Aggregation of β<sub>2</sub>-Glycoprotein I Induced by Sodium Lauryl Sulfate and Lysophospholipids

Hagihara, Yoshihisa; Hong, Dong-Pyo; Hoshino, Minoru; Enjyoji, Keiichi; Kato, Harubumi; Goto, Yuji

doi:10.1021/bi015693q

Cited by 42 publications

(46 citation statements)

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“…SDS has been well known to bind to various kinds of proteins (39), producing, above the CMC, a stable complex of SDS micelles and proteins in which the proteins tend to denature and assume an ␣-helical conformation. There have been several reports that SDS at a concentration lower than the CMC value induces the aggregation of proteins and peptides (28). Furthermore, SDS has been reported to induce amyloid-like fibrils of a peptide from human complement receptor I (29).…”

Section: Discussionmentioning

confidence: 99%

“…Oligomer Formation Revealed by Analytical Centrifugation-A low concentration of SDS, below the CMC, has been suggested to induce the aggregation of proteins, including ␤2-m (28,30). We examined this possibility by measuring sedimentation velocity and sedimentation equilibrium (Fig.…”

Section: Extension Of ␤2-m Amyloid Fibrils Atmentioning

confidence: 99%

“…SDS is an anionic detergent that mimics some characteristics of biological membranes and is considered to be a good model for anionic phospholipids. It has been reported that SDS induces some proteins or peptides to form aggregates (28) or amyloid-like fibrils in vitro (29). Recently, Yamamoto et al (30) found that low concentrations of SDS around the critical micelle concentration (CMC) (0.7 mM) not only stabilize the fibrils but also induce the extensive growth of ␤2-m amyloid fibrils at neutral pH, probably through the SDS-induced con-formational change of ␤2-m monomers.…”

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confidence: 99%

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

Kihara

Chatani

Sakai

et al. 2005

Journal of Biological Chemistry

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showed that a combination of seed fibrils prepared under acidic conditions and a low concentration of sodium dodecyl sulfate below its critical micelle concentration enabled extensive fibril formation at pH 7.0. Here, we found that repeated self-seeding at pH 7.0 with fibrils formed at the same pH causes a marked acceleration of growth, indicating the maturation of fibrils. The observed maturation can be simulated by assuming the existence of two types of fibrils with different growth rates. Importantly, some mutations of ␤2-m or the addition of a low concentration of urea, both destabilizing the native conformation, were not enough to extend the fibrils at pH 7.0, and a low concentration of sodium dodecyl sulfate (i.e. 0.5 mM) was essential. Thus, even though the first stage fibrils in patients are unstable and require stabilizing factors to remain at neutral pH, they can adapt to a neutral pH with repeated selfseeding, implying a mechanism of development of amyloid deposition after a long latent period in patients.Amyloidosis results from the deposition of normally soluble proteins into insoluble amyloid fibrils that are long, unbranched, and often twisted fibrillar structures a few nanometers in diameter and predominantly composed of cross-␤-sheets (1-3). Currently, Ͼ20 proteins are known to be associated with human amyloid diseases (1-3). Moreover, various proteins and peptides that are not related to diseases can also form amyloid-like fibrils, implying that the formation of amyloid fibrils is a general property of polypeptides (2, 3). Most of the amyloidogenic proteins studied to date have been shown to unfold or refold (if they are initially unfolded), such that one or more partially unfolded intermediate(s) are produced prior to the formation of amyloid fibrils (2, 3). These structural alterations are often brought about by changes in the solution, such as a switch to low pH (4 -6), high temperature (7, 8), or by the addition of organic solvents (9, 10). However, the mechanism by which native proteins form amyloid fibrils under physiological conditions is still unclear.Among the various amyloidogenic proteins, ␤ 2 -microglobulin (␤2-m), 1 which is responsible for dialysis-related amyloidosis, is a target of extensive study because of its clinical importance and suitable size for examining the relationship between protein folding and amyloid fibril formation (10 -18). Dialysisrelated amyloidosis is a common and serious complication in patients receiving hemodialysis for Ͼ10 years (11, 12). ␤2-m, a typical immunoglobulin domain made of 99 residues and seven ␤-strands, is present as the non-polymorphic light chain of the class I major histocompatibility complex (MHC-I) (19). As part of its normal catabolic cycle, ␤2-m dissociates from the MHC-I complex and is transported in serum to the kidneys, where the majority (95%) of it is degraded (12). Renal failure disrupts the clearance of ␤2-m from the serum and, moreover, the ␤2-m does not pass through the dialysis membrane, resulting in an increase in the ␤2-m ...

