title: Cell-associated collagenolytic activity by Candida albicans.
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.
authors: Department of Prosthetic Dentistry, Hiroshima University Faculty of Dentistry, Japan. maakun@hiroshima-u.ac.jp
authors: Masahiro
authors: M
authors: Nishimura
authors: Hiroki
authors: H
authors: Nikawa
authors: Hirofumi
authors: H
authors: Yamashiro
authors: Haruki
authors: H
authors: Nishimura
authors: Taizo
authors: T
authors: Hamada
authors: Graham
authors: G
authors: Embery
mesh_terms: 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
chemical_list: 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