Surfactant Protein A Expression in Chronic Rhinosinusitis and Atrophic Rhinitis

Abstract

Introduction Surfactant protein A (SP-A) exhibits antimicrobial properties and interacts with a variety of respiratory tract pathogens. Objective The objective of this study was to detect the presence of SP-A and measure its alterations in chronic rhinosinusitis (CRS) and primary atrophic rhinitis (PAR) versus healthy controls. Methods Inferior turbinate and sinus mucosal biopsies were taken from 30 patients with CRS, 30 patients with PAR, and 20 healthy controls. Immunohistochemical staining for SP-A and polymerase chain reaction (PCR) amplification of SP-A messenger RNA were performed on nasal tissue samples. Results Immunostaining localized SP-A to the mucosa and submucosal glands in CRS specimens but failed to localize it in PAR specimens. Quantitative PCR showed a high, statistically significant increase in the SP-A levels of patients with CRS when compared with controls (p < 0.0001) and also demonstrated a significant reduction of SP-A in patients with PAR compared with controls (p < 0.005). Conclusion SP-A is significantly increased in CRS and decreased significantly in PAR and appears to be expressed by respiratory epithelial cells and submucosal glandular elements of the sinonasal mucosa. The potential therapeutic applications of surfactant in the enhancement of mucociliary clearance need to be studied.

Airway Epithelial Dynamics in Allergy and Related Chronic Inflammatory Airway Diseases

“…Tipirneni et al (2018) identified that dynamic mucus strand velocities from submucosal glands, a major component of mucociliary clearance, were significantly decreased in CRS. Surfactant protein A gene expression has been shown to be increased in CRS and decreased in primary atrophic rhinitis (El-Anwar et al, 2015). In overview, CRS is commonly associated with mucociliary dysfunction.…”

Candidate genes of idiopathic pulmonary fibrosis: current evidence and research

“…It may interact with pathogen-associated molecular patterns anchored on membranes via the calcium-dependent carbohydrate-binding domains. 33 SP-A has been associated with SP-D in immune cells, in which it activates various cellular functions and acts as an opsonin in the modulation of macrophage phagocytosis and the production of reactive oxygen species. 34 Experimental data showed that the expression of mutant proteins increased the transcription of a BiP-reporter construct, expression of BiP protein, and production of an ER stress-induced XBP-1-spliced product.…”