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1.
FIGURE 4.

FIGURE 4. From: Role of Glycosaminoglycan Sulfation in the Formation of Immunoglobulin Light Chain Amyloid Oligomers and Fibrils.

Morphology of oligomers is altered by HS. LC AL-00131 was incubated in the presence or absence of GAGs using AFM (1 × 1 μm). These experiments were repeated three times and gave similar results. Scale bar = 100 nm.

Ruiyi Ren, et al. J Biol Chem. 2010 November 26;285(48):37672-37682.
2.
FIGURE 8.

FIGURE 8. From: Role of Glycosaminoglycan Sulfation in the Formation of Immunoglobulin Light Chain Amyloid Oligomers and Fibrils.

Sulfated GAGs are detected along amyloid fibrils generated in vitro with HS. A, negatively stained AL κ1 protofibrils AL-00131 generated in vitro from urinary extracted LC protein. B, Cuprolinic blue (arrows)-stained AL κ1 protofibrils AL-00131 generated in vitro. C, negative control image of AL-00131 incubated in the absence of GAGs and stained with Cuprolinic blue. Scale bar = 10 nm.

Ruiyi Ren, et al. J Biol Chem. 2010 November 26;285(48):37672-37682.
3.
FIGURE 7.

FIGURE 7. From: Role of Glycosaminoglycan Sulfation in the Formation of Immunoglobulin Light Chain Amyloid Oligomers and Fibrils.

Sulfated GAG chains decorate ex vivo amyloid fibrils. A, negatively stained AL κ1 protofibrils (ap03-261) extracted from heart and imaged with TEM. B, Cuprolinic blue-stained protofibrils extracted from heart (arrows). C, Cuprolinic blue-stained protofibrils extracted from heart after heparinase digestion. D, Cuprolinic blue-stained AL-κ 98002 liver (arrows). The inset shows stained filaments along the AL fibrils (scale bar = 10 nm). E, Cuprolinic blue-stained AL-κ 98002 after heparinase digestion.

Ruiyi Ren, et al. J Biol Chem. 2010 November 26;285(48):37672-37682.
4.
FIGURE 5.

FIGURE 5. From: Role of Glycosaminoglycan Sulfation in the Formation of Immunoglobulin Light Chain Amyloid Oligomers and Fibrils.

AFM analysis of oligomers. AL-00131 was incubated in the presence or absence of GAGs. A, average grain height at maximum. Hep, heparin. B, average Z range. C, average root mean square (RMS) of AL-00131, with the presence or absence of GAGs, changing over time. D, average root mean square of myeloma MM96100, with the presence or absence of GAGs, changing over time. Experiments were repeated three times and gave similar results.

Ruiyi Ren, et al. J Biol Chem. 2010 November 26;285(48):37672-37682.
5.
FIGURE 1.

FIGURE 1. From: Role of Glycosaminoglycan Sulfation in the Formation of Immunoglobulin Light Chain Amyloid Oligomers and Fibrils.

Characteristics of amyloid fibrils extracted from tissue. A and B, characteristics of AL κ1 (AL-98002) protofibrils extracted from liver (A) and heart (B). AFM images are 250 × 250 nm. The line drawn through the image is represented graphically on the right, optimized for periodicity. White arrowheads indicate periodicity measurements, and gray arrowheads indicate height. Multiple measurements were made for these and other fibrils. C, height and periodicity of extracted fibrils (mean ± S.D.) and total GAG in extracted fibrils.

Ruiyi Ren, et al. J Biol Chem. 2010 November 26;285(48):37672-37682.
6.
FIGURE 6.

FIGURE 6. From: Role of Glycosaminoglycan Sulfation in the Formation of Immunoglobulin Light Chain Amyloid Oligomers and Fibrils.

Long term analysis of change in structure in the presence or absence of GAGs. AFM images of LCs in the presence or absence of GAGs over 2 weeks (1 × 1 μm). The circles indicate examples of the protofilaments and protofibrils formed over time. The structures were only detected in the presence of HS at 1 week. Experiments were repeated more than 20 times, with similar results. Scale bar = 100 nm.

Ruiyi Ren, et al. J Biol Chem. 2010 November 26;285(48):37672-37682.
7.
FIGURE 3.

FIGURE 3. From: Role of Glycosaminoglycan Sulfation in the Formation of Immunoglobulin Light Chain Amyloid Oligomers and Fibrils.

Sulfated GAGs alter ThT fluorescence of urinary LC AL-00131 in short term studies. A, LC (1 mg/ml) incubated in the presence or absence of GAGs in Tris-HCl (pH 7) at 60 °C and 250 rpm (ThT: excitation, 450 nm, emission, 482 nm). MW, molecular weight. B, LC (1 mg/ml) incubated in the presence or absence of HS, heparin, and heparin derivatives. C, myeloma LC (MM96100) incubated in the presence or absence of different GAGs under the same conditions. Experiments were repeated three times and gave similar results.

Ruiyi Ren, et al. J Biol Chem. 2010 November 26;285(48):37672-37682.
8.
FIGURE 2.

FIGURE 2. From: Role of Glycosaminoglycan Sulfation in the Formation of Immunoglobulin Light Chain Amyloid Oligomers and Fibrils.

Long term AFM and ThT fluorescence study demonstrates role of GAGs. A, urinary LC AL-00131 purified from urine (0.25 mg/ml) was incubated in the presence or absence of GAGs in Tris-HCl (pH 7) at 37 °C and 25 rpm for 200 h, and ThT fluorescence was measured over time. The experiment was repeated three times with comparable results. a.u., arbitrary units; MW, molecular weight. B, AFM of changes of urinary LC AL-00131 after 2 weeks of incubation. The LC oligomers (1) undergo a structural rearrangement and (2) aggregate to form protofilaments (3). The protofilaments can intertwine to form protofibrils (4). Protofibrils can either intertwine or fold to form fibrils. Each of these experiments was repeated more than 20 times. Scale bar = 100 nm.

Ruiyi Ren, et al. J Biol Chem. 2010 November 26;285(48):37672-37682.

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