Apolipoprotein E Inhibits the Depolymerization of β2-Microglobulin-Related Amyloid Fibrils at a Neutral pH†

Biochemistry ◽  
2001 ◽  
Vol 40 (29) ◽  
pp. 8499-8507 ◽  
Author(s):  
Itaru Yamaguchi ◽  
Kazuhiro Hasegawa ◽  
Naoki Takahashi ◽  
Fumitake Gejyo ◽  
Hironobu Naiki
Keyword(s):  
Apolipoprotein E ◽  
Amyloid Fibrils ◽  
Β2 Microglobulin ◽  
Neutral Ph

scholarly journals Seeding-dependent Maturation of β2-Microglobulin Amyloid Fibrils at Neutral pH

2005 ◽  
Vol 280 (12) ◽  
pp. 12012-12018 ◽  
Author(s):  
Miho Kihara ◽  
Eri Chatani ◽  
Miyo Sakai ◽  
Kazuhiro Hasegawa ◽  
Hironobu Naiki ◽  
...  
Keyword(s):  
Amyloid Fibrils ◽  
Β2 Microglobulin ◽  
Neutral Ph

Low Concentrations of Sodium Dodecyl Sulfate Induce the Extension of β2-Microglobulin-Related Amyloid Fibrils at a Neutral pH†

Biochemistry ◽  
2004 ◽  
Vol 43 (34) ◽  
pp. 11075-11082 ◽  
Author(s):  
Suguru Yamamoto ◽  
Kazuhiro Hasegawa ◽  
Itaru Yamaguchi ◽  
Shinobu Tsutsumi ◽  
József Kardos ◽  
...  
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Amyloid Fibrils ◽  
Sodium Dodecyl ◽  
Β2 Microglobulin ◽  
Neutral Ph ◽  
Low Concentrations ◽  
Dodecyl Sulfate

Thiol Compounds Inhibit the Formation of Amyloid Fibrils by β2-Microglobulin at Neutral pH

2008 ◽  
Vol 376 (1) ◽  
pp. 258-268 ◽  
Author(s):  
Kaori Yamamoto ◽  
Hisashi Yagi ◽  
Daisaku Ozawa ◽  
Kenji Sasahara ◽  
Hironobu Naiki ◽  
...  
Keyword(s):  
Amyloid Fibrils ◽  
Thiol Compounds ◽  
Β2 Microglobulin ◽  
Neutral Ph

Growth of β2-microglobulin-related amyloid fibrils by non-esterified fatty acids at a neutral pH

2008 ◽  
Vol 416 (2) ◽  
pp. 307-315 ◽  
Author(s):  
Kazuhiro Hasegawa ◽  
Shinobu Tsutsumi-Yasuhara ◽  
Tadakazu Ookoshi ◽  
Yumiko Ohhashi ◽  
Hideki Kimura ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Amyloid Fibrils ◽  
Binding Capacity ◽  
Compact Structure ◽  
Β2 Microglobulin ◽  
Neutral Ph ◽  
Esterified Fatty Acids ◽  
Partial Unfolding

Aβ2M (β2-microglobulin-related) amyloidosis is a frequent and serious complication in patients on long-term dialysis. Partial unfolding of β2-m (β2-microglobulin) may be essential to its assembly into Aβ2M amyloid fibrils in vivo. Although SDS around the critical micelle concentration induces partial unfolding of β2-m to an α-helix-containing aggregation-prone amyloidogenic conformer and subsequent amyloid fibril formation in vitro, the biological molecules with similar activity under near-physiological conditions are still unknown. The effect of various NEFAs (non-esterified fatty acids), which are representative anionic amphipathic compounds in the circulation, on the growth of Aβ2M amyloid fibrils at a neutral pH was examined using fluorescence spectroscopy with thioflavin T, CD spectroscopy, and electron microscopy. Physiologically relevant concentrations of laurate, myristate, oleate, linoleate, and mixtures of palmitate, stearate, oleate and linoleate, induced the growth of fibrils at a neutral pH by partially unfolding the compact structure of β2-m to an aggregation-prone amyloidogenic conformer. In the presence of human serum albumin, these NEFAs also induced the growth of fibrils when their concentrations exceeded the binding capacity of albumin, indicating that the unbound NEFAs rather than albumin-bound NEFAs induce the fibril growth reaction in vitro. These results suggest the involvement of NEFAs in the development of Aβ2M amyloidosis, and in the pathogenesis of Aβ2M amyloidosis.

scholarly journals Investigation into the Role of Macrophages in the Formation and Degradation of β2-Microglobulin Amyloid Fibrils

2007 ◽  
Vol 282 (40) ◽  
pp. 29691-29700 ◽  
Author(s):  
Isobel J. Morten ◽  
Walraj S. Gosal ◽  
Sheena E. Radford ◽  
Eric W. Hewitt
Keyword(s):  
Amyloid Fibrils ◽  
Β2 Microglobulin

scholarly journals Advanced Glycation End Product-Modified β2-Microglobulin is a Component of Amyloid Fibrils of Primary Localized Cutaneous Nodular Amyloidosis

2002 ◽  
Vol 118 (3) ◽  
pp. 479-484 ◽  
Author(s):  
Norihiro Fujimoto ◽  
Mayumi Yajima ◽  
Yoshihiro Ohnishi ◽  
Shingo Tajima ◽  
Akira Ishibashi ◽  
...  
Keyword(s):  
Amyloid Fibrils ◽  
Advanced Glycation ◽  
Advanced Glycation End Product ◽  
Β2 Microglobulin

Thermal Response with Exothermic Effects of β2-Microglobulin Amyloid Fibrils and Fibrillation

2009 ◽  
Vol 389 (3) ◽  
pp. 584-594 ◽  
Author(s):  
Kenji Sasahara ◽  
Hisashi Yagi ◽  
Hironobu Naiki ◽  
Yuji Goto
Keyword(s):  
Amyloid Fibrils ◽  
Thermal Response ◽  
Β2 Microglobulin

Heat-Triggered Conversion of Protofibrils into Mature Amyloid Fibrils of β2-Microglobulin†

Biochemistry ◽  
2007 ◽  
Vol 46 (11) ◽  
pp. 3286-3293 ◽  
Author(s):  
Kenji Sasahara ◽  
Hisashi Yagi ◽  
Hironobu Naiki ◽  
Yuji Goto
Keyword(s):  
Amyloid Fibrils ◽  
Β2 Microglobulin

Kinetic analysis of the polymerization and depolymerization of β2-microglobulin-related amyloid fibrils in vitro

2005 ◽  
Vol 1753 (1) ◽  
pp. 34-43 ◽  
Author(s):  
Suguru Yamamoto ◽  
Kazuhiro Hasegawa ◽  
Itaru Yamaguchi ◽  
Yuji Goto ◽  
Fumitake Gejyo ◽  
...  
Keyword(s):  
Kinetic Analysis ◽  
Amyloid Fibrils ◽  
Β2 Microglobulin
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