22, 923-930.
15. Beauvais, A., Monod, M., Debeaupuis, J. P., Diaquin, M., Kobayashi, H., and Latgé, J. P. (1997a). Biochemical and antigenic characterization of a new dipeptidyl-peptidase isolated from Aspergillus fumigatus. J. Biol. Chem. 272, 6238-6244.
16. Beauvais, A., Monod, M., Wyniger, J., Debeaupuis, J. P., Grouzmann, E., Brakch, N., Svab, J., Hovanessian, A. G., and Latgé, J. P. (1997b). Dipeptidyl-peptidase IV secreted by Aspergillus fumigatus, a fungus pathogenic to humans. Infect Immun. 65, 3042-3047.
17. Beck, D. L., Dogan, N., Maro, V., Sam, N. E., Shao, J., and Houpt, E. R. (2008). High prevalence of Entamoeba moshkovskii in a Tanzanian H. I. V. population. Acta Trop. 107, 48-49.
18. Beecher, D. J., Olsen, T. W., Somers, E. B., and Wong, A. C. (2000). Evidence for contribution of tripartite hemolysin B. L., phosphatidylcholine-preferring phospholipase C, and collagenase to virulence of Bacillus cereus endophthalmitis. Infect Immun. 68, 5269-5276.
19. Behnsen, J., Lessing, F., Schindler, S., Wartenberg, D., Jacobsen, I. D., Thoen, M., Zipfel, P. F., and Brakhage, A. A. (2010). Secreted Aspergillus fumigatus protease Alp1 degrades human complement proteins C3, C4, and C5. Infect Immun. 78, 3585-3594.
20. Bejarano, P. A., Langeveld, J. P., Hudson, B. G., and Noelken, M. E. (1989). Degradation of basement membranes by Pseudomonas aeruginosa elastase. Infect Immun. 57, 3783-3787.
21. Berasain, P., Carmona, C., Frangione, B., Dalton, J. P., and Goñi, F. (2000). Fasciola hepatica: parasite-secreted proteinases degrade all human IgG subclasses: determination of the specific cleavage sites and identification of the immunoglobulin fragments produced. Exp. Parasitol. 94, 99-110.
22. Berman, E. (1991). Biochemistry of the eye. New York, N. Y.: Plenum Press.
23. Bertini, I., Fragai, M., Luchinat, C., Melikian, M., Toccafondi, M., Lauer, J. L., and Fields, G. B. (2012). Structural basis for matrix metalloproteinase 1-catalyzed collagenolysis. J. Am. Chem. Soc. 134, 2100-2110.
24. Bidwell, E., and Van Heyningen, W. E. (1948). The biochemistry of the gas gangrene toxins; the kappa-toxin, collagenase, of Clostridium welchii. Biochem. J. 42, 140-151.
25. Birkedal-Hansen, H., Moore, W. G., Bodden, M. K., Windsor, L. J., Birkedal-Hansen, B., DeCarlo, A., and Engler, J. A. (1993). Matrix metalloproteinases: a review. Crit. Rev. Oral. Biol. Med. 4, 197-250.
26. Blackwood, L. L., Stone, R. M., Iglewski, B. H., and Pennington, J. E. (1983). Evaluation of Pseudomonas aeruginosa exotoxin A and elastase as virulence factors in acute lung infection. Infect Immun. 39, 198-201.
27. Bodey, G. P., Bolivar, R., Fainstein, V., and Jadeja, L. (1983). Infections caused by Pseudomonas aeruginosa. Rev. Infect. Dis. 5, 279-313.
28. Bond, M. D., and Van Wart, H. E. (1984). Purification and separation of individual collagenases of Clostridium histolyticum using red dye ligand chromatography. Biochemistry 23, 3077-3085.
29. Bottone, E. J. (2010). Bacillus cereus, a volatile human pathogen. Clin. Microbiol. Rev. 23, 382-398.
30. Brodsky, B., and Persikov, A. V. (2005). Molecular structure of the collagen triple helix. Adv. Protein. Chem. 70, 301-339.
31. Bruchhaus, I., Jacobs, T., Leippe, M., and Tannich, E. (1996). Entamoeba histolytica and Entamoeba dispar: differences in numbers and expression of cysteine proteinase genes. Mol. Microbiol. 22, 255-263.
32. Burleigh, B. A., and Woolsey, A. M. (2002). Cell signalling and Trypanosoma cruzi invasion. Cell Microbiol. 4, 701-711.
33. Bycroft, M., Bateman, A., Clarke, J., Hamill, S. J., Sandford, R., Thomas, R. L., and Chothia, C. (1999). The structure of a P. K. D. domain from polycystin-1: implications for polycystic kidney disease. E. M. B. O. J. 18, 297-305.
34. Callegan, M. C., Booth, M. C., Jett, B. D., and Gilmore, M. S. (1999). Pathogenesis of gram-positive bacterial endophthalmitis. Infect Immun. 67, 3348-3356.
