Sexual dysfunction in cervical dystonia and blepharospasm

M Marek,1 M Grobe-Einsler,1 JR Bedarf,1 B Wabbels,2 S Paus1 1Department of Neurology, University of Bonn, Bonn, Germany; 2Department of Ophthalmology, University of Bonn, Bonn, Germany Background: Sexual dysfunction is a frequent, yet underrated, symptom of neurological disease. While knowledge of non-motor comorbidity in focal dystonia is growing rapidly, there is no information on the prevalence of sexual dysfunction in cervical dystonia (CD) or blepharospasm (BL). Methods: In this controlled study, we examined sexual dysfunction in 65 patients with CD and 54 patients with BL by the Arizona Sexual Experience Scale, a validated self-rating scale. Results: Sexual dysfunction was significantly higher in CD patients (45%) than in controls (24%), and frequent in BL (39%). Interestingly, variables of dystonia such as disease duration or severity did not influence sexuality; yet, 23% of CD patients ascribed worsening of their sexual life to dystonia. Symptoms of depression were identified as the most important predictors for sexual dysfunction, followed by age, and personal status (single). Conclusion: Our observations establish sexual dysfunction as a frequent non-motor symptom in CD and BL that is perceived as a burden. It should be considered when investigating patients with adult-onset focal dystonia. Keywords: dystonia, cervical dystonia, blepharospasm, sexual dysfunction, depression&nbsp

Identification of amyloidogenic proteins in the microbiomes of a rat Parkinson's disease model and wild‐type rats

Cross seeding between amyloidogenic proteins in the gut is receiving increasing attention as a possible mechanism for initiation or acceleration of amyloid formation by aggregation‐prone proteins such as αSN, which is central in the development of Parkinson's disease (PD). This is particularly pertinent in view of the growing number of functional (i.e., benign and useful) amyloid proteins discovered in bacteria. Here we identify two amyloidogenic proteins, Pr12 and Pr17, in fecal matter from PD transgenic rats and their wild type counterparts, based on their stability against dissolution by formic acid (FA). Both proteins show robust aggregation into ThT‐positive aggregates that contain higher‐order β‐sheets and have a fibrillar morphology, indicative of amyloid proteins. In addition, Pr17 aggregates formed in vitro showed significant resistance against FA, suggesting an ability to form highly stable amyloid. Treatment with proteinase K revealed a protected core of approx. 9 kDa. Neither Pr12 nor Pr17, however, affected αSN aggregation in vitro. Thus, amyloidogenicity does not per se lead to an ability to cross‐seed fibrillation of αSN. Our results support the use of proteomics and FA to identify amyloidogenic protein in complex mixtures and suggests that there may be numerous functional amyloid proteins in microbiomes