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Section: Discussionmentioning

confidence: 99%

Section: Extension Of ␤2-m Amyloid Fibrils Atmentioning

confidence: 99%

mentioning

confidence: 99%

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

Kihara

Chatani

Sakai

et al. 2005

Journal of Biological Chemistry

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“…Oligomers formed in the presence of SDS micelles may be stable during SDS-PAGE, thus misrepresenting the natural assembly state of the peptide or protein prior to treatment with SDS. Artifactual aggregation induced by SDS has been observed for Hepatitis B surface antigen polypeptides [26], bradykinin [27], b(2)-glycoprotein I [28], and collagen [29]. In addition to aggregation, conformational changes in the presence of SDS may cause aberrant electrophoretic mobility, a phenomenon that has been reported for various proteins [30,31], including Ab [32].…”

Section: Potential Pitfalls In Characterization Of Oligomers Of Amylomentioning

confidence: 99%

Neurotoxic protein oligomers — what you see is not always what you get

Bitan¹,

Fradinger²,

Spring³

et al. 2005

Amyloid

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“…because of the existence of strong electrostatic and hydrophobic interactions between the micelles and the proteins (5,6). Conversely, nonionic surfactants do not alter protein conformation in comparison with anionic surfactants since they are free of any electrostatic interaction (7).…”

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Enhancement of enzymatic catalysis of Bacillus amyloliquefaciens α‐amylase by nonionic surfactant micelles

Hoshino

Tanaka

2003

J Surfact & Detergents

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Some enzymes are considerably more stable when formulated with nonionic surfactants than when formulated with anionic surfactants. The effect of a nonionic surfactant, polyoxyethylene mono-N-dodecyl ether (Brij 35; number of units of ethylene oxide moieties, 23), on the kinetic behavior of hydrolysis of amylopectin with Bacillus amyloliquefaciens α-amylase (BAA) was studied at a temperature of 25°C and a pH of 7.0. The hydrolytic rate was accelerated by the addition of the nonionic surfactant above its critical micelle concentration. Lineweaver-Burk plots for the enzymatic hydrolysis in the absence and presence of the nonionic surfactant at 0.5 to 2.5% (wt/vol) had linear relationships, and the kinetic parameters, K m and k cat , were obtained. The value of k cat was increased with an increased concentration of Brij 35, whereas the K m value was approximately constant. Therefore, the increase in k cat contributed to the acceleration of the apparent hydrolytic rate. The interaction of amylopectin with the surfactant was examined by a surface tension measurement, and the result confirmed the corresponding binding between the substrate and the surfactant. A fluorescence analysis due to tryptophan in BAA suggested that BAA bound to the nonionic micelles. The increase in k cat suggested that hydrolytic catalysis at the micellar pseudophase was more efficient than that at the aqueous pseudophase. The enhancement of the catalytic rate contributed to the effective removal of food stains containing starch when BAA was added with Brij 35 in a laundry detergent washing test.Amphiphilic media such as micelles and microemulsion droplets can influence enzyme structure and activity (1,2). An investigation of the interaction between synthetic surfactants and enzymes in aqueous solutions has shown that there is a range of possible surfactant effects on the activity of enzymes (3,4). The micelle-forming anionic surfactants are known to alter protein and substrate conformations because of the existence of strong electrostatic and hydrophobic interactions between the micelles and the proteins (5,6). Conversely, nonionic surfactants do not alter protein conformation in comparison with anionic surfactants since they are free of any electrostatic interaction (7). Moreover, some nonionic surfactants reportedly increase the catalytic activity of enzymes. For example, polyethyleneglycol mono-N-dodecyl ether (Brij 35; number of units of ethylene oxide moieties, 23) stimulates cytoplasmic glycerol-3-phosphate dehydrogenase 1.5-fold (8).α-Amylase (EC 3.2.1.1; 1,4-α-D-glucan glucanohydrolase) hydrolyzes starch by cleaving the internal α-1,4-glucosidic bonds (9-12). This enzyme, produced from genus Bacillus, has been studied extensively for industrial applications in the sugar, brewing, alcohol, desizing, and detergent industries (13,14). The nucleotide sequence of the α-amylase genes from Bacillus amyloliquefaciens has been determined (15). The kinetic properties of this enzyme with use of linear maltooligosaccharides have been studied in det...

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Aggregation of β₂-Glycoprotein I Induced by Sodium Lauryl Sulfate and Lysophospholipids

Cited by 42 publications

References 42 publications

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

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

Neurotoxic protein oligomers — what you see is not always what you get

Enhancement of enzymatic catalysis of Bacillus amyloliquefaciens α‐amylase by nonionic surfactant micelles

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Aggregation of β2-Glycoprotein I Induced by Sodium Lauryl Sulfate and Lysophospholipids

Cited by 42 publications

References 42 publications

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

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

Neurotoxic protein oligomers — what you see is not always what you get

Enhancement of enzymatic catalysis of Bacillus amyloliquefaciens α‐amylase by nonionic surfactant micelles

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Product

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Aggregation of β₂-Glycoprotein I Induced by Sodium Lauryl Sulfate and Lysophospholipids