“Amyloid” diseases: Can we treat them? by Dr. Arthur Horwich, MD

Arthur Horwich, MD, Sterling Professor, Genetics,Yale University & Investigator, Howard Hughes Medical Institute. 8 – 9:00 a.m., Auditorium E. Sponsors: MD/Ph, DHMC,& Geisel

May 2, 2014
8 am - 9 pm
Location
Aud E, Rubin, DHMC
Sponsored by
Geisel School of Medicine
Audience
Public
More information
Margaret Kerouac

Sponsored by MD/PhD, DHMC, & Geisel

Objectives – Participants will be able to:

  1. Understand the notion that particular degenerative conditions, affecting specific cell populations, involve aggregation of particular proteins, sometimes in the form of classic beta-sheet rich amyloids.
  2. Comprehend that in the case of neurodegenerative “amyloid” diseases, it is likely that soluble oligomeric protein species are the most neurotoxic, as compared with the aggregates/inclusions themselves.
  3. Know that a variety of treatment approaches are under trial, including: BACE inhibitors (for Alzheimer's); antisense oligonucleotides aimed at gene shutoff (for a number of conditions, including polyglutamine diseases - SCA2 and Huntington); unfolded protein response inhibitors (prion disease e.g.); and native state stabilizers that prevent a normal native protein from misfolding into an amyloid state (transthyretin amyloidosis).

Arthur Horwich, MD

Dr. Horwich graduated from Brown University’s six year medical program, trained in Pediatrics at Yale-New Haven Hospital, carried out postdoctoral work in the Tumor Virology Laboratory at the Salk Institute, and returned to the Yale University School of Medicine training in Medical Genetics.  He then joined the Genetics Department where he has been an attending and investigator for the past 30 years.  In the course of studying the biogenesis of the mitochondrial urea cycle enzyme OTC, he uncovered a protein folding activity in the mitochondrial matrix, found to be mediated by a double ring assembly dubbed heat shock protein 60, and, using a variety of techniques and with a collective of collaborators, over a period of 20 years, as they worked on the mechanism of chaperonin-mediated protein folding.  His group is now pursuing the mechanism of SOD1-linked ALS, using a mouse model, to understand the progressive motor defects that occur in ALS, with a view to seeking therapy.

Location
Aud E, Rubin, DHMC
Sponsored by
Geisel School of Medicine
Audience
Public
More information
Margaret Kerouac