Features | Partner Sites | Information | LinkXpress
Sign In
GLOBETECH PUBLISHING LLC
PZ HTL SA
GLOBETECH PUBLISHING LLC

Receptor May Help Spread of Alzheimer’s and Parkinson’s in Brain

By BiotechDaily International staff writers
Posted on 10 Sep 2013
Image: Electron micrograph shows clumps of corrupted tau protein outside a nerve cell. Scientists have identified a receptor that lets these clumps into the cell, where the corruption can spread. Blocking this receptor with drugs may help treat Alzheimer’s, Parkinson’s and other disorders (Photo courtesy of PNAS - Proceedings of the National Academy of Sciences of the United States of America).
Image: Electron micrograph shows clumps of corrupted tau protein outside a nerve cell. Scientists have identified a receptor that lets these clumps into the cell, where the corruption can spread. Blocking this receptor with drugs may help treat Alzheimer’s, Parkinson’s and other disorders (Photo courtesy of PNAS - Proceedings of the National Academy of Sciences of the United States of America).
Scientists have found the process in which corrupted, disease-causing proteins spread in the brain, potentially contributing to Alzheimer’s disease, Parkinson’s disease, and other brain-damaging disorders.

The research identifies a specific type of receptor and suggests that blocking it may help treat of these disorders. The receptors are called heparan sulfate proteoglycans (HSPGs). “Many of the enzymes that create HSPGs or otherwise help them function are good targets for drug treatments,” said senior author Marc I. Diamond, MD, a professor of neurology at the Washington University School of Medicine in St. Louis (MO, USA). “We ultimately should be able to hit these enzymes with drugs and potentially disrupt several neurodegenerative conditions.”

The study’s findings were published online August 2013 in the Proceedings of the National Academy of Sciences of the United States of America (PNAS). Over the 10 years, Dr. Diamond has gathered evidence that Alzheimer’s disease and other neurodegenerative disorders spread through the brain in a manner similar to conditions such as mad cow disease, which are caused by misfolded proteins known as prions.

Dr. Diamond and his colleagues have shown that a part of nerve cells’ inner structure known as tau protein can misfold into a formation called an amyloid. These corrupted versions of tau adhere to each other in clumps within the cells. Similar to prions, the clumps spread from one cell to another, seeding additional dispersal by causing copies of tau protein in the new cell to change into amyloids.

In the new study, first author Brandon Holmes, an MD/PhD student, demonstrated that HSPGs are necessary for binding, internalizing, and dispersing clumps of tau. When he genetically inactivated or chemically modified the HSPGs in cell cultures and in a mouse model, clumps of tau could not enter cells, thereby suppressing the spread of misfolded tau from cell to cell. Mr. Holmes also found that HSPGs are essential for the cell-to-cell spread of degraded forms of alpha-synuclein, a protein linked to Parkinson’s disease.

“This suggests that it may one day be possible to unify our understanding and treatment of two or more broad classes of neurodegenerative disease,” Dr. Diamond concluded. “We’re now sorting through about 15 genes to determine which are the most essential for HSPGs’ interaction with tau,” Mr. Holmes said. “That will tell us which proteins to target with new drug treatments.”

Related Links:
Washington University School of Medicine in St. Louis

comments powered by Disqus

Channels

Drug Discovery

view channel
Image: The new peptide offers a triple hormone effect in a single-cell molecule (Photo courtesy of Indiana University).

Tripeptide Drug Effectively Controls Metabolic Syndrome in Rodent Model

Promising results in reducing obesity and normalizing glucose metabolism obtained with a synthetic dipeptide drug have been enhanced by the addition of a molecule of a third hormone, glucagon.... Read more

Biochemistry

view channel

Blocking Enzyme Switch Turns Off Tumor Growth in T-Cell Acute Lymphoblastic Leukemia

Researchers recently reported that blocking the action of an enzyme “switch” needed to activate tumor growth is emerging as a practical strategy for treating T-cell acute lymphoblastic leukemia. An estimated 25% of the 500 US adolescents and young adults diagnosed yearly with this aggressive disease fail to respond to... Read more

Business

view channel

R&D Partnership Initiated to Reduce Development Time for New Drugs

nanoPET Pharma, GmbH (Berlin, Germany) signed an open-ended framework contract with the international pharmaceutical company Boehringer Ingelheim (Ridgefield, CT, USA). By developing customized contrast agents for research in both basic and preclinical studies, nanoPET Pharma will contribute to the enhancement of Boehringer... Read more
 
Copyright © 2000-2014 Globetech Media. All rights reserved.