Related Experiment Video
Updated: May 10, 2026
05:48
Rapid Generation of Amyloid from Native Proteins In vitro
Published on: December 5, 2013
[Amyloid polyneuropathies--biochemical and genetic aspects]
1Biochimie et génétique moléculaire, Centre hospitalier Cochin, 75679 Paris cedex 14. marc.delpech@inserm.fr
Bulletin De L'Academie Nationale De Medecine
|July 3, 2013
Summary
Familial amyloid polyneuropathies (FAP) are inherited diseases caused by transthyretin gene mutations. New drugs targeting tetramer destabilization offer hope for treatment beyond liver transplantation.
Area of Science:
- Genetics and Molecular Biology
- Neurology
- Biochemistry
Context:
- Familial amyloid polyneuropathies (FAP) are frequent, severe, autosomal dominant hereditary amyloidoses.
- Mutations in transthyretin, Al-apoliprotein, gelsolin, or beta-2 microglobulin genes cause FAP.
- Transthyretin protein structure and function are crucial in FAP pathogenesis.
Purpose:
- To review the genetic basis and molecular mechanisms of FAP.
- To explore the variability in FAP presentation and underlying factors.
- To discuss the development of novel therapeutic strategies for FAP.
Summary:
- Over 120 transthyretin gene variations exist, with ~80% being pathogenic.
- Mutations destabilize the transthyretin tetramer, leading to misfolded monomers and amyloid fibril formation.
- Mutation spectrum and clinical variability differ significantly across populations.
Impact:
- Understanding FAP mechanisms aids in developing drugs that inhibit transthyretin tetramer destabilization.
- These novel therapies aim to replace liver transplantation as the primary curative treatment.
- Improved FAP treatments could significantly enhance patient outcomes and quality of life.
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