Quantitative analysis of amyloid fibril protein in systemic organs of patients with familial amyloidotic polyneuropathy.
The purpose of this study was to develop a quantitative method for variant transthyretin (also called prealbumin) in amyloid-laden tissues of familial amyloidotic polyneuropathy (FAP). The variant transthyretin was extracted by using 70% formic acid solution in which the protein was solubilized completely and rapidly. The quantity of the variant transthyretin was measured by a radioimmunoassay (RIA). An immunoreactive species detected in the tissues of FAP was confirmed to be the variant transthyretin by reverse-phase high-performance liquid chromatography. The quantity of the variant transthyretin in the thyroid gland of 2 FAP patients was 9.90 and 9.76 micrograms/mg tissue, and that of the kidney was 4.03 and 6.27 micrograms/mg tissue, respectively, while its quantity in the liver was only 0.15 and 0.12 microgram/mg tissue. We present here a quantitative analysis of the distribution and predominance of amyloid deposits in systemic organs of FAP.
Nakazato
M
M
Third Department of Internal Medicine, Miyazaki Medical College, Japan.
Tanaka
M
M
Matsukura
S
S
Kangawa
K
K
Matsuo
H
H
D000328:Adult; D000686:Amyloidosis / Q000235:genetics / Q000378:metabolism*; D005260:Female; D006801:Humans; D007668:Kidney / Q000378:metabolism*; D008099:Liver / Q000378:metabolism*; D008297:Male; D008875:Middle Aged; D000685:Serum Amyloid A Protein / Q000378:metabolism*; D013961:Thyroid Gland / Q000378:metabolism*
D000685:Serum Amyloid A Protein