Direct activation of gelatinase B (MMP-9) by hay dust suspension and different components of organic dust.
Abstract: Matrix metalloproteinases (MMPs) are involved in tissue destruction in allergic airway diseases. We studied the ability of various allergenic substances to directly activate recombinant 92kDa proMMP-9. The substances included hay dust suspension (HDS) and its components (supernatant, particulate matter and wash fluid of particulate matter), storage mite extract and two Aspergillus fumigatus extracts. The allergen suspensions were incubated in vitro with proMMP-9. After incubation the conversion of proMMP-9 to 10kDa lower active forms were studied using gelatin zymography and Western immunoblot quantified by computerized densitometry. All studied allergens except HDS significantly and efficiently activated proMMP-9 as compared to a negative control. At the concentrations employed, the most potent activators were A. fumigatus extracts and mite suspension. The greater potency of mite and fungi as proMMP-9 activators suggests that these allergens may be more damaging to airways even at low concentrations.
Publication Date: 2005-09-21 PubMed ID: 16181685DOI: 10.1016/j.vetimm.2005.08.019Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The research explores how different allergens, particularly hay dust and its components, storage mite extract, and two types of fungus extracts, can directly activate a protein (proMMP-9) involved in tissue destruction in allergic airway illnesses. The study found that all tested allergens, excluding hay dust, notably activated proMMP-9 compared to a control, with fungus and mite allergens showing the highest activation potential.
Research Methodology
- The study involved testing various allergens to see their capability to activate a protein known as proMMP-9, which is implicated in tissue damage in allergic airway diseases.
- The allergens tested were hay dust suspension (HDS), its various components (the supernatant, particulate matter and wash fluid of particulate matter), an extract from storage mites, and two extracts from a fungus species known as Aspergillus fumigatus.
- The allergen suspensions were all combined in vitro with proMMP-9 and then incubated.
- Following incubation, the transformation of proMMP-9 into lower active forms was examined using techniques known as gelatin zymography and Western immunoblot, which were quantified by computerized densitometry.
Research Findings
- The study found that all the allergens under investigation, with the exception of HDS, were able to activate proMMP-9 significantly and efficiently as compared to a negative control.
- Among the tested allergens, the extracts of Aspergillus fumigatus and the mite suspension showed the highest potency in terms of activating proMMP-9.
Conclusions and Implications
- The research concludes that mite and fungi allergens, due to their greater potency as activators of proMMP-9, could potentially cause more damage to airways, even at low concentrations.
- This implication suggests a need for further research into preventative measures and treatments for allergic reactions triggered by these particular allergens.
Cite This Article
APA
Simonen-Jokinen T, Maisi P, Tervahartiala T, McGorum B, Pirie S, Sorsa T.
(2005).
Direct activation of gelatinase B (MMP-9) by hay dust suspension and different components of organic dust.
Vet Immunol Immunopathol, 109(3-4), 289-295.
https://doi.org/10.1016/j.vetimm.2005.08.019 Publication
Researcher Affiliations
- Department of Clinical Veterinary Sciences, Faculty of Veterinary Medicine, University of Helsinki, Finland. terhi.simonen@helsinki.fi
MeSH Terms
- Acaridae / immunology
- Animals
- Aspergillus fumigatus / immunology
- Blotting, Western / veterinary
- Collagenases / immunology
- Collagenases / metabolism
- Dust / immunology
- Electrophoresis, Polyacrylamide Gel / veterinary
- Enzyme Activation / immunology
- Enzyme Precursors / immunology
- Enzyme Precursors / metabolism
- Horse Diseases / enzymology
- Horse Diseases / immunology
- Horses
- Hypersensitivity / enzymology
- Hypersensitivity / immunology
- Hypersensitivity / veterinary
- Matrix Metalloproteinase 9
Citations
This article has been cited 3 times.- Jeong KY, Hong CS, Lee JS, Park JW. Optimization of allergen standardization.. Yonsei Med J 2011 May;52(3):393-400.
- Yike I. Fungal proteases and their pathophysiological effects.. Mycopathologia 2011 May;171(5):299-323.
- Kurup VP, Barrios CS, Raju R, Johnson BD, Levy MB, Fink JN. Immune response modulation by curcumin in a latex allergy model.. Clin Mol Allergy 2007 Jan 25;5:1.
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