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

Research output: Contribution to journalArticlepeer-review

65 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)187-194
Number of pages8
JournalKidney International
Issue number1
Publication statusPublished - 1997

All Science Journal Classification (ASJC) codes

  • Nephrology


Dive into the research topics of 'Amyloid β<sub>2</sub>-microglobulin is modified with imidazolone, a novel advanced glycation end product, in dialysis-related amyloidosis'. Together they form a unique fingerprint.

Cite this