Specific binding of amyloid-β-protein to IMR-32 neuroblastoma cell membrane

被引：9

作者：

Inaba, S

Okada, T

Konakahara, T

Kodaka, M

机构：

[1] Natl Inst Adv Ind Sci & Technol, Inst Biol Resources & Funct, Tsukuba, Ibaraki 3058566, Japan

[2] Tokyo Univ Sci, Fac Ind Sci & Technol, Noda, Chiba 2788510, Japan

来源：

JOURNAL OF PEPTIDE RESEARCH | 2005年 / 65卷 / 05期

关键词：

aggregation; amyloid-beta-protein; conformation; neuroblastoma cell; specific binding;

D O I：

10.1111/j.1399-3011.2005.00250.X

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

In flow cytometry using two detecting methods, we have found that amyloid-beta-protein(1-40) [A beta(1-40)] has high affinity to IMR-32 neuroblastoma cell membrane when it is aggregated to form beta-sheet conformation, whereas random coil small A beta-species has low affinity. The difference in the binding ability to the cell membranes well accounts for the cytotoxicity of A beta(1-40); namely, aggregated beta-sheet A beta(1-40) gives cytotoxicity higher than random coil A beta(1-40). Specific binding between A beta(1-40) and ganglioside GM1 of the raft-like domain in lipid membrane is suggested from a surface plasmon resonance (SPR) experiment.

引用

收藏

页码：485 / 490

页数：6

相关论文

共 19 条

[1]

CARMICHAEL J, 1987, CANCER RES, V47, P936

[2] MUTATION OF THE BETA-AMYLOID PRECURSOR PROTEIN IN FAMILIAL ALZHEIMERS-DISEASE INCREASES BETA-PROTEIN PRODUCTION [J].

CITRON, M ;

OLTERSDORF, T ;

HAASS, C ;

MCCONLOGUE, L ;

HUNG, AY ;

SEUBERT, P ;

VIGOPELFREY, C ;

LIEBERBURG, I ;

SELKOE, DJ .

NATURE, 1992, 360 (6405) :672-674

[3] Soluble amyloid A beta-(1-40) exists as a stable dimer at low concentrations [J].

GarzonRodriguez, W ;

SepulvedaBecerra, M ;

Milton, S ;

Glabe, CG .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (34) :21037-21044

[4] ALZHEIMERS-DISEASE - INITIAL REPORT OF THE PURIFICATION AND CHARACTERIZATION OF A NOVEL CEREBROVASCULAR AMYLOID PROTEIN [J].

GLENNER, GG ;

WONG, CW .

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1984, 120 (03) :885-890

[5] Spherical aggregates of β-amyloid (amylospheroid) show high neurotoxicity and activate tau protein kinase I/glycogen synthase kinase-3β [J].

Hoshi, M ;

Sato, M ;

Matsumoto, S ;

Noguchi, A ;

Yasutake, K ;

Yoshida, N ;

Sato, K .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2003, 100 (11) :6370-6375

[6] The Aβ peptide of Alzheimer's disease directly produces hydrogen peroxide through metal ion reduction [J].

Huang, XD ;

Atwood, CS ;

Hartshorn, MA ;

Multhaup, G ;

Goldstein, LE ;

Scarpa, RC ;

Cuajungco, MP ;

Gray, DN ;

Lim, J ;

Moir, RD ;

Tanzi, RE ;

Bush, AI .

BIOCHEMISTRY, 1999, 38 (24) :7609-7616

[7] Cholesterol-dependent formation of GM1 ganglioside-bound amyloid β-protein, an endogenous seed for Alzheimer amyloid [J].

Kakio, A ;

Nishimoto, S ;

Yanagisawa, K ;

Kozutsumi, Y ;

Matsuzaki, K .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (27) :24985-24990

[8] Interactions of amyloid β-protein with various gangliosides in raft-like membranes:: Importance of GM1 ganglioside-bound form as an endogenous seed for Alzheimer amyloid [J].

Kakio, A ;

Nishimoto, S ;

Yanagisawa, K ;

Kozutsumi, Y ;

Matsuzaki, K .

BIOCHEMISTRY, 2002, 41 (23) :7385-7390

[9] Formation of a membrane-active form of amyloid β-protein in raft-like model membranes [J].

Kakio, A ;

Nishimoto, SI ;

Kozutsumi, Y ;

Matsuzaki, K .

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2003, 303 (02) :514-518

[10] Alzheimer's β-amyloid, human islet amylin, and prion protein fragment evoke intracellular free calcium elevations by a common mechanism in a hypothalamic GnRH neuronal cell line [J].

Kawahara, M ;

Kuroda, Y ;

Arispe, N ;

Rojas, E .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (19) :14077-14083