35. Camargo, A. C., Caldo, H., and Reis, M. L. (1979). Susceptibility of a peptide derived from bradykinin to hydrolysis by brain endo-oligopeptidases and pancreatic proteinases. J. Biol. Chem. 254, 5304-5307.
36. Chapman, J. A., Tzaphlidou, M., Meek, K. M., and Kadler, K. E. (1990). The collagen fibril--a model system for studying the staining and fixation of a protein. Electron Microsc. Rev. 3, 143-182.
37. Chen, X. L., Zhang, Y. Z., Lu, J. T., Xie, B. B., Sun, C. Y., and Guo, B. (2007). Autolysis of a novel multidomain subtilase-cold-adapted deseasin MCP-01 is pH-dependent and the surface loops in its catalytic domain, the linker, and the P_proprotein domain are susceptible to proteolytic attack. Biochem. Biophys. Res. Commun. 358, 704-709.
38. Cheng, H. C., Abdel-Ghany, M., Elble, R. C., and Pauli, B. U. (1998). Lung endothelial dipeptidyl peptidase IV promotes adhesion and metastasis of rat breast cancer cells via tumor cell surface-associated fibronectin. J. Biol. Chem. 273, 24207-24215.
39. Chung, L., Dinakarpandian, D., Yoshida, N., Lauer-Fields, J. L., Fields, G. B., Visse, R., and Nagase, H. (2004). Collagenase unwinds triple-helical collagen prior to peptide bond hydrolysis. E. M. B. O. J. 23, 3020-3030.
40. Clark, C. G., Alsmark, U. C., Tazreiter, M., Saito-Nakano, Y., Ali, V., Marion, S., Weber, C., Mukherjee, C., Bruchhaus, I., Tannich, E., et al. (2007). Structure and content of the Entamoeba histolytica genome. Adv. Parasitol. 65, 51-190.
41. Clark, I. M., and Cawston, T. E. (1989). Fragments of human fibroblast collagenase. Purification and characterization. Biochem. J. 263, 201-206.
42. Coudrier, E., Amblard, F., Zimmer, C., Roux, P., Olivo-Marin, J. C., Rigothier, M. C., and Guillén, N. (2005). Myosin II and the Gal-GalNAc lectin play a crucial role in tissue invasion by Entamoeba histolytica. Cell Microbiol. 7, 19-27.
43. Dalton, J. P., Neill, S. O., Stack, C., Collins, P., Walshe, A., Sekiya, M., Doyle, S., Mulcahy, G., Hoyle, D., Khaznadji, E., et al. (2003). Fasciola hepatica cathepsin L-like proteases: biology, function, and potential in the development of first generation liver fluke vaccines. Int. J. Parasitol. 33, 1173-1181.
44. Das, S., Mandal, M., Chakraborti, T., Mandal, A., and Chakraborti, S. (2003). Structure and evolutionary aspects of matrix metalloproteinases: a brief overview. Mol. Cell Biochem. 253, 31-40.
45. Davey, R. T., and Tauber, W. B. (1987). Posttraumatic endophthalmitis: the emerging role of Bacillus cereus infection. Rev. Infect Dis. 9, 110-123.
46. Di Lullo, G. A., Sweeney, S. M., Korkko, J., Ala-Kokko, L., and San Antonio, J. D. (2002). Mapping the ligand-binding sites and disease-associated mutations on the most abundant protein in the human, type I collagen. J. Biol. Chem. 277, 4223-4231.
47. Diacovich, L., and Gorvel, J. P. (2010). Bacterial manipulation of innate immunity to promote infection. Nat. Rev. Microbiol. 8, 117-128.
48. Docherty, A. J., and Murphy, G. (1990). The tissue metalloproteinase family and the inhibitor T. I. M. P.: a study using cDNAs and recombinant proteins. Ann. Rheum. Dis. 49 Suppl. 1, 469-479.
49. Dresdner, K., Barker, L. A., Orlowski, M., and Wilk, S. (1982). Subcellular distribution of prolyl endopeptidase and cation-sensitive neutral endopeptidase in rabbit brain. J. Neurochem. 38, 1151-1154.
50. Ducka, P., Eckhard, U., Schönauer, E., Kofler, S., Gottschalk, G., Brandstetter, H., and Nüss, D. (2009). A universal strategy for high-yield production of soluble and functional clostridial collagenases in E. coli. Appl. Microbiol. Biotechnol. 83, 1055-1065.
51. Döring, G., Maier, M., Müller, E., Bibi, Z., Tümmler, B., and Kharazmi, A. (1987). Virulence factors of Pseudomonas aeruginosa. Antibiot. Chemother. 39, 136-148.
52. Eckhard, U., Schönauer, E., Ducka, P., Briza, P., Nüss, D., and Brandstetter, H. (2009). Biochemical characterization of the catalytic domains of three different Clostridial collagenases. Biol. Chem. 390, 11-18.
53. Eckhard, U., Schönauer, E., Nüss, D., and Brandstetter, H. (2011). Structure of collagenase G. reveals a chew-and-digest mechanism of bacterial collagenolysis. Nat. Struct. Mol. Biol. 18, 1109-1114.
