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1.
Artigo em Inglês | MEDLINE | ID: mdl-36231910

RESUMO

Stromelysin-1 and stromelysin-2 (matrix metalloproteinase 3; MMP-3 and matrix metalloproteinase 10; MMP-10, respectively) are enzymes that activate other metalloproteinases. Apart from collagen, they also degrade elastin, fibronectin, gelatin and laminin. In carcinogenic processes, they are involved in angiogenesis and metastasis. Therefore, the aim of this study was to evaluate the DNA content, expression and activity of both stromelysines in cancers of human kidney. Renal carcinoma tissue samples were analyzed. Low- and high-grade cancer tissues were collected. Control material was collected from part of the kidney opposite to the tumor. DNA content, stromelysines content and stromelysin-1 and stromelysin-2 activity were measured using ELISA and Western blot methods. A higher content of deoxyribonucleic acid in low- and high-grade cancer tissues in comparison to the respective control tissue was observed. Both stromelysines were presented in control and cancer tissues in high-molecular-weight complexes. The content of MMP-10 was significantly higher in comparison to MMP-3 in all investigated tissues. Moreover, the content of stromelysin-2 was significantly higher in high-grade (G3) tissues compared to grade 2 (G2) kidney cancer. A significant decrease in the actual and specific activities of both stromelysines was observed with the increase in renal cancer grade. The presented results may indicate that the degradation of extracellular matrix increases with a higher grade of cancer. Moreover, the elevated content and decreased specific activity of stromelysin-2 in cancer tissue indicate that MMP-10 is mainly present in an inactive form in renal carcinoma. Detailed knowledge of the mechanism and participation of stromelysines in extracellular matrix degradation may be important in understanding the pathomechanism of renal cancer development. Therefore, the potential application of stromelysines in the monitoring or prognosis of kidney cancer should be discussed.


Assuntos
Carcinoma de Células Renais , Neoplasias Renais , Metaloproteinase 10 da Matriz/metabolismo , Metaloproteinase 3 da Matriz/metabolismo , Colágeno , DNA , Elastina , Fibronectinas/metabolismo , Gelatina , Humanos , Laminina , Metaloendopeptidases/genética , Metaloendopeptidases/metabolismo
2.
J Clin Med ; 10(16)2021 Aug 19.
Artigo em Inglês | MEDLINE | ID: mdl-34441979

RESUMO

Human urinary bladder cancer is a huge worldwide oncological problem causing many deaths every year. The degradation of extracellular matrix (ECM) induced by molecules such as matrix metalloproteinases (MMPs) is one of the main factors influencing the process of metastasis origination. The MMP expression is tied to tumor aggressiveness, stage, and patient prognosis. The cleavage of constituent proteins is initiated and prolonged by matrix metalloproteinases, such as MMP-3 and MMP-10. The aim of this study was to evaluate the expression and activity of both MMPs in human urinary bladder cancer occurring at various stages of the disease. Tissue samples from patients with urinary bladder cancer were analyzed. Samples were collected from patients with a low- and high-grade cancer. Control tissue was collected from the site opposite to the tumor. DNA content, MMPs content, and activity of MMP-3 and MMP-10 were measured using ELISA and Western blot techniques. MMP-3 and MMP-10 occur in high molecular complexes in human urinary bladder in healthy and cancerous tissues. Particularly, in high-grade tumors, the content of MMP-10 prevails over MMP-3. The actual and specific activities vary in both grades of urinary bladder cancer; however, the highest activity for MMP-3 and MMP-10 was found in low-grade tissues. In conclusion, MMP-10 had a higher content, but a lower activity in all investigated tissues compared to MMP-3. Generally, obtained results demonstrated a contrary participation of MMP-3 and MMP-10 in ECM remodeling what may be crucial in the pathogenesis of human urinary bladder carcinoma.

