Current Students

Neuroscience Research Day 2014

Thank you to all the students, faculty members, and volunteers who made Neuroscience Research Day 2014 a great success. It truly was a celebration of student research in neuroscience!

The keynote lecture was presented by Dr. Lawrence Steinman from the Stanford School of Medicine and recipient of the Charcot Prize for Lifetime Achievement in MS.

Keynote title: A beneficial role for amyloid structures in neuroinflammation.

Abstract: The amyloid-forming proteins tau, αB crystallin, and amyloid P protein are all found in lesions of multiple sclerosis (MS). Our previous work established that amyloidogenic peptides from the small heat shock protein αB crystallin (HspB5) and from amyloid β fibrils, characteristic of Alzheimer's disease, were therapeutic in experimental autoimmune encephalomyelitis (EAE), reflecting aspects of the pathology of MS. To understand the molecular basis for the therapeutic effect, we showed a set of amyloidogenic peptides composed of six amino acids, including those from tau, amyloid β A4, major prion protein (PrP), HspB5, amylin, serum amyloid P, and insulin B chain, to be anti-inflammatory and capable of reducing serological levels of interleukin-6 and attenuating paralysis in EAE. The chaperone function of the fibrils correlates with the therapeutic outcome. Fibrils composed of tau 623-628 precipitated 49 plasma proteins, including apolipoprotein B-100, clusterin, transthyretin, and complement C3, supporting the hypothesis that the fibrils are active biological agents. A second independent mechanism has been discovered whereby uptake of amyloid fibrils induces a type 1 interferon response. This second mechanism is only a portion of the emerging story. In summary, amyloid fibrils thus may provide benefit in MS and other neuroinflammatory disorders.