54. Engman, D. M., and Leon, J. S. (2002). Pathogenesis of Chagas heart disease: role of autoimmunity. Acta Trop. 81, 123-132.
55. Fotedar, R., Stark, D., Marriott, D., Ellis, J., and Harkness, J. (2008). Entamoeba moshkovskii infections in Sydney, Australia. Eur. J. Clin. Microbiol. Infect. Dis. 27, 133-137.
56. French, M. F., Bhown, A., and Van Wart, H. E. (1992). Identification of Clostridium histolyticum collagenase hyperreactive sites in type I, II, and III collagens: lack of correlation with local triple helical stability. J. Protein. Chem. 11, 83-97.
57. French, M. F., Mookhtiar, K. A., and Van Wart, H. E. (1987). Limited proteolysis of type I collagen at hyperreactive sites by class I and II Clostridium histolyticum collagenases: complementary digestion patterns. Biochemistry 26, 681-687.
58. Fülöp, V., Böcskei, Z., and Polgár, L. (1998). Prolyl oligopeptidase: an unusual beta-propeller domain regulates proteolysis. Cell 94, 161-170.
59. Garcia, M. P., Nóbrega, O. T., Teixeira, A. R., Sousa, M. V., and Santana, J. M. (1998). Characterisation of a Trypanosoma cruzi acidic 30 kDa cysteine protease. Mol. Biochem. Parasitol. 91, 263-272.
60. Gelbard, M. K., James, K., Riach, P., and Dorey, F. (1993). Collagenase versus placebo in the treatment of Peyronie's disease: a double-blind study. J. Urol. 149, 56-58.
61. Geurts, N., Opdenakker, G., and Van den Steen, P. E. (2012). Matrix metalloproteinases as therapeutic targets in protozoan parasitic infections. Pharmacol. Ther. 133, 257-279.
62. Goodwin, L. G. (1971). Pathological effects of Trypanosoma brucei on small blood vessels in rabbit ear-chambers. Trans. R. Soc. Trop. Med. Hyg. 65, 82-88.
63. Grab, D. J., Garcia-Garcia, J. C., Nikolskaia, O. V., Kim, Y. V., Brown, A., Pardo, C. A., Zhang, Y., Becker, K. G., Wilson, B. A., de A Lima, A. P., et al. (2009). Protease activated receptor signaling is required for African trypanosome traversal of human brain microvascular endothelial cells. PLoS Negl. Trop. Dis. 3, e479.
64. Granum, P. E. (1994). Bacillus cereus and its toxins. Soc. Appl. Bacteriol. Symp. Ser. 23, 61S-66S.
65. Granum, P. E., and Lund, T. (1997). Bacillus cereus and its food poisoning toxins. F. E. M. S. Microbiol. Lett. 157, 223-228.
66. Grellier, P., Vendeville, S., Joyeau, R., Bastos, I. M., Drobecq, H., Frappier, F., Teixeira, A. R., Schrével, J., Davioud-Charvet, E., Sergheraert, C., et al. (2001). Trypanosoma cruzi prolyl oligopeptidase Tc80 is involved in nonphagocytic mammalian cell invasion by trypomastigotes. J. Biol. Chem. 276, 47078-47086.
67. Haque, R., Huston, C. D., Hughes, M., Houpt, E., and Petri, W. A. (2003). Amebiasis. N. Engl. J. Med. 348, 1565-1573.
68. Heck, L. W., Morihara, K., McRae, W. B., and Miller, E. J. (1986). Specific cleavage of human type III and IV collagens by Pseudomonas aeruginosa elastase. Infect Immun. 51, 115-118.
69. Hergenrother, P. J., and Martin, S. F. (1997). Determination of the kinetic parameters for phospholipase C. (Bacillus cereus) on different phospholipid substrates using a chromogenic assay based on the quantitation of inorganic phosphate. Anal. Biochem. 251, 45-49.
70. Hesse, F., Burtscher, H., Popp, F., and Ambrosius, D. (1995). Recombinant enzymes for islet isolation: purification of a collagenase from Clostridium histolyticum and cloning/expression of the gene. Transplant. Proc. 27, 3287-3289.
71. Hou, Y., Mortimer, L., and Chadee, K. (2010). Entamoeba histolytica cysteine proteinase 5 binds integrin on colonic cells and stimulates NFkappaB-mediated pro-inflammatory responses. J. Biol. Chem. 285, 35497-35504.
72. Hublart, M., Lagouche, L., Racadot, A., Boersma, A., Degand, P., Noireau, F., Lemesre, J. L., and Toudic, A. (1988). Endocrine function and African trypanosomiasis. Evaluation of 79 cases. Bull. Soc. Pathol. Exot. Filiales. 81, 468-476.
73. Hurst, D. R., Schwartz, M. A., Ghaffari, M. A., Jin, Y., Tschesche, H., Fields, G. B., and Sang, Q. X. (2004). Catalytic- and ecto-domains of membrane type 1-matrix metalloproteinase have similar inhibition profiles but distinct endopeptidase activities. Biochem. J. 377, 775-779.
