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

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Advanced Glycation End Product-Modified β2-Microglobulin is a Component of Amyloid Fibrils of Primary Localized Cutaneous Nodular Amyloidosis Norihiro Fujimoto, Mayumi Yajima, Yoshihiro Ohnishi, Shingo Tajima, Akira Ishibashi Journal of Investigative Dermatology Volume 118, Issue 3, Pages 479-484 (March 2002) DOI: 10.1046/j.0022-202x.2001.01695.x Copyright © 2002 The Society for Investigative Dermatology, Inc Terms and Conditions

Figure 1 Histochemistry and immunohistochemistry of amyloid deposit in the lesional skin of PLCNA (case 1). Paraffin-embedded skin sections were stained with (a) Congo red, or with the antibodies for (b) κ light chain, (c) λ light chain, (d) β2 M, (e) AGE Scale bars: 200 μm. Journal of Investigative Dermatology 2002 118, 479-484DOI: (10.1046/j.0022-202x.2001.01695.x) Copyright © 2002 The Society for Investigative Dermatology, Inc Terms and Conditions

Figure 2 Double immunofluorescence labeling of the lesional skin of PLCNA (case 1). The sections were stained with anti-β2M (left), anti-AGE (middle) or both (right) antibodies (A), or anti-β2 M (left), anti-κ light chain (middle) or both (right) antibodies (B). Scale bar: 100 μm. Journal of Investigative Dermatology 2002 118, 479-484DOI: (10.1046/j.0022-202x.2001.01695.x) Copyright © 2002 The Society for Investigative Dermatology, Inc Terms and Conditions

Figure 3 Water-extracted amyloid fibrils in the combined fractions I–V as visualized by negative staining.Scale bar: 100 nm. Journal of Investigative Dermatology 2002 118, 479-484DOI: (10.1046/j.0022-202x.2001.01695.x) Copyright © 2002 The Society for Investigative Dermatology, Inc Terms and Conditions

Figure 4 Immunoblotting analysis of amyloid protein recovered in five fractions. Amyloid proteins were serially extracted with distilled water and resolved on 10–20% gradient SDS–PAGE. The proteins were blotted on to nitrocellulose membranes and reacted with anti-κ light chain antibody (a), anti-β2 M antibody (b), anti-AGE antibody (c), or both anti-β2 M and anti-AGE antibodies (d). Antigen–antibody complex was detected by chemiluminescence. Molecular markers were indicated in the left side. Journal of Investigative Dermatology 2002 118, 479-484DOI: (10.1046/j.0022-202x.2001.01695.x) Copyright © 2002 The Society for Investigative Dermatology, Inc Terms and Conditions

Figure 5 Two forms of β2M are components of amyloid fibrils in PLCNA. Authentic β2M and the proteins in fractions I and V were resolved on two-dimensional PAGE, then transblotted on to membranes. The membrane were incubated with anti-β2M antibody at 1:1000 dilution for 2 h: (a) authentic β2 M; (b) the proteins in fraction I; (c) the proteins in fraction V; (d) the proteins in the mixture of fractions I and V; (e) authentic β2 M and the proteins in fraction V; (f) authentic β2M and the proteins in fraction I. Positive spots are indicated by arrows. Journal of Investigative Dermatology 2002 118, 479-484DOI: (10.1046/j.0022-202x.2001.01695.x) Copyright © 2002 The Society for Investigative Dermatology, Inc Terms and Conditions

Figure 6 β2M in fraction V but not in fraction I is modified by AGE. Authentic β2M and the proteins in fractions I and V were resolved on two-dimensional PAGE, then transblotted on to membranes. The membranes were incubated with anti-AGE antibody at 1:500 dilution for 24 h: (a) authentic β2 M and the proteins in fraction I; (b) authentic β2M and the proteins in fraction V. Positive spot is indicated by arrows. Journal of Investigative Dermatology 2002 118, 479-484DOI: (10.1046/j.0022-202x.2001.01695.x) Copyright © 2002 The Society for Investigative Dermatology, Inc Terms and Conditions