Familial Amyloid Polyneuropathy: A Proposal for an Epidemiological Study Through the Creation of a Virtual Platform


  • Arielle Kirmse
  • Camila Castelo Branco Pupe
  • Karoline Queiroz Muniz De Medeiros
  • Pamela Passos
  • Osvaldo J. M. Nascimento






Amyloidosis are characterized by mutations in the gene coding for transthyretin (TTR), located on chromosome 18. TTR is a set of four 127-aminoacid polypeptides structured as homotetrameric protein of 56 kDa with a secondary ß sheet structure. It plays the role of thyroxin (T4) carrier, and has a binding
domain for retinol (vitamin A). It is synthesized in the liver, although a small quantity is also produced by the choroid plexus, and retinal cells. Mutations of this gene result in loss of tetramer stability. Insoluble amyloid fibrils (AF) are formed and deposited in tissues and organs. The abnormal aggregation of
TTR protein trigger several syndromes, such as familial amyloid polyneuropathy (FAP-TTR), cardiomyopathies (CMP), and senile systemic amyloidosis (SSA). It is estimated there are 5,000 to 10,000 cases of FAP-TTR globally. Objective: The study intends to develop an online platform for the diagnosis of FAP-TTR. The aim is to facilitate the diagnosis process and promote a tool for epidemiological study.
Methods: The project was based on a literature review featuring clinical and epidemiological evidence for the development of a practical platform (applied research). Results: It was elaborated a platform containing a questionnaire
to allow a more dynamic, cheaper, and efficient operation, mediated by a better characterization of the disease to enable its early diagnosis. Conclusion: The platform might become a valuable resource for the characterization, diagnosis, and future epidemiological study of FAP-TTR.