Urinary gelatinase activities (matrix metalloproteinases 2 and 9) in human bladder tumors

Carlo, Angelina Di; Terracciano, Daniela; Mariano, Angela; Macchia, Vincenzo

doi:10.3892/or.15.5.1321

Cited by 28 publications

(31 citation statements)

References 18 publications

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“…Zymography was performed using 7.5 % (w/v) polyacrylamide gels containing 0.1% (w/v) of gelatine as previously described (8,9). Briefly, serum samples or concentrated urine samples were mixed with sample buffer (10 mM Tris-HCl pH 6.8, 12.5% SDS, 5% sucrose, 0.1% bromophenol blue) and applied directely without prior heating or reduction to the gel.…”

Section: Patientsmentioning

confidence: 99%

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

Carlo

2012

Oncology Reports

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Abstract. Matrix 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.

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Section: Patientsmentioning

confidence: 99%

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

Carlo

2012

Oncology Reports

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“…These zymographyc tests have some advantages over immunological assay such as lower cost, a more rapid time of execution and the possibility of simultaneously detecting multiple forms of the same enzyme. We have previously reported that urinary MMP-9 is increased in the high grade and advanced stage bladder cancers whereas only traces were detected in urine of healthy subjects (22), indicating that MMP-9 may be one of the important enzymes involved in the progression of neoplasias. Other researchers determined urinary MMPs lytic activity in urine from cancer patients (17) and they reported that MMP-9 was detected with higher frequency in the urine of patients with prostate cancer compared with those with bladder cancer.…”

Section: ------------------------------------------------------------mentioning

confidence: 99%

Matrix metalloproteinase-2 and -9 in the urine of prostate cancer patients

et al. 2010

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Abstract. The matrix metalloproteinase family of enzymes is comprised of critically important extracellular proteases whose activity has been implicated in a number of key normal and pathological processes. The latter include growth, progression and metastasis as well as dysregulated angiogenesis that is associated with these events. The MMPs are secreted by all types of cells, and they also carve through the extracellular matrix, allowing cancer cells to take root and metastasize. Endogenous inhibitors typically hold MMPs in check but in cancer, the balance shifts against the inhibitors and in favor of MMPs, which ultimately spill over from blood into urine. By gelatin zymography we verified MMP activity in concentrated urine of patients with prostate disease. Of these patients, 30 had cancer, consisting of 13 with Gleason score 6, 12 with Gleason 7, 2 with Gleason 8, 3 with Gleason 9 and 8 had benign prostate hyperplasia. Zymography showed 4 dominant gelatinolityc bands of 240, 130, 92 and 72 kDa in prostate disease. The most abundant lytic activity is at 92 kDa (MMP-9), whereas MMP-2 is present in lesser quantities. Moreover, MMP-9 activity is enhanced in the urine from patients with benign prostate hyperplasia compared with cancer patients. No correlation between gelatinolytic activity and Gleason score or pathological findings was found.

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“…8-well chamber slides were used to culture IOMM-Lee cells at a concentration of 5x10 3 per well. After a 24-h incubation period, cells were transfected with pSV, pCB, pM and pMC.…”

Section: Construction Of Sirna Plasmid Vectors Targeting Cathepsin Bmentioning

confidence: 99%

“…In vitro cell proliferation ability was determined as viable cell mass in both untreated IOMM-Lee cells and cells transfected with pSV, pM, pCB and pMC using Cell Titer 96™ colorimetric assay. IOMM-Lee cells (5x10 3 ) were cultured in triplicate in 96-well plates and transfected with 1 μg of one of the shRNA expressing plasmid vectors following standard protocol. Untreated cells were also maintained under similar conditions to serve as the control (mock).…”

Section: Construction Of Sirna Plasmid Vectors Targeting Cathepsin Bmentioning

confidence: 99%

“…Earlier studies have shown that during tumorigenesis, various proteolytic cascades consisting INTERNATIONAL JOURNAL OF ONCOLOGY 31: 1039-1050, 2007 RNAi-mediated abrogation of cathepsin B and MMP-9 gene expression in a malignant meningioma cell line leads to decreased tumor growth, invasion and angiogenesis of enzymes such as cysteine proteases, metalloproteinases (MMPs) and serine proteases act in a synchronized manner and aid in tumor growth, invasion into surrounding tissue, metastasis, etc. (2)(3)(4)(5). Tumorigenesis is a complex process that involves equal contribution from extracellular as well as intracellular proteolytic events (6).…”

Section: Introductionmentioning

confidence: 99%

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RNAi-mediated abrogation of cathepsin B and MMP-9 gene expression in a malignant meningioma cell line leads to decreased tumor growth, invasion and angiogenesis

et al. 2007

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Abstract. Malignant meningiomas are highly aggressive and frequently recur after surgical resection of the tumor. Earlier studies have reported that the cysteine protease cathepsin B and the matrix metalloproteinase MMP-9 play important roles in tumor progression. In the present study, we made an attempt to evaluate the roles of these proteases in the malignant meningioma tumor microenvironment and determined the effectiveness of using single or bicistronic siRNA constructs for cathepsin B and MMP-9, in both in vitro and in vivo models. Transfection of a plasmid vector expressing doublestranded RNA for cathepsin B and MMP-9 significantly inhibited mRNA and protein levels of cathepsin B and MMP-9. The migration and invasion of meningioma cells were decreased after treatment with single or bicistronic siRNA constructs for cathepsin B and MMP-9 compared to controls and vector controls. Inhibition of angiogenesis was observed when the cells were transfected with single or bicistronic constructs for cathepsin B and MMP-9, when compared to controls or empty vector controls. Our study revealed that abrogation of cathepsin B and MMP-9 expression decreased the activation of major proteins involved in MAP kinase and PI3 kinase pathways indicating that targeting these proteases may hinder intracellular signaling and thus decrease cell survival and proliferation in malignant meningiomas. In addition to the in vitro evidence, we observed a significant regression of pre-established orthotopic tumors after treatment with RNAi plasmid vectors targeting cathepsin B and MMP-9. Furthermore, these observations demonstrate that the simultaneous RNAi-mediated targeting of cathepsin B and MMP-9 has potential application for the treatment of human meningiomas.

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Urinary gelatinase activities (matrix metalloproteinases 2 and 9) in human bladder tumors

Cited by 28 publications

References 18 publications

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

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

Matrix metalloproteinase-2 and -9 in the urine of prostate cancer patients

RNAi-mediated abrogation of cathepsin B and MMP-9 gene expression in a malignant meningioma cell line leads to decreased tumor growth, invasion and angiogenesis

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