Disruptions favor alzheimer’s and parkinson’s, Study finds

In an International Research Collaboration Involving The University Medical Center Göttingen (UMG), Researchers have Produced the Most Complete Map to Date of How Long Different Proteins Persist In Many Tissues of the Body. Then Were Able to Identify a Mechanism That Increases The Stability of Proteins and Thus Favors Neurodegenerative Diseases Such As Alzheimer’s and Parkinson’s Disease. The results have been published in Cell.

Proteins Ensure That Human Cells Function and Are Viable. Proteins Are Formed to Perform a Specific Task in the Cell and Once This Task Has Been Completed, They Are Broken Down Again. If this process is disrupted, dissees such as parkinson’s or Alzheimer’s can develop.

BOTH DISEASES ARE CHARACTERIZED BY THE DESTRATION OF NERVE CELLS IN THE BRAIN AND ARE THERFORE REFERRED TO AS NEURODEGEGENERIVE DISEASES. While Parkinson’s Disease Leads to Movement Disorders Such As Trembling, Slowed Movements, Balance Problems and Stiffened Muscles, Alzheimer’s Disease Manifests in Increasing Memory Problems and Perceptual Disorders, Among Other Things.

In Both Cases, The Cause Is That Old And Damaged Proteins Are Not Broken Down Properly, Accumulate in the Cells and Clump Together. These Protein Clumps, Also Known AS AGGREGATES, CAN IN THE LONG BROKEN Down by the Body, and They Ensure That The Nerve Cells are gradually destroyed.

In an International Collaboration Involving The University Medical Center Göttingen (UMG), Dr. Eugenio F. Fornasiero, Group Leader at the Umg’s Department of Neuro- and Sensory Physology, and His US Colleagues from Yale University In New Haven, Connecticut, and St. Jude Children’s Research In Memphis Hospital, Tennessee, Have Produced the Most Complete Map to Date of How Long Different Proteins Persist in Many Tissues of the Body.

“This extensive data set is like a blueprint for Understanding How Different Organs Manage Their Proteins,” Says Dr. Fornasiero, One of the Study’s Last Authors. “We can See Which Proteins Are Turned Over Quickly in the Brain, For Example, And Which One Persist Longer – This Gives US Clues About Their Stability and Their Role In Neurodegenerative Diseases.”

The Researchers Discoved That a Mechanism That Switches Proteins “On” and “Off” Also Plays a Role in the Stabilization of Proteins: Protein Phosphrylation. In this process, phosphate groups are transfered to proteins, Which leads to the corresponding protein being switched on, ie, activated. Removing The Phosphate Groups Switches The Protein Off.

In the Brain Tissue of Mice Suffering from Alzheimer’s Disease, For Example, The Scientists Were Aple to Show That the Protein “Tau,” Which is Evaved in the Development of the Disease, Is Increasingly Phosphory in Right Sections. This incorses The Stability of the Tau Protein and Prolongs its Lifespan. This in turn promotes the formation of protein aggregates and the death of nerve cells.

“Understanding How PhosphoryLation Influences The Stability and Turnover of Proteins Could Help to Development New Therapeutic Strategies for the Treatment of Parkinson’s and Alzheimer’s Disease. For Example, by Preventing or Reversing Such Pathological Changes,” Says Fornasiero.

In Addition to Identifying Disease-Relevant Proteins, Understanding Protein Turnover and Its Regulation Also Helps to Identify Those Proteins That Are particularly Susceptible to Aging Processes. This also opens up new Avenues for Future Anti-Agging Therapies.

Provided by Universitätsmedizin Göttingen-Georg-August-Universität