3.
Medicine (Baltimore) ; 99(7): e19224, 2020 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-32049862

RESUMO

BACKGROUND: Human urinary bladder cancer is one of the most common cancers worldwide with the mortality rate of approximately 165,000 people annually. The modulation of extracellular matrix is a crucial event in the metastatic spread, among others in angiogenesis. It is initiated and prolonged by the cascade of matrix metalloproteinases. MMP-14 and MMP-15 are associated with a high degree of malignancy, aggressiveness, and survival prognosis by the activation of other matrix metalloproteinases (MMPs). This study was aimed at evaluating the expression and the activity of selected transmembrane metalloproteinases at different stages of human urinary bladder cancer. METHODS: Western blot and enzyme linked immunosorbent assay (ELISA) method were used to evaluate the expression and content of MMPs and TIMP-1. The activity of studied enzymes was determined with fluorometric method. RESULTS: Both transmembrane metalloproteinases are found in healthy or cancerous tissue in high molecular complexes of human urinary bladder. MMP-14 dominates over MMP-15, particularly in high-grade urinary bladder cancer. Their contents significantly change with the grade of bladder tumor. The amount of MMP-14 increases with increasing grade of tumor. MMP-15 content decreases in high-grade bladder cancer. With increasing grade of urinary bladder cancer their actual activity (per kg of total protein content) is varying in different ways. In all examined tissues, the specific activity of MMP-15 (per kg of the enzyme content) is much higher in comparison to MMP-14. Human urinary bladder cancer contains higher TIMP-1 amounts than control tissue but with the decrease with an increase in tumor grade. CONCLUSION: Comparison of investigated enzymes' activity and the inhibitor content suggests it opposite effects, higher suppression of MMP-14 than MMP-15 activity in low-grade bladder cancer and reverse TIMP-1 action in high-grade cancer. The MMP-14 activity determination in urinary bladder cancer tissue may be used as a predictor of a risk of metastasis.


Assuntos
Carcinoma/enzimologia , Metaloproteinase 14 da Matriz/metabolismo , Metaloproteinase 15 da Matriz/metabolismo , Inibidor Tecidual de Metaloproteinase-1/metabolismo , Neoplasias da Bexiga Urinária/enzimologia , Estudos de Casos e Controles , Humanos
4.
Mol Cell Probes ; 49: 101488, 2020 02.
Artigo em Inglês | MEDLINE | ID: mdl-31733276

RESUMO

OBJECTIVES: Peyronie's disease (PD) is accompanied by remodelling of connective tissue into fibrotic plaque. Treatment of the inflammatory and fibrotic phases of the disease is not established. The aim of the study was to evaluate the effect of verapamil (VER) and bacterial collagenase (COLL) on collagen metabolism and cell migration in fibroblasts with experimental wound healing and inflammation as an in vitro model of PD. MATERIALS AND METHODS: In vitro model of PD was designed using experimental model of inflammation induced by Interleukin-1 (IL-1) in cultured fibroblasts and mechanical damage of the cells. Cell viability, cell proliferation, collagen biosynthesis, prolidase activity and cell migration were studied in both models of the cells treated with VER and COLL. RESULTS: VER decreased cell viability, DNA and collagen biosynthesis and increased prolidase activity in control fibroblast, while in "wounded" fibroblasts it significantly decreased all the processes. COLL did not affect cell viability and DNA biosynthesis, while inhibited collagen biosynthesis and prolidase activity in both control and "wounded" fibroblasts. In IL-1-treated fibroblasts VER inhibited all studied processes except prolidase activity, while COLL inhibited only collagen biosynthesis and prolidase activity. COLL accelerated cell migration, while VER attenuated the process in fibroblast model of wound healing, compared to control cells. CONCLUSION: VER and COLL attenuate collagen biosynthesis in both fibroblast models. The VER-dependent inhibition of collagen biosynthesis was accompanied by inhibition of DNA biosynthesis at high prolidase activity, while COLL affected this process through inhibition of prolidase activity at high rate of DNA biosynthesis. It shows that anti-fibrotic activity of VER/COLL and anti-inflammatory activity of VER may represent approach to establish standard treatment of PD.


Assuntos
Colágeno/metabolismo , Modelos Biológicos , Induração Peniana/tratamento farmacológico , Induração Peniana/metabolismo , Verapamil/farmacologia , Animais , Linhagem Celular , Movimento Celular/efeitos dos fármacos , Sobrevivência Celular/efeitos dos fármacos , DNA/biossíntese , Dipeptidases/metabolismo , Fibroblastos/efeitos dos fármacos , Fibroblastos/metabolismo , Humanos , Masculino , Induração Peniana/patologia , Cicatrização/efeitos dos fármacos
5.
Pathobiology ; 86(4): 201-207, 2019.
Artigo em Inglês | MEDLINE | ID: mdl-31129674

