New England Journal of Medicine · 2002 · 687 citations · 27 references
Life SciencesGeneticsPathologyHuman GeneticsMedical GeneticsMolecular PathologyAmyloid FormationGenetic Disease PathologyGenetic DisordersRare Disease GeneticsAmyloidogenic ProteinsApolipoprotein A-i AmyloidosisDifferential Diagnosis CriteriaFamily Health HistoryFibrinogen A Alpha-chain AmyloidosisHereditary AmyloidosisLysozyme Amyloidosis
BACKGROUND: Hereditary, autosomal dominant amyloidosis, caused by mutations in the genes encoding transthyretin, fibrinogen A alpha-chain, lysozyme, or apolipoprotein A-I, is thought to be extremely rare and is not routinely included in the differential diagnosis of systemic amyloidosis unless there is a family history. METHODS: We studied 350 patients with systemic amyloidosis, in whom a diagnosis of the light-chain (AL) type of the disorder had been suggested by clinical and laboratory findings and by the absence of a family history, to assess whether they had amyloidogenic mutations. RESULTS: Amyloidogenic mutations were present in 34 of the 350 patients (9.7 percent), most often in the genes encoding fibrinogen A alpha-chain (18 patients) and transthyretin (13 patients). In all 34 of these patients, the diagnosis of hereditary amyloidosis was confirmed by additional investigations. A low-grade monoclonal gammopathy was detected in 8 of the 34 patients (24 percent). CONCLUSIONS: A genetic cause should be sought in all patients with amyloidosis that is not the reactive systemic amyloid A type and in whom confirmation of the AL type cannot be obtained.
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ON THE BINDING OF CONGO RED BY AMYLOID
Holde Puchtler, Faye Sweat, Monroe I. Levine · Journal of Histochemistry & Cytochemistry · 1962 · 1.1K citations
Robert A. Kyle, Morie A. Gertz, Philip R. Greipp et al. · New England Journal of Medicine · 1997 · 691 citations · Full text
Human lysozyme gene mutations cause hereditary systemic amyloidosis
Mark B. Pepys, Philip N. Hawkins, David R. Booth et al. · Nature · 1993 · 660 citations