%0 Journal Article %T Influence of heparin molecular size on the induction of C-terminal unfolding in ¦Â2-microglobulin %A Kanon Fukasawa %A Yuichiro Higashimoto %A Yoshihiro Motomiya %A Yoshinori Uji %A Yukio Ando %J Molecular Biology Research Communications %P 225-232 %D 2016 %I Shiraz University Press %R - %X Dialysis-related amyloidosis (DRA) is characterized by accumulation of amyloid ¦Â2-microglobulin (¦Â2m) in the interstitial matrix. Matrix substances such as heparin have reportedly been strongly implicated in the pathogenesis of dialysis-related amyloidosis. In clinical setting of hemodialysis, two types of heparin, i.e., high and low molecular heparin (H.M.H. and L.M.H.) have been routinely used. Still commonly used is H.M.H., followed by L.M.H. preparations with distinct advantages. Here, we studied that the interaction of native and two amyloidogenic ¦Â2m variants: ¦¤N6¦Â2m and D76N ¦Â2m with H.M.H. and L.M.H. We also investigated whether heparin could induce ¦Â2m to have an amyloidogenic conformation.Biolayer interferometry revealed that ¦¤N6¦Â2m had a strong reaction and D76N ¦Â2m had a moderate reaction with H.M.H.. Furthermore, H.M.H. induced the C-terminal unfolding in a native ¦Â2m. By contrast, L.M.H. showed no reaction even with ¦¤N6¦Â2m.This study showed firstly a direct binding of ¦Â2m with H.M.H.. H.M.H. would provoked a C-terminal unfolding of ¦Â2m, which indicated production of an amyloidogenic intermediate, i.e., ¦Â2m92-99. In addition, our findings also suggest that L.M.H. may provide beneficial effects against the development of the DRA %K ¦Â2-microglobulin %K Heparin %K Dialysis-related amyloidosis %K Biolayer interferometry %U http://mbrc.shirazu.ac.ir/article_3866_e3deb7382c93556b2b8e5e1c43d317e1.pdf