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Other Common Peripheral Neuropathies
Published in Maher Kurdi, Neuromuscular Pathology Made Easy, 2021
Amyloid neuropathy is defined as widespread amyloidosis that affects multiple nerves. It could be familial such as familial amyloid polyneuropathy (FAP) or non-familial (primary or secondary subtypes). FAP is associated with apolipoprotein Ig-light chain. It usually occurs as an isolated neuropathy. Primary amyloidosis occurs in 50% of cases and is associated with paraprotein deposition and underlying plasma cell diseases such as multiple myeloma. The clinical diagnosis is always established before the biopsy. Patients may present with painful symmetrical distal sensorimotor neuropathy associated with muscle weakness. Findings of monoclonal free-light chain or plasma cells in bone marrow biopsy and urinary test are suggestive for primary amyloidosis. Secondary amyloidosis is the rarest causative variant of amyloid neuropathy because it is not always present with peripheral neuropathy. Secondary amyloidosis is commonly associated with systemic chronic inflammatory diseases.
Peripheral Autonomic Neuropathies
Published in David Robertson, Italo Biaggioni, Disorders of the Autonomic Nervous System, 2019
A review of 86 patients with peripheral neuropathy showed autonomic disturbances in 45%. This excluded peripheral neuropathy due to diabetes mellitus, toxic causes and the Guillain-Barre’ syndrome, where the frequency of autonomic disturbances was 41%. On the other hand, in familial amyloid polyneuropathy and in thallium neuropathy, autonomic dysfunction was present in all patients and in 80% of those with causalgia (Kuroiwa et al., 1986).
Upregulation of the Extracellular Matrix Remodeling Genes, Biglycan, Neutrophil Gelatinase-Associated Lipocalin and Matrix Metalloproteinase-9 in Familial Amyloid Polyneuropathy
Published in Gilles Grateau, Robert A. Kyle, Martha Skinner, Amyloid and Amyloidosis, 2004
M. M. Sousa, J.B. Amaral, A. Guimarães, M. J. Saraiva
In the peripheral nervous system (PNS) of familial amyloid polyneuropathy (FAP) patients, transthyretin (TTR) aggregates and fibrils occur extracellularly; in latter stages of disease progression, nerves present complete axonal loss and endoneurial contents are replaced by amyloid, collagen, Schwann cells and fibroblasts. Changes in proteoglycan type and distribution could account for the derangement of collagen and the altered physical properties of tissues with TTR deposition; however, information is lacking concerning the molecular events that underlie tissue remodelling in FAP. The identification of genes differentially expressed during the course of FAP is needed. However, the amount of mRNA that is possible to obtain from nerve biopsies is limiting to perform gene expression studies. Labial salivary gland (SG) biopsies have been reported as a useful tool for the diagnosis of amyloid neuropathy (1); this tissue presents TTR deposition that correlates with deposition in the PNS and represents a minimally invasive method (1). In the present study we investigated differentially expressed genes related to ECM remodelling in SG biopsies aiming at further elucidating the molecular effects of TTR deposition in FAP.
Cardiac involvement after liver transplantation in patients with Val30Met transthyretin amyloidosis from Majorca focus
Published in Amyloid, 2019
Tomas Ripoll-Vera, Jorge Alvarez, Juan Buades, Eugenia Cisneros, Yolanda Gomez, Catalina Melia, Asunción Ferrer, Ines Losada, Juan Gonzalez, Mercedes Uson, Antonio Figuerola
Familial amyloid polyneuropathy (FAP) is an autosomal dominant disease caused by mutations in transthyretin (TTR) gene. Over 100 TTR mutations have been described to date in patients with TTR amyloidosis. Val30Met is the most common variant in FAP [1,2]. Although rare worldwide, there are some endemic foci in Portugal, Brazil, Sweden, Japan and Spain (the majority from Majorca-Balearic Islands-, the fifth most important focus of the world) [3]. The TTR Val30Met mutation presents classically with peripheral sensory neuropathy and progresses to autonomic and motor neuropathy, with occurrence of cardiac conduction abnormalities late in the disease progression [4]. Orthotopic liver transplantation (OLT) is considered the best treatment. The abnormal TTR protein is synthesized in 95% in the liver, but also in retina and choroid plexus [5]. Thus, it could be some worsening in spite of OLT. There are few published data about cardiac disease in post-OLT FAP patients. The aim of this study was to investigate the occurrence and development of heart symptoms, arrhythmias, conduction abnormalities and myocardial involvement in Majorca TTR Val30Met FAP patients who underwent OLT.
Cardiac involvement in a large cohort of patients with Val30Met transthyretin amyloidosis from Majorca focus
Published in Amyloid, 2019
Tomas Ripoll-Vera, Jorge Alvarez, Juan Buades, Eugenia Cisneros, Yolanda Gomez, Catalina Melia, Asunción Ferrer, Ines Losada, Juan Gonzalez, Mercedes Uson, Antonio Figuerola
Familial amyloid polyneuropathy (FAP) is an autosomal dominant disease caused by mutations in transthyretin (TTR) gene. Over 100 TTR mutations have been described to date in patients with TTR amyloidosis. Val30Met is the most common variant in FAP [1,2]. Although rare worldwide, there are some endemic foci in Portugal, Brazil, Sweden, Japan and Spain (the majority from Majorca –Balearic Islands–, the fifth most important focus of the world) [3] Val30Met mutation presents classically with progressive polyneuropathy, with occurrence of cardiac conduction abnormalities late in the disease without significant cardiac hypertrophy [4]. The aim of this study was to assess the cardiac involvement in a large group of FAP patients, from a specific endemic area.
Bilateral Progressive Optic Neuropathy in a Patient with Familial Amyloid Polyneuropathy: Amyloid Deposits in the Optic Nerve Head?
Published in Neuro-Ophthalmology, 2023
José Ignacio Vela, Sandra Perich, Victoria Bulnes, Irene Loscos, María Baradad
Familial amyloid polyneuropathy (FAP) is a rare autosomal dominant hereditary disease. Its origin resides in the mutation of the gene that codes for the protein transthyretin (TTR), located on chromosome 18. The abnormal protein produced loses its tetrameric configuration and aggregates forming amyloid deposits. There are several mutations, but the most frequent is Val30Met. The abnormal TTR protein is 90% produced by the liver and less than 2% by the choroid plexus and the retinal pigment epithelium. It is characterised by the deposition of amyloid in peripheral nerves and other multiple organs. Among hereditary TTR amyloidosis patients 10% present with ocular involvement.1