scholarly journals The Value of Combined Use of Survivin mRNA and Matrix Metalloproteinase 2 and 9 for Bladder Cancer Detection in Voided Urine

2013 ◽  
Vol 34 (1) ◽  
pp. 57-62 ◽  
Author(s):  
Sanaa Eissa ◽  
Soheir Badr ◽  
Shadia Abd Elhamid ◽  
Azza Salah Helmy ◽  
Mohamed Nour ◽  
...  
Keyword(s):  
Bladder Cancer ◽  
Matrix Metalloproteinase ◽  
Urothelial Carcinoma ◽  
Gelatin Zymography ◽  
Urine Cytology ◽  
Matrix Metalloproteinase 2 ◽  
Rt Pcr ◽  
Diagnostic Efficacy ◽  
Cancer Early Detection ◽  
Combined Use

Objective: In a trial to improve the diagnostic efficacy of conventional urine cytology we determine survivin RNA and matrix metalloproteinase 2 and 9 in urine of bladder cancer cases.Method: Voided urine specimens were collected from patients with histologically confirmed bladder urothelial carcinoma (Group 1;n= 46), urological patients without urothelial carcinoma (Group 2;n= 20), and healthy volunteers (Group 3;n= 20). Urine cytology, survivin RNA was estimated by qualitative nested RT-PCR and MMP-2, MMP-9 activity were detected by gelatin zymography. The expression of survivin RNA and matrix metalloproteinase 2 and 9 in bladder cancer was compared with benign and normal cases.Results: Positivity rates of survivin RNA and MMPs zymography were significantly different among the 3 groups. Urine survivin detection by qualitative nested RT-PCR showed 76.1% sensitivity and 95% specificity. The overall sensitivity, specificity of urinary MMP zymography was 67.3%, 90% respectively. The combined use of urine cytology with urine survivin or MMPs zymography increased sensitivity of urine cytology from 50% to 84.7%. The highest sensitivity (95.6%) was obtained on combining the three markers.Conclusion: Survivin RNA and MMPS zymography can be considered as promising noninvasive markers for bladder cancer early detection. Combined use of the three markers improved the sensitivity for detecting bladder cancer.

scholarly journals Suppressions of Migration and Invasion by Cantharidin in TSGH-8301 Human Bladder Carcinoma Cells through the Inhibitions of Matrix Metalloproteinase-2/-9 Signaling

2013 ◽  
Vol 2013 ◽  
pp. 1-8 ◽  
Author(s):  
Yi-Ping Huang ◽  
Chien-Hang Ni ◽  
Chi-Cheng Lu ◽  
Jo-Hua Chiang ◽  
Jai-Sing Yang ◽  
...  
Keyword(s):  
Bladder Cancer ◽  
Matrix Metalloproteinase ◽  
Cancer Cells ◽  
Cancer Metastasis ◽  
Gelatin Zymography ◽  
Matrix Metalloproteinase 2 ◽  
Migration And Invasion ◽  
Dependent Manner ◽  
Human Bladder Cancer ◽  
Human Bladder

Cancer metastasis becomes an initial cause of cancer death in human population. In many cancers, it has been shown that the high levels of matrix metalloproteinase (MMP)-2 and/or MMP-9 are associated with the invasive phenotypes of cancer cells. In this study, we investigated the effects of cantharidin, a derivative ofblister beetleswhich is one of the traditional Chinese medicines, on the adhesion, migration, and invasion of human bladder cancer TSGH-8301 cells. Cantharidin effectively suppressed TSGH-8301 cell adhesion, migration, and invasion in a concentration-dependent manner. Results from Western blotting, RT-PCR, and gelatin zymography assays indicated that cantharidin blocked the protein levels, gene expression (mRNA), and activities of MMP-2 and -9 in TSGH-8301 cells. Cantharidin also significantly suppressed the protein expressions of p-p38 and p-JNK1/2 in TSGH-8301 cells. Taken together, cantharidin was suggested to present antimetastatic potentialviasuppressing the levels of MMP-2 and MMP-9 expression that might be mediated by targeting the p38 and JNK1/2 MAPKs pathway in TSGH-8301 human bladder cancer cells.

scholarly journals Prognostic values of matrix metalloproteinase-2 and tissue inhibitor of metalloproteinase-2 expression in bladder cancer

Cancer ◽  
1998 ◽  
Vol 82 (7) ◽  
pp. 1359-1366 ◽  
Author(s):  
Hiro-omi Kanayama ◽  
Kin-ya Yokota ◽  
Yasushi Kurokawa ◽  
Yoshihide Murakami ◽  
Masaaki Nishitani ◽  
...  
Keyword(s):  
Bladder Cancer ◽  
Matrix Metalloproteinase ◽  
Tissue Inhibitor Of Metalloproteinase ◽  
Matrix Metalloproteinase 2 ◽  
Tissue Inhibitor

scholarly journals Lidocaine Alleviates Sepsis-Induced Acute Lung Injury in Mice by Suppressing Tissue Factor and Matrix Metalloproteinase-2/9

