Five recent Parkinson’s disease drug target discoveries

Five recent Parkinson’s disease drug target discoveries

Publication date: Sep 10, 2019

The research team used cutting-edge imaging techniques to find that Lewy bodies in Parkinson’s disease brains contain α-synuclein protein aggregates, known as amyloid fibrils, that can propagate through the brain.

-Our work follows on from in vitro findings that aggregates of α-synuclein that can propagate through the brain have a cross-β structure,” says lead author of the study Dr Hideki Mochizuki.

The study, using mouse models, has potential therapeutic applications for Parkinson’s disease in humans, according to the researchers.

According to the authors, the -data provide the basis for understanding sex differences in α-synuclein homeostasis and the development of therapeutic approaches to treating men and postmenopausal women,” with Parkinson’s disease.

A study conducted by Oregon Health & Science University, US suggests that Lewy bodies cause problems when they pull α-synuclein out from the nucleus of brain cells.

Using mice models and post-mortem brain tissue from humans, the researchers found that the α-synuclein repair DNA breaks.

The role of α-synuclein in DNA restoration could therefore be crucial in preventing cell death, but this function may be lost in brain diseases such as Parkinson’s, leading to the widespread death of neurons.

The team revealed that the α-synuclein protein is rapidly recruited to the site of DNA damage in the neurons of mice.

According to the researchers, the results suggest that α-synuclein plays a crucial role in binding broken strands of DNA within the cell’s nucleus.

The researchers say that their findings could lead to the development of methods to deliver α-synuclein proteins into the nucleus of cells, or design replacements for its function.

Concepts Keywords
Active Ingredient Peripheral membrane proteins
Amyloid Neuropathology
Amyloidosis Lewy body dementia
Astrocytes Proteins
Brain Branches of biology
Brain Diseases Parkinsons disease
Chain Reaction Chemical complexes
Clinical Trials Imaging
Clumped Systemic amyloidosis
Cross Drug development
Cytoplasm RTT
Denmark Parkinson’s disease
Drug Development Amyloid
Drug Target Synuclein
Energy
Fibrils
Germany
Gero
Glucose
Glycolysis
Harvard
Heinrich Heine
Homeostasis
Japan
Lewy Bodies
Metabolic Pathway
Metabolise
Metabolism
Mice
Monomer
Monomers
Motor Skills
Nerve Tissue
Neurological Diseases
Neurology
Neurons
Neuropathological
Nucleus
Oestrogen
Oregon
Osaka University
Parkinson
PhD
Post Mortem
Postmenopausal
Russia
Salamanca
Small Molecule
Spain
Vivek
Vivo

Semantics

Type Source Name
gene UNIPROT PFKFB3
drug DRUGBANK Dextrose unspecified form
disease MESH amyloidosis
disease DOID amyloidosis
disease MESH rare diseases
disease MESH death
pathway BSID Glucose metabolism
pathway BSID glycolysis
pathway BSID Glycolysis
disease MESH development
gene UNIPROT PLXNA3
disease MESH men
gene UNIPROT MAP6
gene UNIPROT DESI1
gene UNIPROT SLC35G1
disease MESH brain diseases
gene UNIPROT PDC

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