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Updated: Jun 13, 2026
A Soluble Tetrazolium-Based Reduction Assay to Evaluate the Effect of Antibodies on Candida tropicalis Biofilms
Published on: September 16, 2022
The effects of Candida proteinases on human proMMP-9, TIMP-1 and TIMP-2
Pirjo Pärnänen1, Jukka H Meurman, Timo Sorsa
1Institute of Dentistry, University of Helsinki, Helsinki, Finland. pirjo.parnanen@helsinki.fi
Abstract:
Matrix metalloproteinase (MMP)-9 activity is controlled by the balance between MMP-9 and its major tissue inhibitor of metalloproteinases (TIMPs). We hypothesised whether Candida proteinases may affect local tissue inflammatory processes by modifying these molecules. The effects of sonicated cells and concentrated growth media of six Candida species on MMP-9, TIMP-1 and TIMP-2 were tested. Incubated samples were analysed by Western blot and detected by enhanced chemoluminescence techniques. The residual activity of degraded TIMP-1 was evaluated by a casein degradation assay. The proteinase activity of the microbial strains was also assessed by a fluorimetric assay, and the action of inhibitors on MMP-14 and Candida parapsilosis Cp2 was demonstrated. Cell fractions of both strains of C. parapsilosis exerted a weak ability to convert 92-kDa proMMP-9 to 86-kDa active form. Cell fractions of both strains of Candida albicans, C. parapsilosis Cp2, Candida glabrata reference strain, and both strains of Candida krusei fragmented TIMP-1 (28 kDa) to a 24-kDa species, which associated with reduced inhibitory activity on MMP-9 caseinolysis. Our findings indicate that Candida can participate in tissue inflammation by modifying the host's MMP-9 and their inhibitors. A rapid fluorimetric assay can be adapted for Candida proteinases.
Insights
Candida proteinases can degrade TIMP-1, a key inhibitor of MMP-9, potentially worsening local tissue inflammation. This study reveals how Candida species impact host inflammatory molecules.
Area of Science:
- Microbiology
- Immunology
- Biochemistry
Background:
- Matrix metalloproteinase (MMP)-9 activity is regulated by its inhibitors, tissue inhibitors of metalloproteinases (TIMPs).
- Candida species are known pathogens that can trigger inflammatory responses.
Purpose of the Study:
- To investigate whether Candida proteinases can modify MMP-9 and its inhibitors (TIMP-1 and TIMP-2).
- To explore the potential role of Candida in modulating host inflammatory processes.
Main Methods:
- Testing the effects of sonicated cells and growth media from six Candida species on MMP-9, TIMP-1, and TIMP-2.
- Analysis using Western blot and enhanced chemiluminescence.
- Evaluation of residual TIMP-1 activity via casein degradation assay.
- Assessment of Candida proteinase activity using fluorimetric and caseinolysis assays.
Main Results:
- Candida albicans, C. parapsilosis, C. glabrata, and C. krusei fragmented TIMP-1, reducing its inhibitory activity against MMP-9.
- C. parapsilosis showed a weak ability to activate proMMP-9.
- A fluorimetric assay was effective for detecting Candida proteinase activity.
Conclusions:
- Candida species can degrade TIMP-1, thereby potentially increasing MMP-9 activity and contributing to local tissue inflammation.
- These findings highlight a novel mechanism by which fungal infections can influence host inflammatory responses.
- A rapid fluorimetric assay is suitable for assessing Candida proteinase activity.
