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. 1999 May 31;145(5):1009–1026. doi: 10.1083/jcb.145.5.1009

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Localization of cross-linking proteins in fibroblast cytoskeleton. (a–c) Fluorescence microscopy and corresponding intensity profiles (a′–c′) of Xenopus (a and c) or human 356 (b) fibroblast lamellipodia double stained with TRITC-phalloidin (red) and either p21 (a and a′), ABP-280 (b and b′), or α-actinin (c and c′) antibodies (green). The protein/actin ratio at the leading edge of the lamellipodium is high for Arp2/3 complex (a and a′), medium for ABP-280 (b and b′), and low for α-actinin (c and c′) compared with internal actin structures. (d–i) Immuno-EM of the cell edge (d–f) or interior (g–i) of CD-treated Xenopus (d, f, g, and i) or human 356 (e and h) fibroblasts stained with p21 (d and g), ABP-280 (e and h), or α-actinin (f and i) primary antibody and 10-nm (d, e, g, and h) or 18-nm (f and i) gold-conjugated secondary antibody. Gold particles (yellow) reveal Arp2/3 complex at Y-junctions at cell edge and ABP-280 and α-actinin at filament crossovers in the cell interior. Bars: (a–c) 1 μm; (d–i) 0.1 μm.