RESUMO

BACKGROUND: Collagenases are enzymes starting collagen degradation. The role of collagenases in renal carcinoma development is not well understood. OBJECTIVE: Evaluation of collagen content and collagenase expression and activity in human kidney cancers. METHODS: Collagen content was measured by the hydroxyproline assay. The expression and the content of collagenases were evaluated by Western blotting and ELISA. Fluorogenic substrate was used to measure enzyme activity. RESULTS: Collagen content significantly decreases with the progression of kidney cancer. Both collagenases are first present in high molecular complexes in both control and cancer tissue. The healthy part of the kidney contains similar amounts of both collagenases. Collagenase content decreased significantly in tumor tissue with increasing cancer stage. MMP-13 activity is much higher than that of MMP-1 in all tissues investigated. We observed increasing collagenase activity (MMP-1 and MMP-13) with increasing renal cancer grade. CONCLUSIONS: The lower content and higher activity of the collagenases investigated in cancer tissue indicate that most of these enzymes are in active form in renal carcinoma. The lower collagen content in cancer tissue can be explained at least in part by increased collagenase activity.


Assuntos
Carcinoma de Células Renais/genética , Neoplasias Renais/genética , Metaloproteinase 13 da Matriz/metabolismo , Metaloproteinase 1 da Matriz/metabolismo , Idoso , Carcinoma de Células Renais/enzimologia , Colágeno/metabolismo , Feminino , Expressão Gênica , Humanos , Hidroxiprolina/metabolismo , Neoplasias Renais/enzimologia , Masculino , Metaloproteinase 1 da Matriz/genética , Metaloproteinase 13 da Matriz/genética , Pessoa de Meia-Idade
6.
Ann Agric Environ Med ; 24(4): 602-605, 2017 Dec 23.
Artigo em Inglês | MEDLINE | ID: mdl-29284232

RESUMO

INTRODUCTION AND OBJECTIVES: Many epidemiological and experimental studies report a strong role of chemical carcinogens in the etiology of bladder cancer. However, the involvement of heavy metals in tumourigenesis of urothelial carcinoma of the bladder has been poorly investigated. Therefore, the aim of this study was to examine the relationship between chromium (Cr) and bladder cancer. MATERIAL AND METHODS: Chromium concentration in two 36-sample series of bladder cancer tissue and sera from patients with this neoplasm were matched with those of a control group. The amount of trace elements in every tissue sample was determined using atomic absorption spectrometry. This was correlated with tumour stage. RESULTS: While the median chromium concentration levels reached statistically higher values in the bladder cancer tissue, compared with the non-cancer tissue (99.632ng/g and 33.144ng/g, respectively; p<0.001), the median Cr levels in the sera of the patients with this carcinoma showed no statistical difference when compared to those of the control group (0.511µg/l and 0.710µg/l, respectively; p=0.408). The median levels of Cr in the bladder tissue, depending on the stage of the tumour, compared with the tissue without the neoplasm, observed the same relationship for both non-muscle invasive and muscle-invasive tumours (p<0.001 and p<0.01, respectively). CONCLUSIONS: This study shows that patients with urothelial carcinoma of the bladder had higher tissue Cr levels than people without tumour, while no difference was found in the Cr serum levels between the two groups of patients under investigation.


Assuntos
Carcinoma/metabolismo , Cromo/metabolismo , Neoplasias da Bexiga Urinária/metabolismo , Adulto , Idoso , Idoso de 80 Anos ou mais , Carcinoma/sangue , Carcinoma/patologia , Cromo/sangue , Feminino , Humanos , Masculino , Pessoa de Meia-Idade , Estadiamento de Neoplasias , Bexiga Urinária/metabolismo , Neoplasias da Bexiga Urinária/sangue , Neoplasias da Bexiga Urinária/patologia
7.
Acta Biochim Pol ; 64(3): 465-470, 2017.
Artigo em Inglês | MEDLINE | ID: mdl-28742884

