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Immunolocalisation of heme oxygenase isoforms in human nasal polyps

Published online by Cambridge University Press:  07 January 2008

S Lo ,
S Di Palma ,
E George  and
A W McCombe
S Lo*
Affiliation:
Department of Otorhinolaryngology, St George's Hospital Medical School, London, UK
S Di Palma
Affiliation:
Department of Histopathology, Royal Surrey County Hospital, Guildford, UK
E George
Affiliation:
Department of Otorhinolaryngology, Frimley Park Hospital, Frimley, UK
A W McCombe
Affiliation:
Department of Otorhinolaryngology, Frimley Park Hospital, Frimley, UK
*
Address for correspondence: Mr Stephen Lo, 4 Osborne Road Farnborough GU14 6PT, UK. Fax: (+44) (0)208 725 3306 E-mail: stephenlo@lycos.co.uk
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Abstract

Background:

Carbon monoxide is an endogenous vasodilator gas produced by the enzyme heme oxygenase (HO). HO is expressed in human nasal mucosa, but its pathophysiological role in nasal inflammatory diseases is not fully understood. The aim of this study was to detect and compare the expression of HO-1 and -2 isoforms in nasal polyps with normal nasal mucosa.

Methods:

Immunohistochemical analysis using antibodies specific for HO-1 and -2 was conducted on nasal polyps from nine patients with allergic nasal polyposis, and on normal nasal mucosa from six controls.

Results:

Intense HO-1 immunoreactivity was observed in nasal polyp epithelium but was absent in normal nasal mucosa. HO-2 staining was observed in respiratory epithelium, vascular endothelium and seromucous glands, with no difference observed between nasal polyps and normal nasal mucosa.

Conclusions:

HO-1 expression is up-regulated in nasal polyp epithelium, supporting the theory that respiratory epithelium plays a role in the pathogenesis of nasal polyposis.

Keywords

Heme OxygenaseCarbon MonoxideNasal PolypsImmunohistochemistry
Type
Clinical Records
Information
The Journal of Laryngology & Otology , Volume 123 , Issue 1 , January 2009 , pp. 131 - 135
Copyright
Copyright © JLO (1984) Limited 2008

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