Beta 2-microglobulin modified with advanced glycation end products induces interleukin-6 from human macrophages: role in the pathogenesis of hemodialysis-associated amyloidosis - PubMed (original) (raw)
. 1994 Jun 30;201(3):1235-41.
doi: 10.1006/bbrc.1994.1837.
Affiliations
- PMID: 8024566
- DOI: 10.1006/bbrc.1994.1837
Beta 2-microglobulin modified with advanced glycation end products induces interleukin-6 from human macrophages: role in the pathogenesis of hemodialysis-associated amyloidosis
Y Iida et al. Biochem Biophys Res Commun. 1994.
Abstract
Recently, we demonstrated that beta 2-microglobulin (beta 2M) 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 beta 2M (AGE-beta 2M) in the pathogenesis of HAA, we examined the effect of AGE-beta 2M on macrophage production of interleukin-6 (IL-6), an important cytokine for osteoclastogenesis and bone resorption. Purified AGE-beta 2M from long-term hemodialysis patients, but not normal beta 2M, stimulated synthesis and secretion of IL-6 from macrophages. Similar effects were also induced by in vitro-prepared AGE-beta 2M (normal beta 2M incubated with glucose for 60 days in vitro). These findings suggested a potential role of AGE-beta 2M in the pathogenesis of HAA.
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