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Press Release: Why nerve cells die

For over 100 years medical researchers have observed protein deposits, also called aggregates, in the brains of patients with neurodegenerative diseases like Alzheimer's, Parkinson's or Huntington's Disease as well as amyotrophic lateral sclerosis (ALS). These aggregates are suspected to contribute to the death of nerve cells, and play an important role in the progression of these debilitating diseases. Scientists from the Max Planck Institute of Biochemistry in Martinsried, led by Mark Hipp and SyNergy-PI Ulrich Hartl, have now shown that the location of protein aggregates strongly influences the survival of cells. While aggregates within the nucleus barely influence cellular function, deposits of identical proteins within the cytoplasm interfere with important transport routes between the nucleus and the cytoplasm. This results in a blockage of protein and RNA transport into and out of the nucleus. In the long run this can lead to the death of the affected cells, and progression of the disease. The results of these studies have now been published in the journal Science.


Image: To visualize protein aggregates
(red) under the microscope, they have to be stained previously.
The cellular nucleus was stained blue and the mRNA,
the construction manual for proteins, was stained green.
Source: Andreas Woerner, MPI of Biochemistry

Proteins consist of long chains of amino acids and function in cells like small machines. To be able to fulfill their function proteins have to assume a predetermined three-dimensional structure. In healthy cells there is a large variety of folding helpers and extensive quality control machinery. Misfolded proteins are either repaired or rapidly degraded. If this occurs inadequately, or not at all, proteins will clump together, form aggregates and harm the cell. 

Press release of the Max Planck Institute of Biochemistry

Proteine bestehen aus langen Aminosäureketten und funktionieren in Zellen wie kleine Maschinen. Um ihre Arbeit aufnehmen zu können, müssen die Proteine eine vorgegebene dreidimensionale Struktur annehmen. In gesunden Zellen gibt es eine Vielzahl von Faltungshelfern und eine umfangreiche Qualitätskontrolle. Falsch gefaltete Proteine werden entweder repariert oder schnell abgebaut. Geschieht dies nicht oder nicht ausreichend, können Proteine mit sich selbst oder anderen Proteinen zu Aggregaten verklumpen und die Zellen schädigen.

Pressemeldung des Max-Planck-Instituts für Biochemie