1,721,160 research outputs found
Gelatinolytic activities in the sera and in the urine from patients with prostate diseases
No full textThe role of matrix-metalloproteinase-2 (MMP-2) and matrix metalloproteinase-9 (MMP-9) in angiogenesis
No full textConcentrations and activities of metalloproteinases-2 and-9 and their inhibitors (TIMPS) in oncocytoma and clear cell renal carcinoma
No full textMatrix metalloproteinase-2 and-9 in the sera and in the urine of human oncocytoma and renal cell carcinoma
No full textMatrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases, capable of degrading all the molecular components of extracellular matrix. MMPs have 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 with kidney carcinoma by gelatin zymography. Of these patients, 16 had clear cell renal carcinoma (ccRCC) and 4 patients had oncocytoma. The sera and the urine of 16 healthy subjects were used as controls. In the sera, zymography analysis showed gelatinolytic 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 oncocytoma patients. 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 gelatinolytic activity, whereas MMPs could not be detected in the concentrated urine of healthy subjects. The most abundant lytic activity was at 92 kDa, whereas MMP-2 was present in lesser quantities. However, there was broad overlap of the data and we did not find any correlation to type, stage or grade. Therefore, despite previous evidence, MMP-2 and -9 activity in serum and urine may not be useful biomarker for kidney carcinomas
Matrix metalloproteinase-2 and-9 and tissue inhibitor of metalloproteinase-1 and-2 in sera and urine of patients with renal carcinoma
No full textThe matrix metalloproteinase (MMP) family has been shown to play a critical role in tissue remodeling and tumor infiltration. Their activity is normally strictly controlled by tissue inhibitors of metalloproteinases (TIMPs). However, TIMPs act indirectly through modulation of protease activity or directly through cell surface receptors to direct cell fate. These molecules have been proposed as markers of malignant cancer. Previous studies on MMP and TIMP expression in kidney carcinoma have been limited and have reported variable observations. The current study measured the content of MMP-2 and -9 and TIMP-1 and -2 in the sera and urine of patients with kidney carcinoma by enzyme-linked immunosorbent assay. Of these patients, 16 exhibited clear cell renal cell carcinoma (ccRCC) and 4 exhibited oncocytoma. Sera and urine samples of 53 healthy subjects were used as controls. In the sera of the control group, MMP-2 and TIMP-2 were detectable in all samples, while MMP-9 and TIMP-1 were below the sensitivity of the assay. In the pathological specimens, the mean serum values of MMP-2 and TIMP-1 and -2 were similar in the ccRCC and oncocytoma patients, whereas the value for MMP-9 was 2-fold higher in the ccRCC patients compared with the oncocytoma patients. With regard to the urine specimens, all four molecules were undetectable in the normal healthy samples and in a few pathological samples. The mean values for MMP-2 and -9 and TIMP-2 in the positive urine specimens were similar in the ccRCC and oncocytoma patients, whereas the mean value of TIMP-1 was higher in the ccRCC patients compared with that of the oncocytoma patients. The mean urinary levels of the four molecules were less than those of the sera. Statistical analysis of the data did not reveal any correlation between the tumor grades and expression levels of the molecules examined
Evaluation of neutrophil gelatinase-associated lipocalin (NGAL), matrix metalloproteinase-9 (MMP-9) and their complex MMP-9/NGAL in sera and urine of patients with kidney tumors
No full textRecent evidence suggests that neutrophil gelatinase-associated lipocalin (NGAL) is required for the development and/or progression of benign and malignant disease, and is overexpressed in several types of tumor. Matrix metalloproteinase-9 (MMP-9), by degrading components of the extracellular matrix and thus promoting the release of growth factors, is important in tumor growth and tumorigenicity. NGAL protects MMP-9 from proteolytic degradation and enhances its enzymatic activities by binding and forming the MMP-9/NGAL complex. Therefore, NGAL, MMP-9 and their complex MMP-9/NGAL have been proposed as soluble biomarkers for numerous malignancies. In the present study, we measured the concentration of these molecules in sera and urine of patients with kidney disease using ELISA. Of these patients, 16 had clear cell renal cell carcinoma (ccRCC) and 4 had oncocytoma. Sera and urine samples of 53 healthy patients were used as controls. In sera, MMP-9 was enhanced in ccRCC patients compared with oncocytoma patients. In urine, the most abundant molecule was NGAL and its mean value was higher in cancer patients. However, there was a broad overlap of the data and we did not identify any correlation with disease type, stage or grade. Therefore, these molecules may not be useful as biomarkers for predicting kidney carcinoma
The enigmatic role of lipocalin 2 in human cancer. The multifunctional protein neutrophil gelatinase-associated lipocalin (NGAL) and its ambiguous role in human neoplasias
No full textNeutrophil gelatinase-associated lipocalin (NGAL) has been originally identified as a 25 kDa protein covalently linked to
neutrophil gelatinase B. It is an acute phase protein involved in innate immunity with an important role in intracellular
iron transport.
It is currently one of the most ambiguous protein involved in tumorigenesis. In cancer development, its role is
contradictory and not yet completely clarified.
NGAL induces proliferation and angiogenesis, favorite invasion and metastasis. But it can also inhibits proliferation and induce apoptosis. It is likely that the dual contradictory effects of NGAL (pro-neoplastic and anti-tumoral) are neoplasiaspecific and influenced largely by the type of molecule it is complexed with
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