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Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases,capable of degrading all the molecular components of extracellular matrix. MMPshave been shown to play critical roles in tumor cell invasion and metastasis.We verified the activity of MMPs in the sera and in the urine of patients withkidney carcinoma by gelatin zymography. Of these patients, 16 had clear cell renalcarcinoma (ccRCC) and 4 patients had oncocytoma. The sera and the urine of 16healthy subjects were used as controls. In the sera, zymography analysis showedgelatinolytic bands at 72 kDa (gelatinase A) at 92, 130 and 240 kDa (gelatinase B).MMP-9 activity was slightly enhanced in sera from ccRCC compared with oncocytomapatients. Serum MMP-2 activity was similar in ccRCC and in oncocytoma patients.In the urine, 2 oncocytoma patients and 3 (33%) of the ccRCC patients showed gelatinolyticactivity, whereas MMPs could not be detected in the concentrated urine of healthysubjects. The most abundant lytic activity was at 92 kDa, whereas MMP-2 was presentin lesser quantities. However, there was broad overlap of the data and we didnot find any correlation to type, stage or grade. Therefore, despite previousevidence, MMP-2 and -9 activity in serum and urine may not be useful biomarkerfor kidney carcinomas.

Matrix metalloproteinase-2 and -9 in the sera and in the urine of human oncocytoma and renal cell carcinoma