Features | Partner Sites | Information | LinkXpress
Sign In
GLOBETECH PUBLISHING LLC
GLOBETECH MEDIA
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

Channels

Drug Discovery

view channel
Image: Star-like glial cells in red surround alpha-beta plaques in the cortex of a mouse with a model of Alzheimer\'s disease (Photo courtesy of Strittmatter laboratory/Yale University).

Experimental Cancer Drug Reverses Symptoms in Mouse Model of Alzheimer's Disease

An experimental, but clinically disappointing drug for treatment of cancer has been found to be extremely effective in reversing the symptoms of Alzheimer's disease (AD) in a mouse model.... Read more

Biochemistry

view channel
Image:  Model depiction of a novel cellular mechanism by which regulation of cryptochromes Cry1 and Cry2 enables coordination of a protective transcriptional response to DNA damage caused by genotoxic stress (Photo courtesy of the journal eLife, March 2015, Papp SJ, Huber AL, et al.).

Two Proteins Critical for Circadian Cycles Protect Cells from Mutations

Scientists have discovered that two proteins critical for maintaining healthy day-night cycles also have an unexpected role in DNA repair and protecting cells against genetic mutations that could lead... Read more

Business

view channel

NanoString and MD Anderson Collaborate on Development of Novel Multi-Omic Expression Profiling Assays for Cancer

The University of Texas MD Anderson Cancer Center (Houston, TX, USA) and NanoString Technologies, Inc. (Seattle, WA, USA) will partner on development of a revolutionary new type of assay—simultaneously profiling gene and protein expression, initially aiming to discover and validate biomarker signatures for immuno-oncology... Read more
 
Copyright © 2000-2015 Globetech Media. All rights reserved.