Features Partner Sites Information LinkXpress
Sign In
Demo Company

Treatment of Parkinson's Disease May Depend on Augmented Enzyme Activity

By BiotechDaily International staff writers
Posted on 07 Jul 2009
Print article
A naturally occurring brain enzyme has been identified that promotes the breakdown of the toxic protein clumps that characterize familial Parkinson's disease (PD) and some sporadic forms of the disease.

Dominantly inherited mutations in the leucine-rich repeat kinase 2 gene (LRRK2) are the most common cause of familial PD and have also been identified in individuals with sporadic PD. Although the exact cellular function of LRRK2 remains unknown, most PD-linked mutations appear to be toxic to cells in culture via mechanisms that depend on the kinase activity of LRRK2 or on the formation of cytoplasmic inclusions.

Investigators at the University of Texas Southwestern Medical Center (Dallas, USA) reported in the June 17, 2009, online edition of the journal Public Library of Science (PLoS) One that they had identified an E3 ubiquitin ligase known as CHIP, which physically associated with LRRK2. CHIP regulated the cellular abundance of LRRK2 by forming a complex with LRRK2 and another protein; Hsp90. CHIP regulated LRRK2 through a process of ubiquitination and proteasome-dependent degradation.

"CHIP may be a useful therapeutic target for treatments to break down LRRK2 in people with Parkinson's," said senior author Dr. Matthew Goldberg, assistant professor of neurology and psychiatry at the University of Texas Southwestern Medical Center. "Our next step is to identify cellular mechanisms that signal LRRK2 to be degraded by CHIP or by other mechanisms. Because LRRK2 mutations are believed to cause Parkinsonism by increasing the activity of LRRK2, enhancing the normal mechanisms that target LRRK2 for degradation by CHIP may be therapeutically beneficial."
"There are currently enormous efforts to identify potential therapies based on inhibiting this mutated protein," said Dr. Goldberg. "Our paper is a major advance because we identify a protein that binds to the mutated protein and promotes its breakdown."

Related Links:
University of Texas Southwestern Medical Center

Print article



view channel
Image: A partially completed three-dimensional printed airway from nostril to trachea with fine structure of the nasal cavity showing (Photo courtesy of Dr. Rui Ni, Pennsylvania State University).

The Structure of the Nasal Cavity Channels Food Smells into the Nose and Avoids the Lungs

Three-dimensional printing technology was used to create a model of the nasal cavity that enabled researchers to demonstrate why the smell of food goes into the nose rather than down into the lungs.... Read more


view channel

Molecular Light Shed on “Dark” Cellular Receptors

Scientists have created a new research tool to help find homes for orphan cell-surface receptors, toward better understanding of cell signaling, developing new therapeutics, and determining causes of drug side-effects. The approach may be broadly useful for discovering interactions of orphan receptors with endogenous, naturally... Read more

Lab Technologies

view channel
Image:  The BioSpa 8 Automated Incubator (Photo courtesy of BioTek Instruments).

Smart Incubator System Automates Live Cell Assay Operations

A new instrument that automates laboratory workflow by linking microplate washers and dispensers with readers and imaging systems is now available for biotech and other life sciences researchers.... Read more


view channel

Purchase of Biopharmaceutical Company Will Boost Development of Nitroxyl-Based Cardiovascular Disease Drugs

A major international biopharmaceutical company has announced the acquisition of a private biotech company that specializes in the development of drugs for treatment of cardiovascular disease. Bristol-Myers Squibb Co. (New York, NY, USA) has initiated the process to buy Cardioxyl Pharmaceuticals Inc. (Chapel Hill, NC, USA).... Read more
Copyright © 2000-2015 Globetech Media. All rights reserved.