RESUMO

Cancer cells are characterized by an aberrant increase in protein N-glycosylation and by disruption of E-cadherin-mediated adherens junctions. However, the relationship between alterations in N-glycosylation process and loss of E-cadherin adhesion in cancer remains unclear. The mechanisms of altered expression of adhesive glycoproteins in cancer cells have not been fully elucidated. Thus, the aim of this study was to examine the expression of E-cadherin and sialyl Lewisa/x, NeuAcα2-3Gal, NeuAcα2-6Gal/GalNAc structures in the normal renal tissue and intermediate and cancerous tissues from patients with clear cell RCC. Moreover, we attempted to correlate the E-cadherin expression with some specific sugar residues of renal cancer tissue glycoproteins. The expression of E-cadherin was analysed using ELISA test and immunoblotting. Oligosaccharide structures and sialylation level were detected with ELISA test using specific biotinylated lectins or antibodies. A significant decrease of E-cadherin expression as well as a significant increase in sialylated oligosaccharides level in intermediate zone and renal cancer tissue in comparison to normal renal tissue are reported. Significant decrease in expression of cadherins and increase in sialylation of oligosaccharide structures in renal cancer tissue in comparison to normal renal tissue, and in renal cancer tissue in comparison to intermediate zone of renal tissue, are important for the future research concerning detection and quantification of cadherins and sialylated oligosaccharide structures in urine and cells of urinary sediment as possible non-invasive marker of early RCC.


Assuntos
Caderinas/metabolismo , Carcinoma de Células Renais/metabolismo , Neoplasias Renais/metabolismo , Acetilglucosamina/metabolismo , Idoso , Antígenos CD , Carcinoma de Células Renais/patologia , Feminino , Glicoconjugados/metabolismo , Glicoproteínas/metabolismo , Humanos , Rim/metabolismo , Neoplasias Renais/patologia , Antígenos CD15/metabolismo , Masculino , Pessoa de Meia-Idade , Valores de Referência , Ácidos Siálicos/metabolismo
8.
J Membr Biol ; 248(2): 301-7, 2015 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-25572835

RESUMO

Phenomena associated with changes in cell membranes are thought to play an important role in the cancer transformation. We hypothesized that the electrical charge of tumor cells can indirectly represent membrane-based changes that have occurred during cell transformation and may indicate tumor cell status. Here, we describe work showing that phospholipids, proteins content, and electric charge, are all altered in the cell membranes of pT2 stage/grade G3 bladder cancer. Qualitative and quantitative phospholipid composition and the presence of integral membrane proteins were identified using high-performance liquid chromatography. Protein composition was determined using selective hydrolysis of isolated bladder cell membrane proteins and peptide resolution. The surface charge density of human bladder cell membranes was determined using electrophoresis. Our results show that cancer transformation is associated with increased phospholipid levels and a decreased level of integral proteins. Moreover, the process of cancer transformation significantly enhanced changes in the surface charge density of the human bladder cell membrane. In conclusion, this study demonstrates that cell membrane structure and function are modified in bladder cancer cells and that further work in this area is warranted.


Assuntos
Membrana Celular/metabolismo , Transformação Celular Neoplásica/metabolismo , Bexiga Urinária/metabolismo , Idoso , Aminoácidos/química , Linhagem Celular Tumoral , Membrana Celular/química , Feminino , Humanos , Masculino , Proteínas de Membrana/química , Proteínas de Membrana/metabolismo , Pessoa de Meia-Idade , Peptídeos/química , Fosfolipídeos/química , Bexiga Urinária/patologia
9.
Pol J Pathol ; 65(1): 55-9, 2014 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-25119010

RESUMO

The aim of this study was to examine the relationship between cadmium (Cd) and bladder cancer (urothelial carcinoma of the bladder). Cadmium concentrations in two 36-sample series of bladder cancer tissue and blood, from patients with the neoplasm, were matched with those of the control group. The amount of heavy metal in every tissue sample was determined using atomic absorption spectrometry. This was correlated with tumour stage. While the median cadmium concentration levels reached statistically lower values in the bladder cancer tissue, as compared with the non-cancer one (11.695 ng/g and 56.32 ng/g respectively, p < 0.001), the median Cd levels in the blood of the patients with this carcinoma showed no statistical difference when compared to those of the control group (8.237 µg/l and 7.556 µg/l respectively, p = 0.121). The median levels of cadmium in the bladder tissue, depending on the stage of the tumour, compared with the tissue without the neoplasm, observed the same relationship for both non-muscle invasive and muscle-invasive tumours (p < 0.002 and p < 0.02 respectively). This study has shown that patients with urothelial carcinoma of the bladder had lower tissue cadmium levels than people without tumour while no difference in the Cd blood levels between the two groups of patients under investigation was found.


