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Heme oxygenase (HO)-1 is upregulated in the nasal mucosa with allergic rhinitis.

Authors: Elhini, A  Abdelwahab, S  Ikeda, K 
Citation: Elhini A, etal., Laryngoscope. 2006 Mar;116(3):446-50.
Pubmed: (View Article at PubMed) PMID:16540907
DOI: Full-text: DOI:10.1097/01.mlg.0000194692.51979.d1

BACKGROUND: Heme oxygenase (HO) is considered to be an antioxidant enzyme that catabolizes heme to produce carbon monoxide (CO) and biliverdin. Three isoforms of HO have been discovered. Recently, HO-1 has been found to be upregulated after allergic inflammations of the lower airway. OBJECTIVE: The objective of this study was to address the expression of HO isoenzymes 1 and 2 in the nasal mucosa of patients with allergic rhinitis as well as normal control subjects. METHODS: Nasal mucosa from 30 patients with persistent allergic rhinitis as well as from 10 normal volunteers was used in this study. We used immunofluorescent technique, Western blotting, and real-time quantitative polymerase chain reaction to localize and quantify the expression of these isoenzymes in normal and allergic human nasal tissues. RESULTS: We found that HO-1 is expressed in the epithelial cells of seromucinous glands and macrophages with significant upregulation of its glandular expression in allergic rhinitis but with no difference in its macrophage expression between the study groups in contrast to HO-2 that is expressed in the vascular endothelial lining cells as well as macrophages with no marked difference between the study groups. CONCLUSION: We demonstrated that expression of HO-1, but not HO-2, was upregulated within the nasal tissues in allergic rhinitis inflammation, and understanding the induction of HO-1 expression may provide for better management of allergic rhinitis that involves oxidative stress.


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CRRD Object Information
CRRD ID: 4145406
Created: 2010-11-03
Species: All species
Last Modified: 2010-11-03
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.