74. Irving, J. A., Spithill, T. W., Pike, R. N., Whisstock, J. C., and Smooker, P. M. (2003). The evolution of enzyme specificity in Fasciola spp. J. Mol. Evol. 57, 1-15.
75. Jensen, G. B., Hansen, B. M., Eilenberg, J., and Mahillon, J. (2003). The hidden lifestyles of Bacillus cereus and relatives. Environ. Microbiol. 5, 631-640.
76. Kadler, K. E., Holmes, D. F., Trotter, J. A., and Chapman, J. A. (1996). Collagen fibril formation. Biochem. J. 316 (Pt 1), 1-11.
77. Kafienah, W., Brömme, D., Buttle, D. J., Croucher, L. J., and 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 (Pt 3), 727-732.
78. Katayama, S., Dupuy, B., Daube, G., China, B., and Cole, S. T. (1996). Genome mapping of Clostridium perfringens strains with I-CeuI shows many virulence genes to be plasmid-borne. Mol. Gen. Genet. 251, 720-726.
79. Keene, W. E., Petitt, M. G., Allen, S., and McKerrow, J. H. (1986). The major neutral proteinase of Entamoeba histolytica. J. Exp. Med. 163, 536-549.
80. Keiser, J., and Utzinger, J. (2005). Emerging foodborne trematodiasis. Emerg. Infect. Dis. 11, 1507-1514.
81. Khairnar, K., Parija, S. C., and Palaniappan, R. (2007). Diagnosis of intestinal amoebiasis by using nested polymerase chain reaction-restriction fragment length polymorphism assay. J Gastroenterol 42, 631-640.
82. Knäuper, V., Osthues, A., DeClerck, Y. A., Langley, K. E., Bläser, J., and Tschesche, H. (1993). Fragmentation of human polymorphonuclear-leucocyte collagenase. Biochem. J. 291 (Pt 3), 847-854.
83. Kolattukudy, P. E., Lee, J. D., Rogers, L. M., Zimmerman, P., Ceselski, S., Fox, B., Stein, B., and Copelan, E. A. (1993). Evidence for possible involvement of an elastolytic serine protease in aspergillosis. Infect Immun. 61, 2357-2368.
84. Kurup, V. P., and Grunig, G. (2002). Animal models of allergic bronchopulmonary aspergillosis. Mycopathologia 153, 165-177.
85. Labruyère, E., Zimmer, C., Galy, V., Olivo-Marin, J. C., and Guillén, N. (2003). EhPAK, a member of the p21-activated kinase family, is involved in the control of Entamoeba histolytica migration and phagocytosis. J. Cell Sci. 116, 61-71.
86. Landis, B. N., Grouzmann, E., Monod, M., Busso, N., Petak, F., Spiliopoulos, A., Robert, J. H., Szalay-Quinodoz, I., Morel, D. R., and Lacroix, J. S. (2008). Implication of dipeptidylpeptidase IV activity in human bronchial inflammation and in bronchoconstriction evaluated in anesthetized rabbits. Respiration 75, 89-97.
87. Lauer-Fields, J. L., Chalmers, M. J., Busby, S. A., Minond, D., Griffin, P. R., and Fields, G. B. (2009). Identification of specific hemopexin-like domain residues that facilitate matrix metalloproteinase collagenolytic activity. J. Biol. Chem. 284, 24017-24024.
88. Leikina, E., Mertts, M. V., Kuznetsova, N., and Leikin, S. (2002). Type I collagen is thermally unstable at body temperature. Proc. Natl. Acad. Sci. US 99, 1314-1318.
89. Lemichez, E., Lecuit, M., Nassif, X., and Bourdoulous, S. (2010). Breaking the wall: targeting of the endothelium by pathogenic bacteria. Nat. Rev. Microbiol. 8, 93-104.
90. Lund, T., De Buyser, M. L., and Granum, P. E. (2000). A new cytotoxin from Bacillus cereus that may cause necrotic enteritis. Mol. Microbiol. 38, 254-261.
91. Lund, T., and Granum, P. E. (1999). The 105-kDa protein component of Bacillus cereus non-haemolytic enterotoxin (Nhe) is a metalloprotease with gelatinolytic and collagenolytic activity. F. E. M. S. Microbiol. Lett. 178, 355-361.
92. Löster, K., Zeilinger, K., Schuppan, D., and Reutter, W. (1995). The cysteine-rich region of dipeptidyl peptidase IV (CD 26) is the collagen-binding site. Biochem. Biophys. Res. Commun. 217, 341-348.
93. MacLennan, J. D. (1962). The histotoxic clostridial infections of man. Bacteriol. Rev. 26, 177-276.
94. MacLennan, J. D., Mandl, I., and Howes, E. L. (1953). Bacterial digestion of collagen. J. Clin. Invest. 32, 1317-1322.