Assuntos
Cádmio/metabolismo , Carcinoma de Células de Transição/metabolismo , Carcinoma de Células de Transição/patologia , Neoplasias da Bexiga Urinária/metabolismo , Neoplasias da Bexiga Urinária/patologia , Adulto , Idoso , Idoso de 80 Anos ou mais , Feminino , Humanos , Masculino , Pessoa de Meia-Idade , Estadiamento de Neoplasias , Urotélio/metabolismo , Urotélio/patologia
10.
J Membr Biol ; 246(5): 421-5, 2013 May.
Artigo em Inglês | MEDLINE | ID: mdl-23649039

RESUMO

Phospholipids are ubiquitous in nature and are essential for the lipid bilayer of cell membranes. Their structural and functional properties are pivotal for the survival of the cell. In this study the phospholipids of healthy and cancerous human renal tissues from the same patients are compared with special reference to the electric charge of the membrane. A simple and highly effective normal-phase method is described for analyzing phospholipids content. This work is focused on changes of phospholipids content (PtdIns, phosphatidylinositol; PtdSer, phosphatidylserine; PtdEtn, phosphatidylethanoloamine; PtdCho, phosphatidylcholine) in cell membranes of renal cancer of pT1 stage, G2 grade, without metastasis. Surface charge density of healthy and cancerous human renal tissues was measured by electrophoresis. The measurements were carried out at various pH of solution. Depending on the surface charge density as a function of pH, acidic (C(TA)) and basic (C(TB)) functional group concentrations and their average association constants with hydrogen (K(AH)) or hydroxyl (K(BOH)) ions were evaluated. The process of cancer transformation was accompanied by an increase in total amount of phospholipids as well as an increase in C(TA) and K(BOH), whereas K(AH) and C(TB) were decreased compared with unchanged tumor cells.


Assuntos
Membrana Celular/metabolismo , Neoplasias Renais/metabolismo , Rim/metabolismo , Metabolismo dos Lipídeos , Fosfolipídeos/metabolismo , Adulto , Idoso , Membrana Celular/patologia , Feminino , Humanos , Rim/patologia , Neoplasias Renais/patologia , Masculino , Pessoa de Meia-Idade , Estadiamento de Neoplasias
11.
Folia Histochem Cytobiol ; 50(4): 599-604, 2012.
Artigo em Inglês | MEDLINE | ID: mdl-23264225

RESUMO

Cancer development is associated with the improper glycosylation of proteins. There are alterations in the synthesis and expression of sugar structures. These changes can be important not only in the early stages of tumour development, but also in the next stages connected with cancer invasiveness and its ability to form metastases. Oligosaccharide structures of glycans in tumours deviate from normal cells. Relatively increased degrees of branching and sialylation of N-glycans, enhanced presentation of short-chain mucin-type O-glycans with sialylation, and alterations in the expression of blood group ABO and Lewis epitopes can be observed. The main aim of our study was to assess changes in the glycosylation of proteins in clear cell renal cell carcinoma. This study was performed on tissues taken from 15 patients. The relative amounts of sugar structures of proteins with molecular mass above 30 kDa in tumour (cancer tissue), intermediate zone i.e. tumour-adjacent tissue, and normal tissue uninvolved by tumour, were determined by ELISA-like test with biotinylated lectins highly specific to examined sugar antigens. A higher expression of all examined structures was revealed in cancer tissue. Increased levels of sialic acid, fucose, T and Tn antigens, compared to healthy renal tissue, were characteristic for clear cell renal cell carcinoma.


Assuntos
Saúde , Neoplasias Renais/metabolismo , Neoplasias Renais/patologia , Rim/metabolismo , Rim/patologia , Proteínas/metabolismo , Idoso , Feminino , Glicosilação , Humanos , Lectinas/metabolismo , Masculino , Pessoa de Meia-Idade , Estadiamento de Neoplasias , Estatísticas não Paramétricas , Carga Tumoral
12.
Urol Int ; 89(3): 342-7, 2012.
Artigo em Inglês | MEDLINE | ID: mdl-23006800

