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J Am Soc Nephrol 15:126-133, 2004
© 2004 American Society of Nephrology

BASIC SCIENCE

Glycosaminoglycans Enhance the Trifluoroethanol-Induced Extension of {beta}2-Microglobulin–Related Amyloid Fibrils at a Neutral pH

Suguru Yamamoto*,{dagger}, Itaru Yamaguchi*, Kazuhiro Hasegawa*, Shinobu Tsutsumi*, Yuji Goto{ddagger},§, Fumitake Gejyo{dagger} and Hironobu Naiki*,§

*Department of Pathology, Fukui Medical University, Fukui, Japan; {dagger}Division of Clinical Nephrology and Rheumatology, Niigata University Graduate School of Medical and Dental Science, Niigata, Japan; {ddagger}Institute for Protein Research, Osaka University, Osaka, Japan; and §CREST of Japan Science and Technology Corporation, Saitama, Japan

Correspondence to Dr. Hironobu Naiki, Department of Pathology, Fukui Medical University, Fukui 910-1193, Japan. Phone: +81-776-61-8320; Fax: +81-776-61-8123;

ABSTRACT. {beta}2-Microglobulin–related (A{beta}2M) amyloidosis is a frequent and serious complication in patients on long-term dialysis, and {beta}2-microglobulin is a major structural component of A{beta}2M amyloid fibrils. Several biologic molecules inhibiting the depolymerization of A{beta}2M amyloid fibrils at a neutral pH were found recently. The effect of trifluoroethanol and glycosaminoglycans (GAG) on the extension of the fibrils at a neutral pH was investigated with the use of fluorescence spectroscopy with thioflavin T, circular dichroism spectroscopy, and electron microscopy. Trifluoroethanol at concentrations of up to 20% (vol/vol) caused fibril extension of heparin-stabilized seeds, inducing a subtle change in the tertiary structure of {beta}2-microglobulin and stabilizing the fibrils at a neutral pH. This extension reaction followed a first-order kinetic model. In addition, some GAG, especially heparin, dose-dependently enhanced the fibril extension. These results suggest that some GAG, especially heparin, may bind to the fibrils and enhance their deposition in vivo. Thus, the experimental system described here should be useful to search for the factors that accelerate A{beta}2M amyloid deposition in vivo. In addition, the interference of the binding of GAG to A{beta}2M amyloid fibrils may be an attractive therapeutic modality. E-mail: naiki@fmsrsa.fukui-med.ac.jp


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