Collagen-Binding Domain of a Clostridium Histolyticum Collagenase Exhibits a Broad Substrate Spectrum Both in Vitro and in Vivo

References

• Bond M. D., Van Wart H. E. Relationship between the individual collagenases of Clostridium histolyticum: Evidence for evolution by gene duplication. Biochemistry 1984; 23: 3092–3099
   PubMed Web of Science ®Google Scholar
• Mookhtiar K. A., Van Wart H. E. Clostridium histolyticum collagenases: a new look at some old enzymes. Matrix Suppl. 1992; 1: 116–126
   PubMedGoogle Scholar
• Yoshihara K., Matsushita O., Minami J., Okabe A. Cloning and nucleotide sequence analysis of the colH gene from Clostridium histolyticum encoding a collagenase and a gelatinase. J. Bacteriol. 1994; 176: 6489–6496
   PubMed Web of Science ®Google Scholar
• Matsushita O., Jung C.-M., Minami J., Katayama S., Nishi N., Okabe A. A study of the collagen-binding domain of a 116-kDa Clostridium histolyticum collagenase. J. Biol. Chem. 1998; 273: 3643–3648
   PubMed Web of Science ®Google Scholar
• Nishi N., Matsushita O., Yuube K., Miyanaka H., Okabe A., Wada F. Collagen-binding growth factors: Production and characterization of functional fusion proteins having a collagen-binding domain. Proc. Natl. Acad. Sci. U.S.A. 1998; 95: 7018–7023
   PubMed Web of Science ®Google Scholar
• Matsushita O., Jung C.-M., Katayama S., Minami J., Takahashi Y., Okabe A. Gene duplication and multiplicity of collagenases in Clostridium histolyticum. J. Bacterial. 1999; 181: 923–933
   PubMed Web of Science ®Google Scholar
• Matsushita O., Koide T., Kobayashi R., Nagata K., Okabe A. Substrate recognition by the collagen-binding domain of Clostridium histolyticum class I collagenase. J. Biol. Chem. 2001; 276: 8761–8770
   PubMed Web of Science ®Google Scholar
• Linsenmayer T. F. “Collagen.”. Cell Biology of Extracellular Matrix, E. D. Hay. Plenum Press, New York 1991; 7–44
   Google Scholar
• Hanson A. N., Bentley J. P. Quantitation of type I to type III collagen ratios in small samples of human tendon, blood vessels, and atherosclerotic plaque. Anal. Biochem. 1983; 130: 32–40
   PubMed Web of Science ®Google Scholar
• Lee R. E., Davison P. F. The collagens of the developing bovine cornea. Exp. Eye Res. 1984; 39: 639–652
   PubMed Web of Science ®Google Scholar
• Birk D. E., Fitch J. M., Babiarz J. P., Linsenmayer T. F. Collagen type I and type V are present in the same fibril in the avian corneal stroma. J. Cell Biol. 1988; 106: 999–1008
   PubMed Web of Science ®Google Scholar
• Hey N. J., Handley C. J., Ng C. K., Oakes B. W. Characterization and synthesis of macromolecules by adult collateral ligament. Biochim. Biophys. Acta 1990; 1034: 73–80
   PubMed Web of Science ®Google Scholar
• van der Rest M., Garrone R. Collagen family of proteins. FASEB J. 1991; 5: 2814–2823
   PubMed Web of Science ®Google Scholar
• Seglen P. O. Preparation of isolated rat liver cells. Methods Cell Biol. 1976; 13: 29–83
   PubMedGoogle Scholar
• Peterkofsky B. Bacterial collagenase. Methods Enzymol. 1982; 82: 2444–2448
   Google Scholar
• Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci, U. S. A. 1979; 76: 4350–4354
   PubMed Web of Science ®Google Scholar
• Atkinson C. T., Millet P., Collins W. E., Aikawa M. Localization of circum sporozoite antigen in exoerythrocytic schizonts of Plasmodium cynomolgi. Am, J. Trop. Med. Hyg. 1989; 40: 131–140
   PubMed Web of Science ®Google Scholar
