Specific IgE Assay for Respiratory Allergens in Patients with Atopy in Ahvaz, Iran.

BACKGROUND: The frequency of sensitization to respiratory allergens is different in various geographical regions. OBJECTIVE: To determine the level of specific IgE to respiratory allergens in patients with atopy in Ahvaz, Iran. METHODS: In this retrospective cross-sectional study, the total and specific IgE data were recorded for 408 patients with allergic rhinitis and asthma referred to allergy diagnostic laboratory in Ahvaz from 2014 to 2017. The specific IgE was measured for nine respiratory allergens including Salsola kali, Triticum aestivum, Lolium perenne, Salix caprea, Prosopis juliflora, Dermatophagoides farinae, Aspergillus fumigatus, Alternaria alternate, Blatella germani using the ImmunoCAP system (Thermofisher-Phadia, Uppsala, Sweden) in referred patients. RESULTS: The median (IQR) age of participants was 15.5(27) years. The most common outdoor aeroallergens were Salsola kali (42.9%), Lolium perenne (32.2%), and Salix caprea (28.2%) while Dermatophagoides farina (21.1%) and Blatella germanica (20.6%) were the most dominant indoor sensitizers. Sensitization to at least one allergen was found in 57.4% of the patients. The prevalence of IgE sensitization to all respiratory allergens was higher in males. The prevalence of IgE sensitization to molds including Aspergillus fumigatus and Alternaria alternata significantly decreased with increased age. CONCLUSION: The pattern of allergen-specific IgE showed that Salsola Kali and Lolium perenne are the most common aeroallergens in allergic patients. This finding demonstrates the high frequency of IgE sensitization to outdoor allergens in the southwest of Iran.

Disruption of mitochondrial membrane integrity induced by amyloid aggregates arising from variants of SOD1.

Amyotrophic lateral sclerosis (ALS) is a fatal progressive neurodegenerative disorder selectively affecting motor neurons; 90% of the total cases are sporadic, but 2% are associated with mutations in the gene coding for copper-zinc superoxide dismutase (SOD1). The causes of motor neuron death in ALS are poorly understood in general, but for SOD1-linked familial ALS (fALS), aberrant oligomerization of SOD1 mutant proteins has been strongly implicated. A growing body of evidence suggests that fALS-causing mutations destabilize the native structure of SOD1, leading to aberrant protein interactions for aggregation. In this work, we show that wild-type human SOD1 and two of its mutants (D101N, G72S) form amyloid like fibrils under destabilizing condition (in the presence of KSCN 0.2 M and DTT 50 mM) at 37 °C, pH 7.4. The formation of the aggregates was monitored by their ability to enhance the fluorescence of Thioflavin T (ThT) and their morphology was assessed by transmission electron microscopy (TEM). Furthermore, interaction of SOD1 aggregates with mitochondrial membrane of rat brain, as an in vitro biological model, with the aim of gaining an insight into possible mechanism of cytotoxicity at the membrane level was verified. Release of mitochondrial enzyme, malate dehydrogenase (MDH), upon exposure to SOD1 aggregates demonstrates that these aggregates could affect membrane permeability.