Transthyretin-Related Familial Amyloid Polyneuropathy: In the Light of New Developments


Cakar A. , Tekce H. D. , Deymeer F. , Serdaroglu P. O. , Parman Y. G.

TURKISH JOURNAL OF NEUROLOGY, vol.23, no.3, pp.105-111, 2017 (Journal Indexed in ESCI) identifier identifier

  • Publication Type: Article / Review
  • Volume: 23 Issue: 3
  • Publication Date: 2017
  • Doi Number: 10.4274/tnd.03206
  • Title of Journal : TURKISH JOURNAL OF NEUROLOGY
  • Page Numbers: pp.105-111

Abstract

Transthyretin-related familial amyloid polyneuropathy (TTR-FAP) is caused by gain-of-toxic-function of TTR, which dissociates from its native tetramer form to a monomer form and aggregates in several tissues and organs. Mutations in the TTR gene lead to this amyloidogenic transformation and cause autosomal dominant disease. TTR-FAP typically causes sensorimotor FAP accompanied by autonomic involvement, but considerable phenotypic diversity is noted between different mutation types. In the event of clinical suspicion, TTR gene sequencing and pathologic confirmation are the recommended paths to follow. Significant improvement has been achieved in treating the disease over the past 20 years, starting with liver transplantation, followed by tetramer stabilizers and TTR-lowering therapies. Although there are still some uncertainties in diagnosing and treating TTR-FAP, recent advances are promising, especially in the field of treatment.