Articles by April M. Weissmiller in JoVE
التصوير في الوقت الحقيقي من محور عصبي نقل الكم دوت المسمى عامل التغذية العصبية في الخلايا العصبية الابتدائية Xiaobei Zhao1, Yue Zhou2, April M. Weissmiller1, Matthew L. Pearn3,4, William C. Mobley1, Chengbiao Wu1 1Department of Neurosciences, University of California, San Diego, 2School of Biomedical Engineering and Med-X Research Institute, Shanghai Jiao Tong University, 3Department of Anesthesiology, University of California, San Diego, 4VA San Diego Healthcare System نقل محور عصبي من عامل التغذية العصبية الدماغي، وهو عامل التغذية العصبية، هو أمر حاسم لبقاء وظيفة العديد من السكان العصبية. وتتميز بعض الاضطرابات التنكسية من اختلال هيكل محور عصبي وظيفة. أثبتنا التقنيات المستخدمة لدراسة الاتجار المباشر لQD-عامل التغذية العصبية في غرف ميكروفلويديك باستخدام الخلايا العصبية الأولية.
Other articles by April M. Weissmiller on PubMed
Enhanced β-secretase Processing Alters APP Axonal Transport and Leads to Axonal Defects Human Molecular Genetics. Nov, 2012 | Pubmed ID: 22843498 Alzheimer's disease (AD) is a neurodegenerative disease pathologically characterized by amyloid plaques and neurofibrillary tangles in the brain. Before these hallmark features appear, signs of axonal transport defects develop, though the initiating events are not clear. Enhanced amyloidogenic processing of amyloid precursor protein (APP) plays an integral role in AD pathogenesis, and previous work suggests that both the Aβ region and the C-terminal fragments (CTFs) of APP can cause transport defects. However, it remains unknown if APP processing affects the axonal transport of APP itself, and whether increased APP processing is sufficient to promote axonal dystrophy. We tested the hypothesis that β-secretase cleavage site mutations of APP alter APP axonal transport directly. We found that the enhanced β-secretase cleavage reduces the anterograde axonal transport of APP, while inhibited β-cleavage stimulates APP anterograde axonal transport. Transport behavior of APP after treatment with β- or γ-secretase inhibitors suggests that the amount of β-secretase cleaved CTFs (βCTFs) of APP underlies these transport differences. Consistent with these findings, βCTFs have reduced anterograde axonal transport compared with full-length, wild-type APP. Finally, a gene-targeted mouse with familial AD (FAD) Swedish mutations to APP, which enhance the β-cleavage of APP, develops axonal dystrophy in the absence of mutant protein overexpression, amyloid plaque deposition and synaptic degradation. These results suggest that the enhanced β-secretase processing of APP can directly impair the anterograde axonal transport of APP and are sufficient to lead to axonal defects in vivo.
Current Advances in Using Neurotrophic Factors to Treat Neurodegenerative Disorders Translational Neurodegeneration. 2012 | Pubmed ID: 23210531 Neurotrophic factors are best known for their roles in both development and continued maintenance of the nervous system. Their strong potential to elicit pro-survival and pro-functional responses in neurons of the peripheral and central nervous system make them good drug candidates for treatment of a multitude of neurodegenerative disorders. However, significant obstacles remain and need to be overcome before translating the potential of neurotrophins into the therapeutic arena. This article addresses current efforts and advances in resolving these challenges and provides an overview of roadmaps for future translational research and neurotrophin-based drug developments.