Human laminin‐332 degradation by Candida proteinases
Abstract
Background: Human laminin‐332 (Lm‐332) degradation by 12 Candida strains and effects of synthetic proteinase inhibitors [Ilomastat (ILM), EDTA, chemically modified tetracycline‐3(CMT‐3), CMT‐308, synthetic peptide CTT‐2, and Pefabloc] were studied. Materials and methods: Laminin‐332 was incubated with sonicated cell fractions and 10 times concentrated cell‐free fractions of reference and clinical strains of C. albicans, C. dubliniensis, C. guilliermondii, C. glabrata, C. krusei, and C. tropicalis. Proteolysis, pH effects, and inhibitors were analyzed by fluorography and zymography. Results: Cell fractions of all species except C. guilliermondii and cell‐free fractions of C. albicans, and C. dubliniensis showed 20–70 kDa gelatinases at pH 5.0 and 6.0. At pH 7.6, C. glabrata, C. krusei, and C. tropicalis cell fractions and C. tropicalis cell‐free fractions showed 55–70 kDa gelatinases. CMT‐3, CMT‐308, and CTT‐2 inhibited Candida gelatinases slightly better than Pefabloc, ILM, and EDTA. No Candida fractions degraded Lm‐332 at pH 7.6, but at pH 5.0, 100 kDa bands were generated by cell fractions of C. dubliniensis and C. tropicalis; C. albicans and C. glabrata clinical strains; and C. guilliermondii reference strain. C. krusei reference strain yielded three 100–130 kDa bands. C. albicans, C. dubliniensis, and C. tropicalis reference and clinical strain’s cell‐free fractions generated 100 kDa band. Conclusions: Laminin‐332 degradation is pH‐dependent and differences exist between studied Candida strains. Lm‐332 degradation can exert functional disturbances on basement membrane integrity, possibly aiding Candida cell invasion into tissues. Certain synthetic matrix metalloproteinase inhibitors (CMTs, CTT) can inhibit Candida proteinases and may be therapeutically useful in future.
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Many fungal pathogens are known to degrade ECM components as part of their tissue invasion strategy.
“Many fungal pathogens are known to degrade ECM components as part of their tissue invasion strategy65–68.”
From Adhesin Als4112 promotes Candida auris skin colonization through interactions with keratinocytes and extracellular matrix proteins (2025) · cites this paper as [67]
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Mavor, A., Thewes, S., & Hube, B. (2005) · Current Drug Targets · doi:10.2174/138945005774912735 · Cited by 252 · see citing works
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Candida glabrata’s Genome Plasticity Confers a Unique Pattern of Expressed Cell Wall Proteins
López-Fuentes, E., Gutiérrez-Escobedo, G., Timmermans, B., Van Dijck, P., De Las Peñas, A., & Castaño, I. (2018) · Journal of Fungi · doi:10.3390/jof4020067 · Cited by 35 · see citing works
Zhao, G., Lyu, J., Veniaminova, N. A., Zarnowski, R., Mattos, E., Johnson, C. J., Quintanilla, D., Hautau, H., Hold, L. A., Xu, B., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-60876-1 · Cited by 32 · see citing works
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Pärnänen, P., Meurman, J. H., Samaranayake, L., & Virtanen, I. (2010) · Journal of Oral Pathology & Medicine · doi:10.1111/j.1600-0714.2009.00866.x · Cited by 28 · see citing works
Self-citation
- Authors
- Pärnänen, P., Kari, K., Virtanen, I., Sorsa, T., & Meurman, J. H.
- Affiliations
- University of Helsinki (FI)
- Corresponding author
- Pärnänen, P.
- Venue
- Journal of Oral Pathology & Medicine
- Publisher
- Wiley
- Published
- 2008-02-17
- Volume
- 37
- Issue
- 6
- Pages
- 329-335
- ISSN
- 0300-9777 (ISSN-L)
- 0904-2512
- 1600-0714
- OpenAlex
- W1508305603
- Cited by
- 24
- References
- 1
- Citations by year
- 2025: 2 · 2022: 2 · 2021: 1 · 2020: 3 · 2018: 1 · 2017: 1 · 2015: 2 · 2014: 2 · 2012: 2
- FWCI
- 1.72
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Oral Pathology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Helsingin ja Uudenmaan Sairaanhoitopiiri
- Topics
- Health Sciences › Medicine › Infectious Diseases › Antifungal resistance and susceptibility
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Keywords
- laminin-5, Candida, Candida albicans, Candida dubliniensis, Candida tropicalis, Candida glabrata, Candida krusei, Candida guilliermondii, fungal proteases, gelatinase, proteolysis, pH dependence, matrix metalloproteinase inhibitors, ilomastat, basement membrane integrity
- MeSH terms
- Kalinin, Basement Membrane, Candida, Cell Line, Edetic Acid, Electrophoresis, Polyacrylamide Gel, Fungal Proteins, Humans, Hydrogen-Ion Concentration, Hydroxamic Acids, Indoles, Peptides, Cyclic, Protease Inhibitors, Sulfones, Tetracyclines, Keratinocytes, Cell Adhesion Molecules, Gelatinases
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