• Ehlers N. Some comparative studies on the mammalian corneal epithelium. Acta Ophthal. 1970; 48: 821–828
   Web of Science ®Google Scholar
• Murata K., Motoyama T., Kotake C. Collagen types in various layers of the human aorta and their changes with the atherosclerotic process. Atherosclerosis 1986; 60: 251–262
   PubMed Web of Science ®Google Scholar
• Nakayasu K., Tanaka M., Konomi H., Hayashi T. Distribution of types I, II, III, IV and V collagen in normal and keratoconus corneas. Ophthalmic Res. 1986; 18: 1–10
   PubMed Web of Science ®Google Scholar
• Farquharson C., Robins S. P. Immunolocalization of collagen types I and III in the arterial wall of the rat. Histochem. J. 1989; 21: 172–178
   PubMedGoogle Scholar
• Tsuzaki M., Yamauchi M., Banes A. J. Tendon collagens: Extracellular matrix composition in shear stress and tensile components of flexor tendons. Connect. Tissue Res. 1993; 29: 141–152
   PubMed Web of Science ®Google Scholar
• McCullagh K. A., Balian G. Collagen characterization and transformation in human atherosclerosis. Nature 1975; 258: 73–75
   PubMed Web of Science ®Google Scholar
• Smith L. T., Holbrook K. A., Madri J. A. Collagen types I, III, and V in human embryonic and fetal skin. Am. J. Anat. 1986; 175: 507–521
   PubMedGoogle Scholar
• Birk D. E., Fitch J. M., Babiarz J. P., Doane K. J., Linsenmayer T. F. Collagen fibrillogenesis in vitro: interaction of types I and V collagen regulates fibril diameter. J. Cell Sci. 1990; 95: 649–657
   PubMed Web of Science ®Google Scholar
• Adachi E., Hayashi T., Hashimoto P. H. Immunoelectron microscopical evidence that type V collagen is a fibrillar collagen: importance for an aggregation capability of the preparation for reconstituting banding fibrils. Matrix 1989; 9: 232–237
   PubMedGoogle Scholar
• Irwin M. H., Silvers S. H., Mayne R. Monoclonal antibody against chicken type IX collagen: preparation, characterization, and recognition of the intact form of type IX collagen secreted by chondrocytes. J. Cell Biol. 1985; 101: 814–823
   PubMed Web of Science ®Google Scholar
• Fawcett D. W. “Cartilage.”. A Textbook of Histology, D. W. Fawcett. Chapman & Hall, New York 1994; 188–198
   Google Scholar
• Furcht L. T., Smith D., Wendelschafer-Crabb G., Mosher D. F., Foidart J. M. Fibronectin presence in native collagen fibrils of human fibroblasts: Immunoperoxidase and immunoferritin localization. J. Histochem. Cytochem. 1980; 28: 1319–1333
   PubMed Web of Science ®Google Scholar
• Pringle G. A., Dodd C. M. Immunoelectron microscopic localization of the core protein of decorin near the d and e bands of tendon collagen fibrils by use of monoclonal antibodies. J. Histochem. Cytochem. 1990; 38: 1405–1411
   PubMed Web of Science ®Google Scholar
• Fleischmajer R., Fisher L. W., MacDonald E. D., Jacobs L., Jr., Perlish J. S., Termine J. D. Decorin interacts with fibrillar collagen of embryonic and adult human skin. J. Struct. Biol. 1991; 106: 82–90
   PubMed Web of Science ®Google Scholar
• San Antonio J., Lander A. D., Karnovsky M. J., Slayter H. S. Mapping the heparin-binding sites on type I collagen monomers and fibrils. J. Cell Biol. 1994; 125: 1179–1188
   PubMed Web of Science ®Google Scholar
• Ramshaw J. A., Shah N. K., Brodsky B. Gly-X-Y tripeptide frequencies in collagen: a context for host-guest triple-helical peptides. J. Struct. Biol. 1998; 122: 86–91
   PubMed Web of Science ®Google Scholar