Mechanisms of Allergy
Matrix metalloproteinases and their inhibitors in the nasal mucosa of patients with perennial allergic rhinitis,☆☆

https://doi.org/10.1067/mai.2001.119024Get rights and content

Abstract

Background: Allergic rhinitis and asthma show many similarities in their epithelial and inflammatory responses to allergens. However, one notable difference is that disruption and desquamation of the epithelium is a characteristic feature of asthma, whereas in perennial allergic rhinitis the epithelium is intact and thickened. One reason for this might be differing expression of matrix metalloproteinases (MMPs) or their inhibitors (TIMPs). There are few published data on the presence of MMPs or TIMPs in the nasal mucosa in rhinitis. Objective: The purpose of this study was to investigate MMP and TIMP mRNA and protein in nasal mucosa from subjects with perennial allergic rhinitis and from nonrhinitic control subjects. Methods: Biopsy specimens of nasal mucosa were taken from 10 well-characterized subjects with perennial allergic rhinitis and 10 nonrhinitic control subjects. MMP and TIMP mRNA was quantified through use of competitive RT-PCR, and protein was detected by means of Western blotting and ELISA. Results: TIMP-1 mRNA and TIMP-2 mRNA were present in nasal samples, but there was no significant difference between the 2 groups. Only small amounts of MMP-1, -2, -3, and -9 mRNA were detected in the same samples. The corresponding proteins were detected by means of Western blotting. TIMP-1 protein and TIMP-2 protein were quantified in tissue homogenates; there was no significant difference between the 2 groups. Conclusion: Our studies have demonstrated the presence of large amounts of TIMP-1 and TIMP-2 mRNA and protein in nasal mucosa. There is no upregulation of MMPs or changes in TIMP expression in the nasal mucosa of patients with allergic rhinitis. (J Allergy Clin Immunol 2001;108:791-6.)

Section snippets

Subjects

Ten well-characterized subjects with perennial allergic rhinitis were recruited. All subjects had symptoms of perennial allergic rhinitis at the time of biopsy. Nasal examination demonstrated signs consistent with rhinitic mucosal inflammation, such as pale swollen mucosa, red engorged mucosa, and excess mucus. All of these rhinitic subjects had symptoms of bilateral or alternating nasal obstruction and rhinorrhea for at least 1 hour a day throughout the year. Skin prick tests were performed in

ELISA

Tissue was homogenized with lysis buffer. Concentrations of TIMP-1 and TIMP-2 were measured through use of commercially available Biotrak ELISA assay systems (Amersham Pharmacia Biotech, Amersham, United Kingdom) according to the manufacturer's instructions. Sufficient protein for assay was available from 8 rhinitic and 8 nonrhinitic subjects. Each assay was performed in duplicate. The optical density at 450 nm was read through use of a Titertek Multiscan Plus Elisa reader (EFLAB, Helsinki,

MMP and TIMP protein production in perennial allergic rhinitic and nonrhinitic nasal mucosa

Immunoreactive bands at the appropriate molecular weights for interstitial collagenase, gelatinase A, stromelysin-1, and gelatinase B were detected by means of Western blotting in 10 rhinitic and 10 nonrhinitic subjects. The latent forms of interstitial collagenase and stromelysin-1 in the rhinitic group were in general slightly higher than those of the nonrhinitic group, but low-molecular-weight active forms of enzymes were not detected. However, there was no difference in gelatinase A or

Discussion

In this study, we have demonstrated the presence of large amounts of mRNA for TIMP-1 and TIMP-2 and shown that the corresponding protein is abundant in both rhinitic and nonrhinitic subjects. Although MMP proteins were detected by Western blotting, mRNAs for interstitial collagenase, gelatinase A, stromelysin-1, and gelatinase B were not detected in large quantities in the majority of samples. We can conclude, therefore, that MMPs are not upregulated in the nasal mucosa in perennial allergic

Acknowledgements

We thank Dr G. Schultz, University of Florida, for the gift of MMP template (National Eye Institute Grant EY-05587).

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    Supported by the Special Trustees of the Royal London Hospitals NHS Trust, Department of Respiratory Medicine, The London Chest Hospital.

    ☆☆

    Reprint requests: Sylvia L. F. Pender, PhD, Tissue Remodeling and Repair Group, Division of Infection, Inflammation and Repair, Mailpoint 813, Level E, South Academic Block, Southampton General Hospital, Southampton SO16 6YD, United Kingdom.

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