95. Martinez, M. F., Haines, T., Waller, M., Tingey, D., and Gomez, W. (2007). Probable occupational endophthalmitis from Bacillus cereus. Arch. Environ. Occup. Health 62, 157-160.
96. Maschmeyer, G., Haas, A., and Cornely, O. A. (2007). Invasive aspergillosis: epidemiology, diagnosis and management in immunocompromised patients. Drugs 67, 1567-1601.
97. Matsushita, O., Yoshihara, K., Katayama, S., Minami, J., and Okabe, A. (1994). Purification and characterization of Clostridium perfringens 120-kilodalton collagenase and nucleotide sequence of the corresponding gene. J. Bacteriol. 176, 149-156.
98. McGonigle, L., Mousley, A., Marks, N. J., Brennan, G. P., Dalton, J. P., Spithill, T. W., Day, T. A., and Maule, A. G. (2008). The silencing of cysteine proteases in Fasciola hepatica newly excysted juveniles using R. N. A. interference reduces gut penetration. Int. J. Parasitol. 38, 149-155.
99. Meemon, K., Grams, R., Vichasri-Grams, S., Hofmann, A., Korge, G., Viyanant, V., Upatham, E. S., Habe, S., and Sobhon, P. (2004). Molecular cloning and analysis of stage and tissue-specific expression of cathepsin B encoding genes from Fasciola gigantica. Mol. Biochem. Parasitol. 136, 1-10.
100. Mentlein, R., Dahms, P., Grandt, D., and Krüger, R. (1993). Proteolytic processing of neuropeptide Y and peptide YY by dipeptidyl peptidase IV. Regul. Pept. 49, 133-144.
101. Miller, E. J., and Gay, S. (1982). Collagen: an overview. Methods Enzymol. 82 Pt A, 3-32.
102. Minor, R. R. (1980). Collagen metabolism: a comparison of diseases of collagen and diseases affecting collagen. Am. J. Pathol. 98, 225-280.
103. Mitchell, G. (2002). Update on Fasciolosis in Cattle and Sheep. In Practice 24(7), 378.
104. Miyamoto, K., Nukui, E., Itoh, H., Sato, T., Kobayashi, T., Imada, C., Watanabe, E., Inamori, Y., and Tsujibo, H. (2002). Molecular analysis of the gene encoding a novel chitin-binding protease from Alteromonas sp. strain O-7 and its role in the chitinolytic system. J. Bacteriol. 184, 1865-1872.
105. Moncada, D., Keller, K., and Chadee, K. (2003). Entamoeba histolytica cysteine proteinases disrupt the polymeric structure of colonic mucin and alter its protective function. Infect Immun. 71, 838-844.
106. Morjhara, K., and Homma, J. (1985). Pseudomonas proteases. In: Holder I, ed. Bacterial enzymes and virulence. Boca Raton, Fl: C. R. C. Press.
107. Morphew, R. M., Wright, H. A., LaCourse, E. J., Woods, D. J., and Brophy, P. M. (2007). Comparative proteomics of excretory-secretory proteins released by the liver fluke Fasciola hepatica in sheep host bile and during in vitro culture ex host. Mol. Cell Proteomics 6, 963-972.
108. Murphy, G., Allan, J. A., Willenbrock, F., Cockett, M. I., O'Connell, J. P., and Docherty, A. J. (1992). The role of the C-terminal domain in collagenase and stromelysin specificity. J. Biol. Chem. 267, 9612-9618.
109. Munoz, M. L., Calderón, J., and Rojkind, M. (1982). The collagenase of Entamoeba histolytica. J. Exp. Med. 155, 42-51.
110. Nagase, H., Visse, R., and Murphy, G. (2006). Structure and function of matrix metalloproteinases and TIMPs. Cardiovasc. Res. 69, 562-573.
111. Ndung'u, J. M., Wright, N. G., Jennings, F. W., and Murray, M. (1992). Changes in atrial natriuretic factor and plasma renin activity in dogs infected with Trypanosoma brucei. Parasitol. Res. 78, 553-556.
112. Netzel-Arnett, S., Salari, A., Goli, U. B., and Van Wart, H. E. (1994). Evidence for a triple helix recognition site in the hemopexin-like domains of human fibroblast and neutrophil interstitial collagenases. Ann. N. Y. Acad. Sci. 732, 22-30.
113. Nikolskaia, O. V., de A. Lima, A. P., Kim, Y. V., Lonsdale-Eccles, J. D., Fukuma, T., Scharfstein, J., and Grab, D. J. (2006). Blood-brain barrier traversal by African trypanosomes requires calcium signaling induced by parasite cysteine protease. J. Clin. Invest. 116, 2739-2747.
114. Nogueira de Melo, A. C., de Souza, E. P., Elias, C. G., dos Santos, A. L., Branquinha, M. H., d'Avila-Levy, C. M., dos Reis, F., Costa, T. F., Lima, A. P., de Souza Pereira, M. C., et al. (2010). Detection of matrix metallopeptidase-9-like proteins in Trypanosoma cruzi. Exp. Parasitol. 125, 256-263.
