Amyloid β2-microglobulin is modified with imidazolone, a novel advanced glycation end product, in dialysis-related amyloidosis

Toshimitsu Niwa, Tomoyuki Katsuzaki, Shigeru Miyazaki, Tomoko Momoi, Takashi Akiba, Takashi Miyazaki, Kazuya Nokura, Fumitaka Hayase, Noriyuki Tatemichi, Yoshifumi Takei

研究成果: Article査読

64 被引用数 (Scopus)

抄録

We have recently demonstrated by immunohistochemistry that amyloid β2-microglobulin (β2m) is modified with advanced glycation end products (AGEs) in dialysis-related amyloidosis (DRA). To further investigate the role of the Maillard reaction in the pathogenesis of DRA, we produced a monoclonal antibody to imidazolone, a novel AGE, and a reaction product of arginine and 3-deoxyglucosone (3-DG) which was accumulated in uremic serum. Then we determined the localization of imidazolone in the amyloid tissues by immunohistochemistry using the antibody. The connective tissues in carpal tunnel and ligamentum flavum were obtained from six patients with carpal tunnel syndrome and two patients with destructive spondyloarthropathy. Imidazolone was localized to all the β2m-positive amyloid deposits in these patients. Western blotting using the antibody demonstrated that β2m extracted from the synovium amyloid of hemodialysis patients was modified with imidazolone. Further, β2m isolated from the blood ultrafiltrate of hemodialyzed patients was also modified with imidazolone. In vitro incubation of β2m with 3-DG produced imidazolone-modified β2m. In conclusion, amyloid tissue β2m is modified with imidazolone in patients with DRA. 3-DG accumulating in uremic serum may be involved in the modification of β2m with imidazolone.

本文言語English
ページ(範囲)187-194
ページ数8
ジャーナルKidney International
51
1
DOI
出版ステータスPublished - 1997

All Science Journal Classification (ASJC) codes

  • Nephrology

フィンガープリント 「Amyloid β<sub>2</sub>-microglobulin is modified with imidazolone, a novel advanced glycation end product, in dialysis-related amyloidosis」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

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