Asthma remains one of the most common respiratory diseases in both children and adults affecting up to 10% of the US population. Asthma is characterized by persistent symptoms, airway inflammation, airflow limitation and frequent exacerbations. Eosinophils are a key immune cell present in a large majority of asthmatics and their presence and dysregulation are clinically associated with more severe asthma. Surfactant protein A (SP-A) provides a first-line of defense in pulmonary innate immunity by virtue of its role in pathogen opsonization. SP-A is known to specifically bind to (Mp), a pathogen associated with asthma exacerbations, and functions to attenuate Mp pathogenicity and abrogate lung inflammation. In addition, SP-A has been shown to inhibit Mp-induced eosinophil peroxidase (EPO) release, a toxic product that can compromise the integrity of the delicate airway epithelia. We have determined that genetic variation in SP-A2 at position 223 that results in a glutamine (Q) to a lysine (K) substitution alters the ability of SP-A to inhibit EPO release and may offer a mechanistic explanation as to why some SP-A extracted from subjects with asthma is unable to carry out normal immune regulatory functions.
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| http://dx.doi.org/10.4172/2155-9899.1000553 | DOI Listing |
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