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Study shows promise in repairing damaged myelin
A scientific breakthrough provides new hope for millions of people living with multiple sclerosis. Researchers at OHSU have developed a compound that stimulates repair of the protective sheath that covers nerve cells in the brain and spinal cord.
The discovery, involving mice genetically engineered to mimic multiple sclerosis, published today in the journal JCI Insight.
“There are no drugs available today that will re-myelinate the de-myelinated axons and nerve fibers, and ours does that,” said senior author Tom Scanlan, Ph.D., professor of physiology and pharmacology in the OHSU School of Medicine.
Researching and riding for MS
Meredith Hartley is part of a team creating new possibilities for treating people with multiple sclerosis. The team of scientists and physicians recently discovered a compound that stimulates repair to the protective sheath surrounding neurons in the brain and spinal cord. Hartley, a postdoctoral researcher in physiology and pharmacology, conducts research in Tom Scanlan’s laboratory. Read more.
Highlighted publication: Valiyaveetil lab"Main-chain mutagenesis reveals intrahelical coupling in an ion channel voltage-sensor"
Membrane proteins catalyze the passage of information across biological membranes. Central to this function is their ability to undergo conformational changes in response to physiological stimuli. Backbone hydrogen bonds have long been proposed to play an important role in these conformational changes but, until now, technical challenges have prevented their investigation. In this study, the Valiyaveetil group (in collaboration with the Ahern group at U of Iowa) used advanced chemical biology approaches to investigate the role of backbone hydrogen bonds in the voltage sensing transmembrane helix of a eukaryotic potassium channel. The study provides key insights into the physiologically important process of voltage gating in ion channels and establishes a methodology for probing backbone hydrogen bonds, which opens new possibilities for investigating membrane proteins.
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