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

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Presentation on theme: "Advanced Glycation End Product-Modified β2-Microglobulin is a Component of Amyloid Fibrils of Primary Localized Cutaneous Nodular Amyloidosis  Norihiro."— Presentation transcript:

1 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 (March 2002) DOI: /j x x Copyright © 2002 The Society for Investigative Dermatology, Inc Terms and Conditions

2 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  , DOI: ( /j x x) Copyright © 2002 The Society for Investigative Dermatology, Inc Terms and Conditions

3 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  , DOI: ( /j x x) Copyright © 2002 The Society for Investigative Dermatology, Inc Terms and Conditions

4 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  , DOI: ( /j x x) Copyright © 2002 The Society for Investigative Dermatology, Inc Terms and Conditions

5 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  , DOI: ( /j x x) Copyright © 2002 The Society for Investigative Dermatology, Inc Terms and Conditions

6 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  , DOI: ( /j x x) Copyright © 2002 The Society for Investigative Dermatology, Inc Terms and Conditions

7 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  , DOI: ( /j x x) Copyright © 2002 The Society for Investigative Dermatology, Inc Terms and Conditions

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