β2-microglobulin modified with advanced glycation end products induces interleukin-6 from human macrophages: Role in the pathogenesis of hemodialysis-associated amyloidosis

Yoshiyasu Iida, Toshio Miyata, Reiko Inagi, Satoshi Sugiyama, Kenji Maeda

Research output: Contribution to journalArticle

83 Citations (Scopus)

Abstract

Recently, we demonstrated that β2-microglobulin (β2M) of amyloid deposits in hemodialysis-associated amyloidosis (HAA), a serious complication leading to hemodialysis arthropathy, is modified with advanced glycation end products (AGEs) of the Maillard reaction. In the present study, to elucidate the possible involvement of AGEs-modified β2M (AGE-β2M) in the pathogenesis of HAA, we examined the effect of AGE-β2M on macrophage production of interleukin-6 (IL-6), an important cytokine for osteoclastogenesis and bone resorption. Purified AGE-β2M from long-term hemodialysis patients, but not normal β2M, stimulated synthesis and secretion of IL-6 from macrophages. Similar effects were also induced by in vitro-prepared AGE-β2M (normal β2M incubated with glucose for 60 days in vitro). These findings suggested a potential role of AGE-β2M in the pathogenesis of HAA.

Original languageEnglish
Pages (from-to)1235-1241
Number of pages7
JournalBiochemical and biophysical research communications
Volume201
Issue number3
DOIs
Publication statusPublished - 1994 Jun 30
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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