Abstract | OBJECTIVE: MATERIALS AND METHODS: RESULTS: Adding interleukin-1beta resulted in progressive gel breakdown. This was associated particularly with a shift in MMP-1 band position from proenzyme to active enzyme and the appearance of active as well as proenzyme forms of cathepsin B. There was also partial processing of pro-MMP-13 and increased immunoreactivity for active cathepsin L. In addition, both pro-forms and active forms of MMP-8, membrane-type-1-MMP and MMP-2 were present in control and treated cultures. CONCLUSIONS: Fibroblast MMP-1 was most likely responsible for collagen dissolution in the culture model, while cathepsin B may have been part of an activation pathway. All studied proteinases contribute to extracellular matrix destruction in inflamed gingival tissue, where they probably activate each other in proteolytic cascades.
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Authors | S W Cox, B M Eley, M Kiili, A Asikainen, T Tervahartiala, T Sorsa |
Journal | Oral diseases
(Oral Dis)
Vol. 12
Issue 1
Pg. 34-40
(Jan 2006)
ISSN: 1354-523X [Print] Denmark |
PMID | 16390466
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Collagen Type I
- Interleukin-1
- Cysteine Endopeptidases
- Cathepsin B
- Matrix Metalloproteinases
- Hydroxyproline
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Topics |
- Adult
- Blotting, Western
- Cathepsin B
(metabolism)
- Collagen Type I
(metabolism)
- Cysteine Endopeptidases
(metabolism)
- Electrophoresis, Polyacrylamide Gel
- Enzyme Activation
- Female
- Fibroblasts
(drug effects, enzymology)
- Gingiva
(cytology, enzymology)
- Humans
- Hydroxyproline
(metabolism)
- Interleukin-1
(pharmacology)
- Male
- Matrix Metalloproteinases
(metabolism)
- Middle Aged
- Periodontitis
(enzymology)
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