Cell-associated collagenolytic activity by Candida albicans.
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.
Nishimura
Masahiro
M
Department of Prosthetic Dentistry, Hiroshima University Faculty of Dentistry, Japan. maakun@hiroshima-u.ac.jp
Nikawa
Hiroki
H
Yamashiro
Hirofumi
H
Nishimura
Haruki
H
Hamada
Taizo
T
Embery
Graham
G
D001673:Biodegradation, Environmental; D002176:Candida albicans / Q000187:drug effects / Q000254:growth & development / Q000378:metabolism*; D017364:Collagenases / Q000378:metabolism*; D004492:Edetic Acid / Q000494:pharmacology; D061965:Matrix Metalloproteinase Inhibitors; D009842:Oligopeptides / Q000378:metabolism; D010436:Pepstatins / Q000494:pharmacology; D011480:Protease Inhibitors / Q000494:pharmacology; D015842:Serine Proteinase Inhibitors / Q000494:pharmacology
D061965:Matrix Metalloproteinase Inhibitors; D009842:Oligopeptides; D010436:Pepstatins; D011480:Protease Inhibitors; D015842:Serine Proteinase Inhibitors; C031821:2-furanacryloyl-leucyl-glycyl-prolyl-alanine; D004492:Edetic Acid; D017364:Collagenases; C031375:pepstatin