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Cell-associated collagenolytic activity by Candida albicans.
Masahiro Nishimura1, Hiroki Nikawa, Hirofumi Yamashiro
1Department of Prosthetic Dentistry, Hiroshima University Faculty of Dentistry, Japan. maakun@hiroshima-u.ac.jp
Mycopathologia
|May 10, 2002
Summary
Candida albicans exhibits cell-associated collagenolytic activity, enhanced by bovine serum albumin (BSA). This activity, inhibited by ethylenediaminetetraacetic acid disodium salt (EDTA-2Na), suggests a pericellular metalloenzyme.
Area of Science:
- Microbiology
- Biochemistry
- Enzymology
Background:
- Candida albicans is an opportunistic fungal pathogen.
- Fungal collagenases play a role in tissue invasion.
- Understanding C. albicans enzymatic activity is crucial for infection control.
Purpose of the Study:
- To quantify and characterize the cell-associated collagenolytic activity of Candida albicans.
- To investigate factors influencing this enzymatic activity.
Main Methods:
- Collagenolytic activity was measured using the synthetic substrate 2-furanacryloyl-Leu-Gly-Pro-Ala (FALGPA).
- Activity was assessed using the freeze-thaw procedure.
- Inhibitor studies were conducted using ethylenediaminetetraacetic acid disodium salt (EDTA-2Na), p-amidinophenyl methanesulfonyl fluoride (APMSF), and pepstatin A.
Main Results:
- Cell-associated collagenolytic activity of C. albicans was detected.
- Activity was enhanced when cells were cultured with bovine serum albumin (BSA).
- The activity was inhibited by EDTA-2Na, indicating a metalloenzyme, but not by APMSF or pepstatin A.
Conclusions:
- Candida albicans possesses cell-associated collagenolytic activity.
- This activity is likely mediated by a metalloenzyme located on the cell surface.
- Bovine serum albumin enhances this metalloenzyme activity.