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Title

INFLUENCE OF HEPARIN MOLECULAR SIZE ON THE INDUCTION OF CTERMINAL UNFOLDING IN β2-MICROGLOBULIN (SHORT COMMUNICATION)

Pages

 Start Page 225 | End Page 232

Abstract

 Dialysis-related amyloidosis (DRA) is characterized by accumulation of amyloid b2- microglobulin (b2m) 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 b2m variants: DN6b2m and D76N b2m with H.M.H. and L.M.H. We also investigated whether HEPARIN could induce b2m to have an amyloidogenic conformation. BIOLAYER INTERFEROMETRY revealed that DN6b2m had a strong reaction and D76N b2m had a moderate reaction with H.M.H.. Furthermore, H.M.H. induced the C-terminal unfolding in a native b2m. By contrast, L.M.H. showed no reaction even with DN6b2m. This study showed firstly a direct binding of b2m with H.M.H.. H.M.H. would provoked a C-terminal unfolding of b2m, which indicated production of an amyloidogenic intermediate, i.e., b2m92-99. In addition, our findings also suggest that L.M.H. may provide beneficial effects against the development of the DRA.

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