Structurally abnormal transthyretin causing familial amyloidotic polyneuropathy in Sweden
1987; Elsevier BV; Volume: 167; Issue: 3 Linguagem: Inglês
10.1016/0009-8981(87)90355-x
ISSN1873-3492
AutoresMasamitsu Nakazato, Lars Steen, Gösta Holmgren, Teruyuki Kurihara, Shigeru Matsukura, Kenji Kangawa, Hisayuki Matsuo,
Tópico(s)Caveolin-1 and cellular processes
ResumoThe complex of diseases referred to as amyloidosis is characterized by the deposition ofamyloid substance in various tissues. The amyloid protein differs in the various forms of amyloidosis. This variation is the basis of the differences in affected tissues and subsequent clinical dissimilarities. Vitreous involvement in amyloidosis seems to be especially linked to some of the hereditary neuropathies associated with the amyloid protein transthyretin. Characterization of the amyloid proteins during recent decades has allowed a chemical and immunologic classification of amyloid fibrils. This paper presents the basis for classification of amyloidosis, reviews the literature on ocular amyloidosis, with special reference to vitreous involvement, and summarizes clinical findings and frequency of vitreous amyloid involvement in Swedish patients with familial amyloidotic polyneuropathy.
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