Premium
Advanced glycation end product in familial amyloidotic polyneuropathy (FAP)
Author(s) -
Nyhlin N.,
Ando Y.,
Nagai R.,
Suhr O.,
El Sahly M.,
Terazaki H.,
Yamashita T.,
Ando M.,
Horiuchi S.
Publication year - 2000
Publication title -
journal of internal medicine
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.625
H-Index - 160
eISSN - 1365-2796
pISSN - 0954-6820
DOI - 10.1046/j.1365-2796.2000.00668.x
Subject(s) - medicine , polyneuropathy , advanced glycation end product , glycation , dermatology , gastroenterology , endocrinology , diabetes mellitus
. Nyhlin N, Ando Y, Nagai R, Suhr O, El Sahly M, Terazaki H, Yamashita T, Ando M, Horiuchi S (Umeå University Hospital, Umeå, Sweden and Kumamoto University School of Medicine, Kumamoto, Japan). Advanced glycation end product in familial amyloidotic polyneuropathy (FAP). J Intern Med 2000; 247 : 485–492. Objectives. Advanced glycation end products (AGE) are present in amyloid deposits in β 2 ‐microglobulin amyloidosis, and it has been postulated that glycation of β 2 ‐microglobulin may be involved in fibril formation. The aim of this paper was to ascertain whether AGE occur in amyloid deposits in familial amyloidotic polyneuropathy (FAP). Setting. Department of Medicine, Umeå University Hospital and First Department of Internal Medicine, Kumamoto University School of Medicine. Design. The presence of AGE was sought immunohistochemically and biochemically in amyloid‐rich tissues from patients with FAP. Subjects. Biopsy specimens from nine patients and 10 controls were used for the immunohistochemical analysis. For amyloid preparation, vitreous samples from three FAP patients were used. Results. Immunohistochemical studies using a polyclonal anti‐AGE antibody revealed positive immunoreactivity in intestinal materials, but the pattern of reactivity was unevenly distributed; it was often present in the border of amyloid deposits, or surrounding them. Non‐amyloid associated immunoreactivity was also observed in a few regions of the specimens, although the AGE‐positive structures were situated in areas containing amyloid deposits. Western blotting of purified amyloid from the vitreous body of FAP patients revealed a significant association of AGE with amyloid fibrils. Conclusion. The immunoreactivity for the AGE antibody suggests that AGE may be involved in fibril formation in FAP.