Skip to main content
padlock icon - secure page this page is secure

Neurodegeneration in familal amyloidotic polyneuropathy

Buy Article:

$52.00 + tax (Refund Policy)

Summary

1. Familial amyloid polyneuropathies (FAP) constitute a group of inherited amyloidoses that affect peripheral nerves. One common form of FAP is caused by transthyretin (TTR) misfolding and deposition in the peripheral nervous system, leading to neuronal toxicity and death.

2. The molecular mechanisms responsible for this toxicity are unclear; however, there is good biochemical and histopathological evidence that the toxicity of TTR mutations is correlated to their aggregation state. In addition, neuronal calcium dysregulation is a mechanism that has been suggested to drive the pathogenesis of FAP.

3. Amyloidogenic TTR mutations cause significant calcium influx via L‐type calcium channels in neuronal cell lines, while in primary sensory neurons, TTR mediates a calcium influx via a novel mechanism of transient receptor potential melanostatin (TRPM8) and voltage‐gated sodium and calcium channel activation.

4. Significantly, calcium dysregulation is a pathological hallmark of other neurodegenerative diseases involving amyloidosis, for example Alzheimer’s disease, and this mechanism could explain the molecular events that drive amyloid toxicity in other neurodegenerative diseases.
No References
No Citations
No Supplementary Data
No Article Media
No Metrics

Document Type: Research Article

Affiliations: Laboratory of Molecular Neurobiology, Menzies Research Institute Tasmania, University of Tasmania, Hobart, Tasmania, Australia

Publication date: August 1, 2012

  • Access Key
  • Free content
  • Partial Free content
  • New content
  • Open access content
  • Partial Open access content
  • Subscribed content
  • Partial Subscribed content
  • Free trial content
Cookie Policy
X
Cookie Policy
Ingenta Connect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more