KineMed, CHDI Foundation Extend Huntington’s Disease Collaboration
News May 23, 2014
KineMed, Inc. and CHDI Foundation, Inc. announce an extension of their Huntington’s disease (HD) collaboration, which aims to evaluate potentially therapeutic interventions.
“We are delighted to continue our collaboration with CHDI in an area that leverages our capabilities to understand the biology of neurodegenerative diseases and monitor potential therapeutically beneficial interventions” said Dr. Patrizia Fanara, Vice President Neuroscience Kinemed.
The initial study identified deficits in microtubule dynamics and altered protein kinetics in the cerebrospinal fluid (CSF) of several HD models. Ongoing work will look to rescue these changes by lowering expression of huntingtin – the protein that causes HD - through an interventional therapeutic approach. The aim is to identify pharmacodynamic biomarkers that can be used in clinical trials; the continuation of the collaboration will allow the characterization of additional CSF protein markers, increasing the chance of success.
“Extending our collaboration will further build on the advances we’ve made through KineMed’s expertise and technology” said Jonathan Bard, PhD, Director, Molecular Pharmacology at CHDI. “By broadening the scope of our exploration we aim to identify biomarkers that can determine target engagement and translate from preclinical models to the clinic.”
There are currently no therapeutics approved that can slow the progression of HD, an inherited neurodegenerative disorder that affects about 30,000 people in the United States, with up to 150,000 additionally at risk of developing the disease. The clinical signs of disease are behavioral, cognitive, and motor impairments that, over the course of the disease, significantly reduce the individual's quality of life and ultimately cause death within 15 to 25 years of overt motor symptom onset.
Decoding the 3-D Structure of HuntingtinNews
Mutations on a single gene, the huntingtin gene, are the cause of Huntington's disease. They lead to an incorrect form of the correspondent protein. With the help of cryo-electron microscopy, researchers have now decoded the three-dimensional, molecular structure of the healthy human huntingtin protein.READ MORE