Metals in ALS TDP-43 Pathology.

Amyotrophic lateral sclerosis (ALS), Alzheimer's disease, Parkinson's disease and similar neurodegenerative disorders take their toll on patients, caregivers and society. A common denominator for these disorders is the accumulation of aggregated proteins in nerve cells, yet the triggers for these aggregation processes are currently unknown. In ALS, protein aggregation has been described for the SOD1, C9orf72, FUS and TDP-43 proteins. The latter is a nuclear protein normally binding to both DNA and RNA, contributing to gene expression and mRNA life cycle regulation. TDP-43 seems to have a specific role in ALS pathogenesis, and ubiquitinated and hyperphosphorylated cytoplasmic inclusions of aggregated TDP-43 are present in nerve cells in almost all sporadic ALS cases. ALS pathology appears to include metal imbalances, and environmental metal exposure is a known risk factor in ALS. However, studies on metal-to-TDP-43 interactions are scarce, even though this protein seems to have the capacity to bind to metals. This review discusses the possible role of metals in TDP-43 aggregation, with respect to ALS pathology.

Recurrent respiratory infections and unusual radiology: a woman with Kartagener's syndrome.

A 39-year-old woman with known situs inversus and a medical history of asthma had been suffering from recurring bronchial pneumonias and sinusitis for as long as she could remember. After being treated several times with antibiotics due to the frequent respiratory infections and after a CT scan that showed bilateral bronchiectasis, she was referred to the department of respiratory diseases, where another confirming X-ray and a bronchoscopy were performed based on a suspicion of Kartagener's syndrome.