Gelatinases belong to a group of enzymes known as matrix metalloproteinases (MMPs). Gelatinases A and B (MMP-2 and MMP-9, respectively) are the enzymes with the highest ability to destroy collagen, primarily type IV collagen, which is an essential component of the base membrane. Hence, it can be assumed that they are involved, among other things, with the metastasis process of cancer. As a result, the objective of this study was to assess the presence, activity, and expression of selected gelatinases in human renal cancer. Healthy (n= 20) and clear-cell kidney cancer tissue samples (G2n= 10, G3n= 10) were analyzed. The presence and content of MMPs were measured using the Western blot and ELISA methods, respectively. The activity (actual and specific) was analyzed with a fluorimetric method. The presence of both investigated enzymes was demonstrated in the representative zymogram. MMP-9 showed the most intensive saturation. It has been observed that both gelatinases occur primarily in high molecular complexes in the human kidney, regardless of whether it is a control or tumor tissue. Both gelatinases were present in comparable amounts in healthy tissues of the kidney. MMP-9 showed a higher content than MMP-2 in both renal cancer grades, but we observed the enhanced activity of both gelatinases with an increase in the grade of renal cancer. A higher MMP-9 content and, on the other hand, lower specific activity in the cancer tissue suggest that MMP-9 is predominantly present in an inactive form in renal cancer. The higher activity of MMP-9 demonstrated using the zymography method may be a cause of different values of activity that depend on the phase of the carcinogenic process. The present study revealed changes in the tested gelatinases in healthy and cancerous tissues of renal cell carcinoma. Therefore, it can be concluded that matrix metalloproteinases 2 and 9 are enzymes directly involved in carcinogenesis, and hence, it seems that MMPs may have potential in the diagnosis and treatment of renal carcinoma.
明胶酶属于基质金属蛋白酶家族。其中明胶酶A和B（分别为MMP-2和MMP-9）具有最强的胶原降解能力，主要作用于基底膜关键组分IV型胶原。因此可推测该类酶参与癌症转移过程。本研究旨在评估特定明胶酶在人肾癌组织中的存在、活性及表达水平。通过分析健康肾组织（n=20）与透明细胞肾癌组织（G2级n=10，G3级n=10），分别采用蛋白质印迹法和酶联免疫吸附法检测MMPs的存在与含量，荧光法测定其实际活性与比活性。代表性酶谱图证实两种目标酶均存在，其中MMP-9显色强度最高。研究发现无论对照组织或肿瘤组织，两种明胶酶在人肾组织中均主要存在于高分子复合物中。健康肾组织中两者含量相当，而在两种分级肾癌组织中MMP-9含量均高于MMP-2，且随癌症分级升高，两种明胶酶活性均增强。癌组织中MMP-9含量更高但比活性更低的现象提示，MMP-9在肾癌中主要以前体形式存在。酶谱法显示的较高MMP-9活性可能源于致癌过程不同阶段的活性差异。本研究揭示了肾细胞癌健康与癌变组织中明胶酶的动态变化，由此证实基质金属蛋白酶2和9是直接参与致癌过程的酶类，表明MMPs在肾癌诊断与治疗中具有潜在应用价值。
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