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Cell-associated collagenolytic activity by Candida albicans

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Abstract

Cell associated collagenolytic activity of Candida albicans was quantified by measuring the degradation of synthetic peptide 2-furanacryloyl-Leu-Gly-Pro-Ala (FALGPA), which is a specific substrate for collagenase, by the freeze-thaw procedure method. This collagenolytic activity was enhanced by cells cultured in the presence of bovine serum albumin (BSA) in culture medium. However, this activity was inhibited in the presence of ethylenediaminetetraacetic acid disodium salt (EDTA-2Na), but not by the serine proteinase inhibitor p-amidinophenyl methanesulfonyl fluoride (APMSF), nor the aspartyl proteinase inhibitor pepstatin A. These results suggested the presence of a metalloenzyme on pericellular C. albicans.

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Authors and Affiliations

  1. Department of Prosthetic Dentistry, Hiroshima University Faculty of Dentistry, 1-2-3 Kasumi Minami-ku, Hiroshima, 734-8553, Japan

    Masahiro Nishimura, Hiroki Nikawa, Hirofumi Yamashiro, Haruki Nishimura & Taizo Hamada

  2. Department of Basic Dental Science, Dental School, University of Wales College of Medicine, Heath Park, Cardiff, CF14 4XY, UK

    Masahiro Nishimura & Graham Embery

Authors
  1. Masahiro Nishimura
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  2. Hiroki Nikawa
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  3. Hirofumi Yamashiro
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  4. Haruki Nishimura
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  5. Taizo Hamada
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  6. Graham Embery
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Nishimura, M., Nikawa, H., Yamashiro, H. et al. Cell-associated collagenolytic activity by Candida albicans . Mycopathologia 153, 125–128 (2002). https://doi.org/10.1023/A:1014506115757

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