2021 ◽  
Vol 2021 ◽  
pp. 1-13
Author(s):  
Binbin Zheng ◽  
Hongbo Yang ◽  
Jianan Zhang ◽  
Xueli Wang ◽  
Hao Sun ◽  
...  
Keyword(s):  
Acute Lung Injury ◽  
Lung Injury ◽  
Matrix Metalloproteinase ◽  
Gelatin Zymography ◽  
Neutrophil Infiltration ◽  
Negative Regulator ◽  
Matrix Metalloproteinase 2 ◽  
Cytokine Signaling

Acute lung injury (ALI) is one of the fatal symptoms of sepsis. However, there were no effective clinical treatments. TF accumulation-induced fibrin deposit formations and coagulation abnormalities in pulmonary vessels contribute to the lethality of ALI. Suppressor of cytokine signaling 3 (SOCS3) acts as an endogenous negative regulator of the TLR4/TF pathway. We hypothesized that inducing SOCS3 expression using lidocaine to suppress the TLR4/TF pathway may alleviate ALI. Hematoxylin and eosin (H&E), B-mode ultrasound, and flow cytometry were used to measure the pathological damage of mice. Gelatin zymography was used to measure matrix metalloproteinase-2/9 (MMP-2/9) activities. Western blot was used to assay the expression of protein levels. Here, we show that lidocaine could increase the survival rate of ALI mice and ameliorate the lung injury of ALI mice including reducing the edema, neutrophil infiltration, and pulmonary thrombosis formation and increasing blood flow velocity. Moreover, in vitro and in vivo, lidocaine could increase the expression of p-AMPK and SOCS3 and subsequently decrease the expression of p-ASK1, p-p38, TF, and the activity of MMP-2/9. Taken together, our study demonstrated that lidocaine could inhibit the TLR4/ASK1/TF pathway to alleviate ALI via activating AMPK-SOCS3 axis.

scholarly journals Use of the Nuclear Matrix Protein 22 BladderChek Test for the Detection of Primary and Recurrent Urothelial Carcinoma

2020 ◽  
Vol 2020 ◽  
pp. 1-6
Author(s):  
Chang-sheng Xia ◽  
Chun-hong Fan ◽  
Ming Su ◽  
Qing-song Wang ◽  
Hui-zhang Bao
Keyword(s):  
Urothelial Carcinoma ◽  
Sensitivity And Specificity ◽  
Nuclear Matrix ◽  
Matrix Protein ◽  
Benign Disease ◽  
Urine Cytology ◽  
Nuclear Matrix Protein ◽  
Combined Use ◽  
Significant Difference ◽  
Low Sensitivity

Objective. To evaluate the performance of the nuclear matrix protein 22 (NMP22) BladderChek test in urothelial carcinoma (UC). Methods. We retrospectively analyzed 1318 patients who performed the NMP22 BladderChek tests. Of them, 103 were primary UC patients, 90 were surgical treatment UC patients, and 1125 were benign disease patients. The performance of the NMP22 BladderChek test for the diagnosis of primary and recurrent UC was evaluated. Moreover, the performance of urine cytology and the NMP22 BladderChek test for the diagnosis of primary UC was compared in 90 available subjects including 48 primary UC patients and 42 benign disease patients. Results. The sensitivity and specificity of the NMP22 BladderChek test were 37.9% and 95.8%, respectively, for the diagnosis of primary UC (n=1228). The corresponding parameters of the NMP22 BladderChek test were 31.0% and 88.5%, respectively, for the diagnosis of recurrent UC (n=90). The sensitivity and specificity of urine cytology were 54.2% and 97.6%, respectively, for the diagnosis of primary UC (n=90); the corresponding parameters of the NMP22 BladderChek test were 41.7% and 83.3%, respectively; the corresponding parameters of the two tests combination were 64.6% and 83.3%, respectively. There was a significant difference in the performance between the NMP22 BladderChek test and urine cytology or the combination of two tests (P=0.017 and 0.001, respectively). Conclusions. The NMP22 BladderChek test has a low sensitivity for detecting primary and recurrent UC. Urine cytology is superior to the NMP22 BladderChek test, and combined use of the two tests improves the sensitivity in the detection of primary UC.

