Chris Patil of Ouroboros set down some notes earlier this week on the annual meeting of the Larry L. Hillblom Foundation, one of a number of non-profit organizations to fund research into the biochemistry of aging.
Bob Hughes, Pankaj Kapahi, Simon Melov and Gordon Lithgow (Buck Institute) gave a group talk under the umbrella topic “Chemical biology of aging” (we heard a bit about this at last year’s meeting). Bob introduced a screen for small molecules that extend lifespan in simple model system; the goal is to screen 100,000 compounds, identify drugs that increase longevity in both yeast and worms, and then test these molecules in mice.
Glabe’s group [has] been developing anti-amyloid antibodies, some of which [recognize] common features of amyloid aggregates formed by many different types of protein (e.g., [amyloid-beta] but also alpha-synuclein, IAPP, and other peptides involved in aggregation-based diseases [such as Alzheimer's, Parkinson's, and so forth]). These reagents will be useful in research but also potentially as therapies against multiple age-related illnesses.
Ken Nakamura (UCSF) is studying Parkinson’s disease in a refreshingly original way: he has developed ways to monitor alpha-synuclein [in] live cells, using fusion with fluorescent proteins. The pathological protein aggregates end up associating with membranes, including mitochondria - which then fragment, potentially contributing to [cell damage and death].
As you might guess from the above items, many age-related conditions are marked by a build-up of errant, damaging proteins - such as alpha-synuclein for Parkinson's and amyloid for Alzheimers. This protein aggregation may or may not be sufficiently close to the root cause of an age-related disease for removal of the protein to be a viable treatment, but we're going to find out during the next few years. The development of therapies aimed at soaking up the most common aggregates - or turning the immune system to destroy them - is advancing rapidly.