RESUMO

INTRODUCTION: Many epidemiological and experimental studies report a strong role of chemical carcinogens in the etiology of bladder cancer. However, involvement of trace elements in the tumorigenesis of transitional cell carcinoma of the bladder has been poorly investigated. The aim of this study was to examine the relationship between zinc, copper and bladder cancer. MATERIALS AND METHODS: Zinc and copper concentration and Cu/Zn ratio in two 36-sample series of bladder cancer tissue and sera from patients with this neoplasm were matched with those of the control group. The amount of trace elements in every tissue sample was determined using atomic absorption spectrometry. This was correlated with tumor stage. RESULTS: While the copper concentrations reached statistically higher values in the bladder cancer tissue, the zinc levels in the sera and bladder tissue of the patients with this carcinoma were substantially lower as compared to those of the control group. The serum Cu/Zn ratio was significantly higher in the bladder cancer group and this increase was greater in the patients with muscle-invasive neoplasm. CONCLUSIONS: The results obtained suggest a relationship between trace elements and the bladder cancer.


Assuntos
Carcinoma de Células de Transição/sangue , Cobre/sangue , Neoplasias da Bexiga Urinária/sangue , Zinco/sangue , Adulto , Idoso , Idoso de 80 Anos ou mais , Feminino , Humanos , Masculino , Pessoa de Meia-Idade , Espectrofotometria Atômica/métodos , Oligoelementos
13.
Nutr Cancer ; 61(5): 629-33, 2009.
Artigo em Inglês | MEDLINE | ID: mdl-19838936

RESUMO

The aim of this study was to determine serum levels of selenium (Se) in patients with larynx and urinary system cancers. We also estimated the influence of dietary habits on Se status in examined patients. The mean content of Se in serum of patients with urinary system cancer (48.94 +/- 16.3 mu/l) and larynx cancer (51.00 +/- 18.6 mu/l) was lower than the mean content of Se in the control group (68.25 +/- 15.6 mircog/l; P = 0.000006 or 64.03 +/- 16.8 microg/l; P = 0.0112, respectively). In tissue only, the mean level of Se in patients with kidney cancer (75.37 +/- 40.3 mircog/l) was lower to compare with the dead body control group (220.68 +/- 83.6 microg/l). We have observed the correlation between the content of Se in serum and tissue (r = 0.297; P = 0.002). Patients with studied cancers have deficiency of Se in serum and kidney tissue, and it depends on the diet in about 30%. Frequent consumption of eggs, ham, and wine has the biggest influence on the content of Se in serum of patients in Poland, whereas frequent consumption of pulses, eggs, bacon, and lard is connected with the content of Se in tissue.


Assuntos
Dieta , Comportamento Alimentar , Alimentos , Neoplasias Laríngeas/sangue , Estado Nutricional , Selênio/sangue , Neoplasias Urológicas/sangue , Adulto , Idoso , Idoso de 80 Anos ou mais , Índice de Massa Corporal , Inquéritos sobre Dietas , Feminino , Humanos , Neoplasias Laríngeas/química , Masculino , Pessoa de Meia-Idade , Polônia , Análise de Regressão , Fatores de Risco , Selênio/análise , Selênio/deficiência , Neoplasias Urológicas/química
14.
Scand J Urol Nephrol ; 43(6): 467-70, 2009.
Artigo em Inglês | MEDLINE | ID: mdl-19707952

RESUMO

OBJECTIVE: To investigate the relationship between lead and bladder cancer. MATERIAL AND METHODS: The levels of lead concentration in blood and bladder cancer tissue from a sample set of 36 bladder cancer patients were measured and then compared with those of a normal group. The levels of lead obtained in the bladder cancer tissue were evaluated depending on the stage of the tumour. The level of lead concentration in each tissue sample was determined by atomic absorption spectrometry. RESULTS: The lead concentration reached statistically higher values in both the bladder cancer tissue and the blood of patients with this carcinoma compared with those of the control group. No relationship between lead concentration levels in the bladder cancer tissue and blood of patients with this neoplasm on stage of tumour was demonstrated. CONCLUSION: The results suggest that there is a relationship between exposure to lead and the initialization and development of bladder cancer.