The diagnostic efficacy of urinary TGF-β1 and VEGF in bladder cancer: Comparison with voided urine cytology

2007 ◽  
Vol 3 (6) ◽  
pp. 275-285 ◽  
Author(s):  
Sanaa Eissa ◽  
Ahmed M. Salem ◽  
Samir F. Zohny ◽  
Marwa G.A. Hegazy
Keyword(s):  
Bladder Cancer ◽  
Urine Cytology ◽  
Diagnostic Efficacy ◽  
Tgf Β1

scholarly journals In Vitro Evidence Suggests Activin-A May Promote Tissue Remodeling Associated with Human Luteolysis

Endocrinology ◽  
2007 ◽  
Vol 148 (8) ◽  
pp. 3730-3739 ◽  
Author(s):  
Michelle Myers ◽  
Eva Gay ◽  
Alan S. McNeilly ◽  
Hamish M. Fraser ◽  
W. Colin Duncan
Keyword(s):  
Granulosa Cells ◽  
Primary Cultures ◽  
Gelatin Zymography ◽  
Activin A ◽  
Primary Cell ◽  
Matrix Metalloproteinase 2 ◽  
Corpora Lutea ◽  
Type I ◽  
Rt Pcr ◽  
Maternal Recognition Of Pregnancy

Luteolysis in women is associated with an up-regulation of the expression and activity of matrix metalloproteinase-2 (MMP-2), which is inhibited by human chorionic gonadotropin (hCG) during maternal recognition of pregnancy. Because the primary source of MMP-2 is fibroblasts that do not express LH/hCG receptors, we aimed to investigate the regulation of MMP-2. Women with regular cycles having hysterectomy for nonmalignant conditions and women undergoing oocyte retrieval for assisted conception were used in this current study. Novel primary cultures and cocultures of luteinized granulosa cells and fibroblast-like cells in conjunction with human corpora lutea from different stages of the luteal phase were used to investigate the role of activin-A in the corpus luteum. The effect of hCG, activin-A, and follistatin on MMP-2 activity and expression was assessed by gelatin zymography and quantitative RT-PCR in primary cell cultures. Confirmation of signaling pathways involved in the activation of MMP-2 was assessed by immunofluorescence, RT-PCR, and quantitative RT-PCR. In primary cell culture, steroidogenic cells secrete activin-A and its inhibitors, inhibin-A and follistatin. Follistatin expression is up-regulated by hCG (P < 0.05). The fibroblast-like cells producing MMP-2 have the machinery for activin reception, expressing both type I and type II activin receptors and Smad proteins. Activin-A up-regulated both activity and expression of MMP-2 in fibroblast-like cells (P < 0.05). This activity was inhibited in cocultures of luteinized granulosa cells and fibroblast-like cells in the presence of hCG (P < 0.05) or follistatin (P < 0.01). Activin-A is an excellent candidate for an effector molecule in human luteolysis whose paracrine action is inhibited during maternal recognition of pregnancy.

scholarly journals Gelatinases Increase in Bleomycin-induced Systemic Sclerosis Mouse Model

2019 ◽  
Author(s):  
Fatemeh Vafashoar ◽  
Kazem Mousavizadeh ◽  
Hadi Poormoghim ◽  
Abbas Tavasoli ◽  
Tahereh Musavi Shabestari ◽  
...  
Keyword(s):  
Systemic Sclerosis ◽  
Mouse Model ◽  
Matrix Metalloproteinase ◽  
Gelatin Zymography ◽  
Gelatinolytic Activity ◽  
Matrix Metalloproteinase 2 ◽  
Control Group ◽  
Tissue Sections ◽  
Tissue Homogenates ◽  
And Control

Systemic sclerosis is a fibrotic autoimmune disease in which aberrant remodeling of the extracellular matrix in organs disturbs their functionalities. The aim of this study was to investigate the expression of gelatinases on systemic sclerosis. Consequently, a mouse model of systemic sclerosis was employed and the gelatinolytic activity of gelatinases was evaluated on the fibrotic tissues of this model. Two groups of ten mice were considered in this work: a group of systemic sclerosis model and control group. For the generation of systemic sclerosis model, mice received bleomycin, while the control group was subjected to phosphate buffered saline (PBS) reception. Mice were tested for fibrosis by using trichrome staining, hydroxyproline measurement and α-SMA detection in tissue sections. Additionally, the gelatinolytic activity of matrix metalloproteinase 2 and matrix metalloproteinase 9 were measured using gelatin zymography in lungs and skin tissue homogenates. The obtained results indicated that subcutaneous injection of bleomycin-induced fibrosis in skin and lung tissues of mice. Pro and active forms of matrix methaloproteinase 9 were increased in fibrotic lung tissues (p<0.05 and p<0.01, respectively), while, the gelatinolytic activity of MMP2 was unaffected in these tissues. Additionally, in skin tissues of bleomycin-treated animals, both pro and active forms of MMP9 and MMP2 were increased (p<0.05). Pro and active forms of gelatinases increase differently in skin and lung tissues of bleomycin-induced scleroderma.  

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