Nmnat Enzyme May Halt Accumulation of Mutant Htt Protein Clumps in Nerve Cells, Study Shows

Nmnat Enzyme May Halt Accumulation of Mutant Htt Protein Clumps in Nerve Cells, Study Shows

Publication date: Oct 03, 2019

This post was originally published on this site Increasing the levels of a natural enzyme called nicotinamide mononucleotide adenylyltransferase – or Nmnat – halts the formation of mutant huntingtin (Htt) protein aggregates that build up in nerves cells in Huntington’s disease, a fruit fly study shows. -We discovered the neuroprotective role of a cellular ‘housekeeping’ enzyme in alleviating disease progression,” R. Grace Zhai, PhD, associate professor of molecular and cellular pharmacology at the University of Miami Miller School of Medicine and the study’s lead author, said in a press release. Huntington’s disease is characterized by mutations in the HTT gene, which results in the abnormal production and accumulation of mutated forms of the huntingtin (HTT) protein inside nerve cells, ultimately causing them to die. To learn more, researchers at the University of Miami Miller School of Medicine used a fruit fly model of Huntington’s disease with many characteristics that resemble those found in the human brain. Importantly, when the researchers engineered flies to express Nmnat only after the onset of Huntington’s disease, it significantly delayed the progression of neurodegeneration – -revealing the therapeutic potential of Nmnat-mediated neuroprotection at advanced stages of [the disease],” they said. -Our next step will involve screening drugs and compounds that could potentially increase Nmnat or enhance its ability to reduce the Htt aggregations that build up in Huntington’s disease,” Zhai said.

Concepts Keywords
Adhesive Autophagy
Autophagy Neuroprotection
Brain Neuron
Clustering Neurodegeneration
Enzyme Huntingtin
Frontotemporal Dementia Neuroscience
Fruit Fly Huntington’s disease
Gene Neurology
Genetic Disorders RTT
Huntingtin Medicine
Miami Branches of biology
Mitochondria Organ systems
Mutant Nerves Huntingtons disease
Nerve Disease
Nerve Cells Adhesive chemical properties
Neurodegeneration
Neurological
Neurons
Neuroprotection
Neuroprotective
Neurotransmitters
Parkinsonism
Pharmacology
PhD
PNAS
Progressive
Recycling
Synapses
Synaptic

Semantics

Type Source Name
gene UNIPROT CD40LG
gene UNIPROT SCYL1
gene UNIPROT TDRD7
disease DOID frontotemporal dementia
disease MESH frontotemporal dementia
gene UNIPROT MAPT
disease MESH genetic disorders
disease MESH death
gene UNIPROT SLC6A4
pathway BSID Release
gene UNIPROT PDC
disease MESH disease progression
drug DRUGBANK Nicotinamide Mononucleotide
gene UNIPROT SLC35G1
gene UNIPROT DESI1
gene UNIPROT HTT
gene UNIPROT NMNAT1
gene UNIPROT PTPN5

Similar

Original Article

Leave a Comment

Your email address will not be published. Required fields are marked *