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Biology Articles » Methods & Techniques » Metabolic Mapping of Proteinase Activity with Emphasis on In Situ Zymography of Gelatinases : Review and Protocols » Figures

Figures
- Metabolic Mapping of Proteinase Activity with Emphasis on In Situ Zymography of Gelatinases : Review and Protocols

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Figure 1: Electron micrograph of an unfixed, permeabilized, isolated liver parenchymal cell incubated for demonstration of cathepsin B activity with Z-ala-arg-arg-4-methoxy-2-naphthylamide as substrate and hexazotized p-rosanilin as coupling reagent. After incubation, cells were fixed in a mixture of glutaraldehyde and formaldehyde, postfixed in a solution of osmium tetroxide, and embedded in Epon. Final reaction product is localized exclusively in lysosomes. Bar = 0.5 µm.

figure 1

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Figure 2 : Gelatin zymography of a homogenate of colon cancer metastases in mouse liver. ProMMP-9 (92 kD), proMMP-2 (72 kD), active MMP-9 (82 kD), and active MMP-2 (62 kD) are present.

figure 2

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Figure 3 : Principle of detection of activity of urokinase-type plasminogen activator (uPA) and tissue-type plasminogen activator (tPA).

figure 3

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Figures 4 and 5 : Figure 4 In situ zymography of gelatinolytic activity with DQ-gelatin as substrate in colon cancer metastasis in rat liver. Fluorescence due to gelatinolytic activity (green) was found in the extracellular matrix of tumors. Nuclei are shown in red. Bar = 35 µm. Figure 5 In situ zymography of urokinase-type plasminogen activator activity with Bodipy-casein as substrate and added plasminogen in colon cancer metastasis in mouse liver. Fluorescence due to caseinolytic activity (red) was found in intratumoral stroma of tumors. Nuclei are shown in green. Bar = 35 µm.

figure 4&5

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