Analysis of serum amyloid β<sub>2</sub> microglobulin from hemodialysis patients using liquid chromatography/mass spectrometry

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  • 透析患者における血中アミロイドβ<sub>2</sub>ミクログロブリンのLC/MSによる解析
  • 透析患者における血中アミロイドβ₂ミクログロブリンのLC/MSによる解析
  • トウセキ カンジャ ニ オケル ケッチュウ アミロイドv ₂ ミクログロブリン ノ LC/MS ニ ヨル カイセキ

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Abstract

<p>The protein responsible for dialysis-related amyloidosis (DRA) is irreversibly unfolded amyloid β2 microglobulin (A-β2M), but a partially unfolded conformer of β2M (I-β2M) has been detected during the amyloidization of native β2M. In this study, we analyzed the serum I-β2M of predialysis chronic kidney disease (CKD) patients, short-term hemodialysis patients, and long-term hemodialysis patients and tissue β2M derived from amyloid tissue using liquid chromatography/mass spectrometry (LC/MS). Four ionized peaks at ＋7 to ＋10 were found in all samples. Since the ionized peak for native β2M was located at＋7 and＋8, and that for A-β2M was located at ＋9 and ＋10, we analyzed the ratio of (＋9 plus ＋10) to (＋7 plus ＋8) as the MS index (MS-I). The serum I-β2M MS-I of the predialysis CKD patients, short-term hemodialysis patients, and long-term dialysis patients were 1.70±0.13, 1.90±0.13, and 1.79±0.25, respectively, and did not differ significantly among the 3 groups. On the other hand, the MS-I of the tissue β2M derived from amyloid tissue were markedly higher (4.15 and 7.33). The main finding of this study; i.e., that A-β2M, which causes the formation of amyloid, could not be detected in the sera of hemodialysis patients by LC/MS, was consistent with our hypothesis that some of the incompletely unfolded β2M moves from the serum to the extravascular tissue, where it continues to unfold, and the accumulation of this substance leads to the onset of DRA.</p>

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