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. 2001 Jun;158(6):1921–1928. doi: 10.1016/S0002-9440(10)64660-3

Figure 2.

Figure 2.

A: MDA-MB-436 breast cancer cells transfected with EMMPRIN/GFP cDNA resulted in enhanced rate of tumor growth after tumor cell implantation into the mammary fat pad of nude mice as compared to GFP-transfected cells. The tumorigenicity of transfected cells was assessed by weekly measurement of tumor size. The data represent the mean ± SE observed in 10 animals in each group injected with 1 × 10 6 transfected cancer cells. The numbers associated with each symbol refer to the number of mice alive at each time point (ie, at week 8, three mice in the EMMPRIN/GFP group had large tumors and were sacrificed, hence the number seven is listed). B: GFP-transfected tumors are readily visible under fluorescent light. EMMPRIN/GFP-transfected MDA-MB-436 breast cancer cells were injected into the mammary tissue of a female NCr nu/nu mouse. Eight weeks later, the mouse was sacrificed and extensive green colored metastatic tumors in the peritoneum, liver, spleen, and mediastinum were visible under fluorescent light (left photo). The photo on the right demonstrates the same tumors visualized by bright light (arrowheads identify tumors). C: Comparison of gelatinases secreted by MDA-MB-436 cells cultivated in serum-free medium and extracts of nude mouse tumors. Spent serum-free conditioned medium from primary cells cultivated for 18 hours with vehicle (medium), PMA, and thrombin (left) and tumor cell extracts (right) were assessed by gelatin substrate zymography. Protein concentration (15 μg/well) of tissue samples was equalized within each group. Conditioned medium and tumor extracts from the EMMPRIN/GFP group displayed more gelatinolytic activity than did the GFP-alone group of mice. The displayed extract from the GFP-alone tumor is from the largest tumor (1.4 cm 3 ) in this group of mice. The intensity of tumor gelatinolytic activity demonstrated in each group of mice did not correlate with tumor size (data not shown). Molecular weights were calculated using protein standards. The conditioned medium of HT-1080 cells was used to confirm the molecular weight of human gelatinase A and gelatinase B (data not shown).

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