Volume 55, Issue 3, Pages 899-906 (March 1999) Impaired lysosomal processing of β2-microglobulin by infiltrating macrophages in dialysis amyloidosis M.A.R. García-García, Àngel Argilés, Annie Gouin-Charnet, Mercè Durfort, José García-Valero, Georges Mourad Kidney International Volume 55, Issue 3, Pages 899-906 (March 1999) DOI: 10.1046/j.1523-1755.1999.055003899.x Copyright © 1999 International Society of Nephrology Terms and Conditions
Figure 1 Amyloid criteria: Congo red staining of a β2-microglobulin amyloid deposit observed under light microscopy (A) and under polarized light (B). The publication of this figure in color was made possible by a grant from Gambro Renal Care R&D, Lund, Sweden. Kidney International 1999 55, 899-906DOI: (10.1046/j.1523-1755.1999.055003899.x) Copyright © 1999 International Society of Nephrology Terms and Conditions
Figure 2 Amyloid deposit location and β2-microglobulin distribution. (Inset) Methylene blue staining showing the cell distribution around the amyloid fibrils. (a) Electron showing a cell engulfing an amyloid deposit (short thick arrows). Cellular processes are indicated by thin arrows (×18,000). Immunogold labeling with anti-β2-microglobulin antibody showing an extracellular (b) and intracellular (c) location of an amyloid deposit (×27,000). Kidney International 1999 55, 899-906DOI: (10.1046/j.1523-1755.1999.055003899.x) Copyright © 1999 International Society of Nephrology Terms and Conditions
Figure 3 Intracellular immunolocalization of β2-microglobulin. No labeling with anti-β2-microglobulin antibody was observed in endoplasmic reticulum (er) (a, ×33,000) nor in the Golgi compartment (g) (b, ×33,000). (c) Double immunolabeling for ×2-microglobulin (15 nm) and lysosome-associated protein (LAMP-1; 10 nm) showing that amyloid fibrils are within the lysosomes (×40,000). (d) Double immunolabeling for β2-microglobulin (15 nm) and CD68 (10 nm) confirming that amyloid fibrils are within the lysosomes and that the cells involved are of macrophage-monocytic lineage (×40,000). Kidney International 1999 55, 899-906DOI: (10.1046/j.1523-1755.1999.055003899.x) Copyright © 1999 International Society of Nephrology Terms and Conditions
Figure 4 Density labeling studies of β2-microglobulin and amyloid P component (APC): Comparison of intracellular and extracellular protein density. It can be observed that extracellular labeling of β2-microglobulin (a, ×27,000) was similar to that observed intracellularly (b, ×27,000), whereas a clear decrease in intracellular APC labeling (d, ×33,000) was observed when comparing with extracellular APC labeling (c ×37,800). Kidney International 1999 55, 899-906DOI: (10.1046/j.1523-1755.1999.055003899.x) Copyright © 1999 International Society of Nephrology Terms and Conditions
Kidney International 1999 55, 899-906DOI: (10. 1046/j. 1523-1755. 1999 Kidney International 1999 55, 899-906DOI: (10.1046/j.1523-1755.1999.055003899.x) Copyright © 1999 International Society of Nephrology Terms and Conditions