Idiopathic rhinitis represents more than 50% of non-allergic rhinitis, a heterogeneous group that involves the symptomatic inflammation of the nasal mucosa. The TRPV1 receptor of unmyelinated C-type neurons appears to be involved in its pathophysiology. Histamine, whose main catabolic enzyme is DAO, is one of the mediators that can activate this receptor. The failure of DAO causes an increase in the level of histamine in the body and, consequently, the activation of TRPV1. The objective was to investigate the existence of a DAO enzyme activity deficit in idiopathic rhinitis and its correlation with symptoms. A cross-sectional study was conducted in 116 idiopathic rhinitis patients, and DAO activity, nasal peak inspiratory flow, and rhinitis severity were recorded. The prevalence of a DAO activity deficit was 41.38% (95%CI 0.33–0.50; p = 0.05). The DAO activity in patients with mild rhinitis was 52.93 ± 8.72 HDU/mL, in those with moderate rhinitis it was 120.33 ± 71.63 HDU/mL, and in those with severe rhinitis it was 92.58 ± 27.75 HDU/mL (p = 0.006). The NPIF in patients with a DAO activity deficit was 107.92 ± 34.05 L/min, compared to 72.35 ± 27.16 L/min in patients with normal enzymatic activity (p < 0.001), demonstrating a linear correlation between activity levels and nasal obstruction (−0.45; p < 0.001). Therefore, patients with a DAO deficiency and idiopathic rhinitis could present a milder disease course, because the repeated and continuous activation of TRPV1 led to a partial or total decrease in their response (desensitization). This new theory represents a different perspective for the study of idiopathic rhinitis and its relationship with TRPV1, with the regulation or modulation of the desensitization of TRPV1 being an important therapeutic target for patients with idiopathic rhinitis in the future.
Diamine Oxidase Activity Deficit and Idiopathic Rhinitis: A New Subgroup of Non-Allergic Rhinitis? / Mayo-Yanez, M.; Diaz-Diaz, A.; Calvo-Henriquez, C.; Lechien, J. R.; Vaira, L. A.; Figueroa, A.. - In: LIFE. - ISSN 2075-1729. - 13:1(2023), p. 240. [10.3390/life13010240]
Diamine Oxidase Activity Deficit and Idiopathic Rhinitis: A New Subgroup of Non-Allergic Rhinitis?
Vaira L. A.;
2023-01-01
Abstract
Idiopathic rhinitis represents more than 50% of non-allergic rhinitis, a heterogeneous group that involves the symptomatic inflammation of the nasal mucosa. The TRPV1 receptor of unmyelinated C-type neurons appears to be involved in its pathophysiology. Histamine, whose main catabolic enzyme is DAO, is one of the mediators that can activate this receptor. The failure of DAO causes an increase in the level of histamine in the body and, consequently, the activation of TRPV1. The objective was to investigate the existence of a DAO enzyme activity deficit in idiopathic rhinitis and its correlation with symptoms. A cross-sectional study was conducted in 116 idiopathic rhinitis patients, and DAO activity, nasal peak inspiratory flow, and rhinitis severity were recorded. The prevalence of a DAO activity deficit was 41.38% (95%CI 0.33–0.50; p = 0.05). The DAO activity in patients with mild rhinitis was 52.93 ± 8.72 HDU/mL, in those with moderate rhinitis it was 120.33 ± 71.63 HDU/mL, and in those with severe rhinitis it was 92.58 ± 27.75 HDU/mL (p = 0.006). The NPIF in patients with a DAO activity deficit was 107.92 ± 34.05 L/min, compared to 72.35 ± 27.16 L/min in patients with normal enzymatic activity (p < 0.001), demonstrating a linear correlation between activity levels and nasal obstruction (−0.45; p < 0.001). Therefore, patients with a DAO deficiency and idiopathic rhinitis could present a milder disease course, because the repeated and continuous activation of TRPV1 led to a partial or total decrease in their response (desensitization). This new theory represents a different perspective for the study of idiopathic rhinitis and its relationship with TRPV1, with the regulation or modulation of the desensitization of TRPV1 being an important therapeutic target for patients with idiopathic rhinitis in the future.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.