Collagen-binding domain of a Clostridium histolyticum collagenase exhibits a broad substrate spectrum both in vitro and in vivo

T. Toyoshima, O. Matsushita, J. Minami, N. Nishi, A. Okabe, T. Itano

Research output: Contribution to journalArticlepeer-review

45 Citations (Scopus)

Abstract

The substrate spectrum of the tandem collagen-binding domain (CBD) of Clostridium histolyticumclass I collagenase (ColG) was examined both in vitro and in vivo. CBD bound to insoluble type I, II, III and IV collagens in vitro, and to skin, aorta, tendon, kidney, trachea and corneal tissues containing various types of collagen fibrils or sheets. CBD bound to all kinds of collagen fibrils regardless of their diameters and also bound to sheet-forming collagen in the glomerular basal lamina or Descemet's membrane of the cornea. This wide substrate spectrum expands possible applications of the drug delivery system we proposed previously (PNAS 95:7018-7023, 1998). Therapeutic agents fused with CBD will bind not only to subcutaneous tissues, but also to other tissues containing non-type I collagen.

Original languageEnglish
Pages (from-to)281-290
Number of pages10
JournalConnective Tissue Research
Volume42
Issue number4
DOIs
Publication statusPublished - Jan 1 2001
Externally publishedYes

Keywords

  • Clostridium histolyticum
  • Collagen-binding domain
  • Collagenase
  • Immunoelectron microscopy
  • Substrate spectrum

ASJC Scopus subject areas

  • Rheumatology
  • Biochemistry
  • Orthopedics and Sports Medicine
  • Molecular Biology
  • Cell Biology

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