Study shows promise in repairing damaged myelin

Tom Scanlan and Meredith Hartley discuss research

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.

Upcoming events

Two basic science departments to join

SoM leverages expertise, technology and fresh investment to form new, expanded department

Dean Sharon Anderson approved a proposal to combine two basic science departments in the OHSU School of Medicine to form a new, expanded department starting July 1.

The Department of Biochemistry and Molecular Biology and the Department of Physiology and Pharmacology will join together to leverage faculty specialties and technology. Read more.

Members of the Department of Biochemistry and Molecular Biology and the Department of Physiology and Pharmacology

Highlighted publication: Valiyaveetil lab

"Investigation of the allosteric coupling mechanism in a glutamate transporter homolog via unnatural amino acid mutagenesis"

Glutamate transporters harness ionic gradients for the concentrative uptake of glutamate. Normal function of glutamate transporters is required for rapid removal of glutamate from the synapse, which is required for efficient neurotransmission and for preventing excitotoxicity. A key question in glutamate transporters is the mechanism by which the ionic gradient is coupled to glutamate uptake. Recent studies from the Valiyaveetil lab used unnatural amino acid mutagenesis to probe this mechanism and their studies now provide a molecular sequence for the events in the coupled binding of sodium and substrate to the glutamate transporter.