115. Oakley, C. L., Warrack, G. H., and Van Heyningen, W. E. (1946). The collagenase (kappa toxin) of Cl. welchii type A. J. Pathol. Bacteriol. 58, 229-235.
116. Oda, K., Ito, M., Uchida, K., Shibano, Y., Fukuhara, K., and Takahashi, S. (1996). Cloning and expression of an isovaleryl pepstatin-insensitive carboxyl proteinase gene from Xanthomonas sp. T-22. J. Biochem. 120, 564-572.
117. Ohuchi, E., Imai, K., Fujii, Y., Sato, H., Seiki, M., and Okada, Y. (1997). Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules. J. Biol. Chem. 272, 2446-2451.
118. Orikoshi, H., Nakayama, S., Hanato, C., Miyamoto, K., and Tsujibo, H. (2005). Role of the N-terminal polycystic kidney disease domain in chitin degradation by chitinase A from a marine bacterium, Alteromonas sp. strain O-7. J. Appl. Microbiol. 99, 551-557.
119. Overall, C. M. (2002). Molecular determinants of metalloproteinase substrate specificity: matrix metalloproteinase substrate binding domains, modules, and exosites. Mol. Biotechnol. 22, 51-86.
120. Palmer, G. E., Askew, D. S., and Williamson, P. R. (2008). The diverse roles of autophagy in medically important fungi. Autophagy 4, 982-988.
121. Park, S. J., and Mehrad, B. (2009). Innate immunity to Aspergillus species. Clin. Microbiol. Rev. 22, 535-551.
122. Perrakis, A., Tews, I., Dauter, Z., Oppenheim, A. B., Chet, I., Wilson, K. S., and Vorgias, C. E. (1994). Crystal structure of a bacterial chitinase at 2.3 A resolution. Structure 2, 1169-1180.
123. Peterkofsky, B. (1982). Bacterial collagenase. Methods Enzymol. 82, 453-471.
124. Pflugfelder, S. C., and Flynn, H. W. (1992). Infectious endophthalmitis. Infect Dis. Clin. North Am. 6, 859-873.
125. Pollack, M. (1984). The virulence of Pseudomonas aeruginosa. Rev. Infect Dis. 6 Suppl. 3, S617-626.
126. Pollack, M. (1985). Pseudomonas aeruginosa. In: Mandell G., Douglas R., and Bennett J., eds. Principles and practice of infectious diseases. New York: John Wiley and Sons.
127. Prockop, D. J., Kivirikko, K. I., Tuderman, L., and Guzman, N. A. (1979). The biosynthesis of collagen and its disorders (first of two parts). N. Engl. J. Med. 301, 13-23.
128. Rawlings, N. D., Barrett, A. J., and Bateman, A. (2012). M. E. R. O. P. S.: the database of proteolytic enzymes, their substrates and inhibitors. Nucleic. Acids. Res. 40, D343-350.
129. Reed, S. L., Keene, W. E., McKerrow, J. H., and Gigli, I. (1989). Cleavage of C3 by a neutral cysteine proteinase of Entamoeba histolytica. J. Immunol. 143, 189-195.
130. Reichard, U., Büttner, S., Eiffert, H., Staib, F., and Rüchel, R. (1990). Purification and characterisation of an extracellular serine proteinase from Aspergillus fumigatus and its detection in tissue. J. Med. Microbiol. 33, 243-251.
131. Reyes, C. D., and García, A. J. (2004). Alpha2beta1 integrin-specific collagen-mimetic surfaces supporting osteoblastic differentiation. J. Biomed. Mater. Res. A 69, 591-600.
132. Robinson, M. W., Corvo, I., Jones, P. M., George, A. M., Padula, M. P., To, J., Cancela, M., Rinaldi, G., Tort, J. F., Roche, L., et al. (2011). Collagenolytic activities of the major secreted cathepsin L peptidases involved in the virulence of the helminth pathogen, Fasciola hepatica. PLoS Negl. Trop. Dis. 5, e1012.
133. Robinson, M. W., and Dalton, J. P. (2009). Zoonotic helminth infections with particular emphasis on fasciolosis and other trematodiases. Philos. Trans. R. Soc. Lond. B. Biol. Sci. 364, 2763-2776.
134. Robinson, M. W., Dalton, J. P., and Donnelly, S. (2008a). Helminth pathogen cathepsin proteases: it's a family affair. Trends. Biochem. Sci. 33, 601-608.
135. Robinson, M. W., Tort, J. F., Lowther, J., Donnelly, S. M., Wong, E., Xu, W., Stack, C. M., Padula, M., Herbert, B., and Dalton, J. P. (2008b). Proteomics and phylogenetic analysis of the cathepsin L protease family of the helminth pathogen Fasciola hepatica: expansion of a repertoire of virulence-associated factors. Mol. Cell Proteomics. 7, 1111-1123.
