Skip to main content
. 2014 Jul 30;87(1):74–84. doi: 10.1038/ki.2014.271

Figure 6.

Figure 6

Inflammasome activation in resident glomerular cells in diabetic nephropathy. Nlrp3 (nucleotide-binding domain and leucine-rich repeat pyrin 3 domain; red) colocalizes with markers for podocytes (synaptopodin, green, left) and endothelial cells (PECAM, green, right) in glomeruli of microalbuminuric diabetic patients (a), scale bar=20 μm. In glomeruli of 20-week-old db/db mice, cleaved caspase-1 (red) colocalizes with markers for podocyte (synaptopodin, green, left) and endothelial cell (CD34, green, right; b, scale bar=20 μm). Representative images of glomeruli obtained by confocal microscopy (Zeiss LSM 4 Pascal microscope, Carl Zeiss, Jena, Germany) and higher magnification of areas indicated by white dotted lines; yellow reflects colocalization (a, b). In mouse glomerular endothelial cells (GENC) and human podocytes (hPodo) glucose (Gluc, 25 mmol/l, 24 h) induces Nlrp3 and cleaved interleukin-1β (cl IL-1β) in comparison to control (C, phosphate-buffered saline) or mannitol (M, 25 mmol/l mannitol)-treated cells (c); representative immunoblots, β-actin as loading control. In primary podocytes isolated from C57BL/6 wild-type (WT), but not from caspase-1–deficient (casp1−/−) mice, cl IL-1β can be readily detected (d). Glucose (G, 25 mmol/l), but not mannitol (M, 25 mmol/l), induces cl IL-1β in WT, but not in caspapse-1–deficient podocytes (d); representative immunoblots, β-actin as loading control.