Familial primary amyloidosis with severe amyloid heart disease

Frederiksen, T; Gøtzsche, H; Harboe, Niels; Kiær, William; Mellemgaard, Kresten

doi:10.1016/0002-9343(62)90230-9

Cited by 114 publications

(39 citation statements)

References 35 publications

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“…This observation, together with the results of a DNA study utilizing the polymerase chain reaction technique, confirms the heterozygosity for position 111 of patients from the Danish siblings with familial amyloidotic cardiomyopathy [37]. It also verifies the results from an old detailed clinical study [19] which suggests that the Danish siblings had autosomal dominantly inherited amyloidosis.…”

Section: Discussionsupporting

confidence: 79%

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Purification and Characterization of Amyloid‐Related Transthyretin Associated with Familial Amyloidotic Cardiomyopathy

Hermansen

Bergman

Jörnvall

et al. 1995

European Journal of Biochemistry

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Analysis of amyloid fibril material associated with familial amyloidotic cardiomyopathy revealed that it contains a mixture of transthyretin-related polypeptides. The major protein band in SDS/polyacrylamide gel corresponding to a molecular mass of 14.5 m a , consists of transthyretin fragments starting at positions 46, 49 and 59, the latter not previously identified, and one blocked fragment derived from the Nterminal part of transthyretin. In reverse-phase HPLC, the major fragment recovered was that starting at Thr49, indicating a trypsin-like cleavage (Lys at position 48). Two minor bands, corresponding to 17 kDa and 35 kDa, contained proteins with blocked N-termini, and migrated as monomeric and dimeric transthyretin, respectively. A 13-kDa protein band was found to contain transthyretin with a ragged N-terminus, mainly starting at positions 2 and 5. Three more bands, corresponding to 10, 25 and 29 kDa, consist of transthyretin molecules with blocked N-termini and most likely of aggregates of truncated molecules.A point mutation of amyloid transthyretin was identified at position 111 (Met instead of Leu in normal serum transthyretin) which confirms the mutation found for Danish siblings with familial amyloidotic cardiomyopathy. However, the presence of a non-variant amyloid transthyretin was also observed, indicating that the Danish kindred is heterozygous with respect to this point mutation. Isoelectric focusing of the amyloid fibril material resolved multiple protein bands ranging over pH 4.5 -6.5, confirming heterogeneit ies.Methanol extraction of the cardiac amyloid fibril material prior to the purification steps reveals a methanol-soluble substance amounting to about 10% (by mass dry material) of the amyloid fibril material. A yellow substance in this fraction shows absorbance maxima (270, 280 and 430 nm) similar to those observed for transthyretin in normal serum. Gas chromatographylmass spectrometry of the methanol extracl revealed the presence of saturated fatty acids (C14:0, C16:O and C18:O in the corresponding ratio 2:8:5) and polyunsaturated fatty acids (C16:1, C18:1, C18:2 and C20:4 in the corresponding ratio of 1 :2:1: 1) as further constituents of the amyloid fibril material.

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Section: Discussionsupporting

confidence: 79%

“…A unique Danish form of familial amyloidotic cardiomyopathy was described in 1962 [19]. Affected family members usually die from heart failure before the age of 50.…”

mentioning

confidence: 99%

Purification and Characterization of Amyloid‐Related Transthyretin Associated with Familial Amyloidotic Cardiomyopathy

Hermansen

Bergman

Jörnvall

et al. 1995

European Journal of Biochemistry

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“…T h e whole gamut of the nephropath y from proteinuria to uremia may last 1-12 years, usually closer to the latter figure. However, the clinically manifest nephropathy is preceded by a n asymptomatic stage of amyloidosis in which amyloid may be found in the blood vessels of the submucosa on rectal biopsy several (53) from Denmark. Each of these entities is thought to be caused by a different autosoma1 dominant gene except for FMF which is recessively inherited.…”

Section: Hereditary Amylol Wslsmentioning

confidence: 99%

Hereditary amyloidosis

Andrade

Araki

Block

et al. 1970

Arthritis & Rheumatism

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A review of hereditary amyloidoses is provided by papers from a 1969 international symposium on primary amyloidosis. These discussions allow comparison of the amyloid neuropathy with onset in the lower extremities (POrtUgueseJapanese families), the neuropathy with onset in the upper extremities (Indiana-Maryland families), the neuropathy and nephropathy of the Iowa family, and the amyloidosis of familial Mediterranean fever. The importance of studies of genetic entities in understanding the pathogenesis of amyloidosis is emphasized.

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“…Unlike the Portuguese FAP, clinically significant renal involvement was absent. While a number ofother kindreds with amyloidosis have been described in the last 30 years (Japanese, Swedish, Danish, Iowa, German, French) (3)(4)(5)(6)(7)(8), the Indiana/Swiss syndrome has remained clinically distinct. Only the Maryland kindred described by Mah-loudji, which also has a high incidence ofcarpal tunnel syndrome, clinically resembles the Indiana syndrome (7).…”

Section: Introductionmentioning

confidence: 99%

Characterization of a transthyretin (prealbumin) variant associated with familial amyloidotic polyneuropathy type II (Indiana/Swiss).

Dwulet

Benson²

1986

J. Clin. Invest.

118

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Amyloid fibrils were isolated from cardiac tissue of two brothers who died from familial amyloidotic polyneuropathy (FAP) type II. Sequence analysis on peptides derived from proteolytic cleavage with trypsin and fragmentation with cyanogen bromide reveal that the fibril subunit protein is derived from plasma transthyretin (prealbumin). About two-thirds of the fibril subunit protein was found to contain an amino acid substitution at position 84 where the normal isoleucine residue has been replaced by serine. Sequence analysis of the plasma transthyretin (prealbumin) from the two brothers as well as two clinically diagnosed FAP type II family members and two of four children of affected individuals showed the presence of serine at position 84. The presence of this substitution also correlates with low serum levels of retinolbinding protein and thus transthyretin (prealbumin) position 84 may be involved with the interaction of these two proteins.

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Familial primary amyloidosis with severe amyloid heart disease

Cited by 114 publications

References 35 publications

Purification and Characterization of Amyloid‐Related Transthyretin Associated with Familial Amyloidotic Cardiomyopathy

Purification and Characterization of Amyloid‐Related Transthyretin Associated with Familial Amyloidotic Cardiomyopathy

Hereditary amyloidosis

Characterization of a transthyretin (prealbumin) variant associated with familial amyloidotic polyneuropathy type II (Indiana/Swiss).

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