136. Rojkind, M. (1979). Chemistry and biosynthesis of collagen. Bull. Rheum. Dis. 30, 1006-1010.
137. Rood, J., McClane, B., Songer, J., and Titball, R. (1997). The Clostridia: Molecular Biology and Pathogenesis. London: Academic, 533.
138. Sanchez-Lopez, R., Alexander, C. M., Behrendtsen, O., Breathnach, R., and Werb, Z. (1993). Role of zinc-binding- and hemopexin domain-encoded sequences in the substrate specificity of collagenase and stromelysin-2 as revealed by chimeric proteins. J. Biol. Chem. 268, 7238-7247.
139. Santana, J. M., Grellier, P., Schrével, J., and Teixeira, A. R. (1997). A Trypanosoma cruzi-secreted 80 kDa proteinase with specificity for human collagen types I and IV. Biochem. J. 325 (Pt 1), 129-137.
140. Schofield, C. J., Jannin, J., and Salvatella, R. (2006). The future of Chagas disease control. Trends Parasitol. 22, 583-588.
141. Shen, H. D., Tam, M. F., Chou, H., and Han, S. H. (1999). The importance of serine proteinases as aeroallergens associated with asthma. Int. Arch. Allergy Immunol. 119, 259-264.
142. Shi, L., Ermis, R., Garcia, A., Telgenhoff, D., and Aust, D. (2010). Degradation of human collagen isoforms by Clostridium collagenase and the effects of degradation products on cell migration. Int. Wound J. 7, 87-95.
143. Singh, B., Fleury, C., Jalalvand, F., and Riesbeck, K. (2012). Human pathogens utilize host extracellular matrix proteins laminin and collagen for adhesion and invasion of the host. F. E. M. S. Microbiol. Rev.
144. Smith, A. M., Dowd, A.., Heffernan, M., Robertson, C. D., and Dalton, J. P. (1993). Fasciola hepatica: a secreted cathepsin L-like proteinase cleaves host immunoglobulin. Int. J. Parasitol. 23, 977-983.
145. Smith, L. D. (1979). Virulence factors of Clostridium perfringens. Rev. Infect Dis. 1, 254-262.
146. Springman, E. B., Angleton, E. L., Birkedal-Hansen, H., and Van Wart, H. E. (1990). Multiple modes of activation of latent human fibroblast collagenase: evidence for the role of a Cys73 active-site zinc complex in latency and a "cysteine switch" mechanism for activation. Proc. Natl. Acad. Sci. US 87, 364-368.
147. Stack, C. M., Caffrey, C. R., Donnelly, S. M., Seshaadri, A., Lowther, J., Tort, J. F., Collins, P. R., Robinson, M. W., Xu, W., McKerrow, J. H., et al. (2008). Structural and functional relationships in the virulence-associated cathepsin L proteases of the parasitic liver fluke, Fasciola hepatica. J. Biol. Chem. -9908.
148. Stanley, S. L., and Reed, S. L. (2001). Microbes and microbial toxins: paradigms for microbial-mucosal interactions. VI. Entamoeba histolytica: parasite-host interactions. Am. J. Physiol. Gastrointest Liver Physiol. 280, G1049-1054.
149. Starkweather, K. D., Lattuga, S., Hurst, L. C., Badalamente, M. A., Guilak, F., Sampson, S. P., Dowd, A., and Wisch, D. (1996). Collagenase in the treatment of Dupuytren's disease: an in vitro study. J. Hand Surg. Am. 21, 490-495.
150. Stenfors Arnesen, L. P., Fagerlund, A., and Granum, P. E. (2008). From soil to gut: Bacillus cereus and its food poisoning toxins. F. E. M. S. Microbiol. Rev. 32, 579-606.
151. Sternlicht, M. D., and Werb, Z. (2001). How matrix metalloproteinases regulate cell behavior. Annu. Rev. Cell Dev. Biol. 17, 463-516.
152. Sweeney, S. M., DiLullo, G., Slater, S. J., Martinez, J., Iozzo, R. V., Lauer-Fields, J. L., Fields, G.., and San Antonio, J. D. (2003). Angiogenesis in collagen I requires alpha2beta1 ligation of a GFPz.ast;GER sequence and possibly p. 38 M. A. P. K. activation and focal adhesion disassembly. J. Biol. Chem. 278, 30516-30524.
153. Sweeney, S. M., Orgel, J. P., Fertala, A., McAuliffe, J. D., Turner, K. R., Di Lullo, G. A., Chen, S., Antipova, O., Perumal, S., Ala-Kokko, L., et al. (2008). Candidate cell and matrix interaction domains on the collagen fibril, the predominant protein of vertebrates. J. Biol. Chem. 283, 21187-21197.
154. Tallant, C., Marrero, A., and Gomis-Rüth, F. X. (2010). Matrix metalloproteinases: fold and function of their catalytic domains. Biochim. Biophys. Acta. 1803, 20-28.
155. Tardieux, I., Webster, P., Ravesloot, J., Boron, W., Lunn, J. A., Heuser, J. E., and Andrews, N. W. (1992). Lysosome recruitment and fusion are early events required for trypanosome invasion of mammalian cells. Cell 71, 1117-1130.
