Ocular amyloidosis, with special reference to thehereditary forms with vitreous involvement

Sandgren, Ola

doi:10.1016/s0039-6257(95)80025-5

Cited by 124 publications

(64 citation statements)

References 170 publications

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“…[6][7][8] Symptoms from the eye are common, and amyloid deposits in the corpus vitrium may lead to blindness if left untreated. 9,[22][23][24][25] Mean survival for patients with FAP is reported to be 9 to 13 years after the onset of symptoms. [5][6][7][8]26 Although neurological symptoms are the most common initial symptom of the disease, variations exist, and kidney failure, gastrointestinal disturbances, or impaired vision may be the first symptoms.…”

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confidence: 99%

Liver transplantation for hereditary transthyretin amyloidosis

et al. 2000

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Liver transplantation for hereditary transthyretin amyloidosis

et al. 2000

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“…Most of these amyloid precursor proteins have been identified for systemic amyloidoses in ocular tissues (Ando et al, 1997a;Campos et al, 1980;Ratnakar and Mohan, 1976;Rodrigues and Zimmerman, 1971;Sandgren, 1995). At least four varieties of lattice corneal dystrophy and gelatinous drop-like corneal dystrophy are classified as hereditary corneal amyloidosis (Gorevic et al, 1991;Klintworth et al, 1997;Nishida et al, 1999).…”

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A Novel Localized Amyloidosis Associated with Lactoferrin in the Cornea

Ando

Nakamura

Kai

et al. 2002

Laboratory Investigation

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SUMMARY:We report a novel localized amyloidosis associated with lactoferrin. To elucidate the precursor protein of corneal amyloidosis associated with trichiasis, we analyzed amyloid deposits from three patients by histopathology and biochemistry. Amyloid deposits showed immunoreactivity, confirmed by electron microscopy, for only anti-human lactoferrin antibody. Electrophoresis of amyloid fibrils revealed lactoferrin with and without sugar chains; N-terminal sequence analysis revealed full-length lactoferrin and a truncated tripeptide of N-terminal amino acids, Gly-Arg-Arg. Carboxymethylated wild-type lactoferrin formed amyloid fibrils in vitro. Lactoferrin gene analysis in the three patients revealed a Glu561Asp mutation in all of the patients and a compound heterozygote of Ala11Thr and Glu561Asp mutations in one patient. A heterozygotic Glu561Asp mutation appeared in 44.8% of healthy Japanese volunteers, suggesting that the mutation may not be an essential mutation for amyloid formation (p ϭ 0.104). Results thus suggest that lactoferrin is this precursor protein. (Lab Invest 2002, 82:757-765).

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“…Our patient, and other affected members of his family, have a rare mutation, 4 TTR-glycine 54. Isolated vitreous amyloidosis is rare, 5 it is usually associated with CNS manifestations. 6 The appearance of the vitreous has been likened to cotton wool or lacelike veils.…”

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confidence: 99%