156. Thibeaux, R., Dufour, A., Roux, P., Bernier, M., Baglin, A. C., Frileux, P., Olivo-Marin, J. C., Guillén, N., and Labruyère, E. (2012). Newly visualized fibrillar collagen scaffolds dictate Entamoeba histolytica invasion route in the human colon. Cell Microbiol. 14, 609-621.
157. Thorsell, W., Björkman, N., and Wittander, G. (1965). Studies on the action of some enzymes on the cyst wall of isolated metacerkariae from the liver fluke, Fasciola hepatica L. Experientia 2, 587-589.
158. Tillack, M., Biller, L., Irmer, H., Freitas, M., Gomes, M. A., Tannich, E., and Bruchhaus, I. (2007). The Entamoeba histolytica genome: primary structure and expression of proteolytic enzymes. B. M. C. Genomics 8, 170.
159. Vahey, J. B., and Flynn, H. W. (1991). Results in the management of Bacillus endophthalmitis. Ophthalmic Surg. 22, 681-686.
160. Van Wart, H. E., and Birkedal-Hansen, H. (1990). The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc. Natl. Acad. Sci. US 87, 5578-5582.
161. Vermout, S., Baldo, A., Tabart, J., Losson, B., and Mignon, B. (2008). Secreted dipeptidyl peptidases as potential virulence factors for Microsporum canis. F. E. M. S. Immunol. Med. Microbiol. 54, 299-308.
162. Wang, Y. K., Zhao, G. Y., Li, Y., Chen, X. L., Xie, B. B., Su, H. N., Lv, Y. H., He, H. L., Liu, H., Hu, J., et al. (2010). Mechanistic insight into the function of the C-terminal P. K. D. domain of the collagenolytic serine protease deseasin MCP-01 from deep sea Pseudoalteromonas sp. SM9913: binding of the P. K. D. domain to collagen results in collagen swelling but does not unwind the collagen triple helix. J. Biol. Chem. 285, 14285-14291.
163. Wilson, J. J., Matsushita, O., Okabe, A., and Sakon, J. (2003). A bacterial collagen-binding domain with novel calcium-binding motif controls domain orientation. E. M. B. O. J. 22, 1743-1752.
164. Wilson, L. R., Good, R. T., Panaccio, M., Wijffels, G. L., Sandeman, R. M., and Spithill, T. W. (1998). Fasciola hepatica: characterization and cloning of the major cathepsin B protease secreted by newly excysted juvenile liver fluke. Exp. Parasitol. 88, 85-94.
165. Wolf, K., Mazo, I., Leung, H., Engelke, K., von Andrian, U. H., Deryugina, E. I., Strongin, A. Y., Bröcker, E. B., and Friedl, P. (2003). Compensation mechanism in tumor cell migration: mesenchymal-amoeboid transition after blocking of pericellular proteolysis. J. Cell Biol. 160, 267-277.
166. Woods, D. E., Cryz, S. J., Friedman, R. L., and Iglewski, B. H. (1982). Contribution of toxin A and elastase to virulence of Pseudomonas aeruginosa in chronic lung infections of rats. Infect Immun. 36, 1223-1228.
167. Woods, D. E., and Iglewski, B. H. (1983). Toxins of Pseudomonas aeruginosa: new perspectives. Rev. Infect. Dis. 5 Suppl. 4, S715-722.
168. Wretlind, B., and Pavlovskis, O. R. (1983). Pseudomonas aeruginosa elastase and its role in pseudomonas infections. Rev. Infect Dis. 5 Suppl. 5, S998-1004.
169. Yong, V. W., Power, C., Forsyth, P., and Edwards, D. R. (2001). Metalloproteinases in biology and pathology of the nervous system. Nat. Rev. Neurosci. 2, 502-511.
170. Yoshihara, K., Matsushita, O., Minami, J., and Okabe, A. (1994). Cloning and nucleotide sequence analysis of the colH gene from Clostridium histolyticum encoding a collagenase and a gelatinase. J. Bacteriol. 176, 6489-6496.
171. Zhao, B., Janson, C. A., Amegadzie, B. Y., D'Alessio, K., Griffin, C., Hanning, C. R., Jones, C., Kurdyla, J., McQueney, M., Qiu, X., et al. (1997). Crystal structure of human osteoclast cathepsin K complex with E-64. Nat. Struct. Biol. 4, 109-111.
172. Zhao, G. Y., Chen, X. L., Zhao, H. L., Xie, B. B., Zhou, B. C., and Zhang, Y. Z. (2008). Hydrolysis of insoluble collagen by deseasin MCP-01 from deep-sea Pseudoalteromonas sp. SM9913: collagenolytic characters, collagen-binding ability of C-terminal polycystic kidney disease domain, and implication for its novel role in deep-sea sedimentary particulate organic nitrogen degradation. J. Biol. Chem. 283, 36100-36107.