Assuntos
Carcinoma de Células de Transição/metabolismo , Chumbo/metabolismo , Neoplasias da Bexiga Urinária/metabolismo , Bexiga Urinária/metabolismo , Adulto , Idoso , Idoso de 80 Anos ou mais , Carcinoma de Células de Transição/patologia , Estudos de Casos e Controles , Feminino , Humanos , Masculino , Pessoa de Meia-Idade , Estadiamento de Neoplasias , Estudos Retrospectivos , Bexiga Urinária/patologia , Neoplasias da Bexiga Urinária/patologia
15.
Clin Biochem ; 42(15): 1565-7, 2009 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-19615986

RESUMO

OBJECTIVES: To compare N-acetyl-beta-hexosaminidase (HEX) activity in the serum and urine of smokers as well as non-smokers with renal cancer, and healthy people. DESIGN AND METHODS: To assess hexosaminidase activity the level of p-nitrophenol released from p-nitrophenol derivatives was measured. RESULTS: The activity of enzyme was significantly higher in cancer group, with the highest activity in non-smokers. CONCLUSIONS: Cigarette smoking can inhibit, by the influence on HEX activity, catabolism of oligosaccharide chains in cancer tissues.


Assuntos
Neoplasias Renais , Fumar , beta-N-Acetil-Hexosaminidases , Biomarcadores Tumorais/sangue , Biomarcadores Tumorais/urina , Humanos , Neoplasias Renais/sangue , Neoplasias Renais/enzimologia , Neoplasias Renais/urina , Nitrofenóis/metabolismo , Oligossacarídeos/metabolismo , Fatores de Risco , Fumar/sangue , Fumar/urina , beta-N-Acetil-Hexosaminidases/sangue , beta-N-Acetil-Hexosaminidases/urina
16.
Pol Merkur Lekarski ; 19(112): 596-9, 2005 Oct.
Artigo em Polonês | MEDLINE | ID: mdl-16379335

RESUMO

Many studies have been carried out to develop unfailing diagnostic methods that could improve cancer detection. There are available cancer markers of relatively low sensitivity and specificity, which makes a reason why they not always let detect neoplasm at their earliest stage. There is a new protease cysteine enzyme named cancer procoagulant (CP) isolated from rabbit V2 Ca neoplasm and characterized by Gordon et al in 1975. Because of its exclusive presentation in the cancer tissues and blood serum of the patients with tumor, this neoplasm-cell-originated protein seems to be a new biochemical cancer disease marker. The elevated activity of CP was found in the cancers of pancreatic, breast, lung, alimentary and urinary system. The blood serum CP activity levels in the patients with renal, bladder, and prostate cancers were determined statistically higher as compared to controls but the difference varied depending on the mentioned organ of the urinary system. The CP highest activity levels was determined in the patients with prostate cancer, lower ones in bladder carcinoma ones and the lowest ones in individuals with renal tumours. That is why it appears to be justifiable to apply the determination of the CP in the oncological diagnosis in the urinary system.


Assuntos
Biomarcadores Tumorais/metabolismo , Cisteína Endopeptidases/metabolismo , Proteínas de Neoplasias/metabolismo , Neoplasias Urológicas/diagnóstico , Neoplasias Urológicas/metabolismo , Animais , Humanos , Estadiamento de Neoplasias , Sensibilidade e Especificidade
17.
Przegl Lek ; 62(3): 169-72, 2005.
Artigo em Polonês | MEDLINE | ID: mdl-16171148

RESUMO

Epidemiological studies point out steady increase of the incidence of cancer disease in Poland and all over the world. Neoplasms are associated with blood coagulation disorders very frequently. The investigations concentrate on searching for the substance producing malignant cells and causing activation of blood coagulation in neoplasm disease patients. Gordon and co-workers were the first who published results of their investigation in searching for such a substance in 1975. It was isolated from the rabbit's neoplasm type V2 Ca and then characterized and named as cancer procoagulant (CP). Cancer procoagulant is responsible for blood coagulation disorders in neoplasm disease patients, incorrect metabolism of fibrin and its concentration around malignant tissues. This enzyme (in vitro) is a direct activator of the factor X, without contribution of factor VII or any other cofactors. CF differs in physical, chemical and enzymatic activity from others procoagulants. The main aim of the paper is a review of the literature for structure, chemical characteristic, occurrence and clinical relevance of the cancer procoagulant (CP) and its clinical use in current oncological diagnostics.


Assuntos
Biomarcadores Tumorais/metabolismo , Cisteína Endopeptidases/metabolismo , Proteínas de Neoplasias/metabolismo , Neoplasias/enzimologia , Animais , Humanos
18.
Pol Merkur Lekarski ; 18(108): 651-3, 2005 Jun.
Artigo em Polonês | MEDLINE | ID: mdl-16124376

RESUMO

The increasing morbidity and mortality rates of bladder cancer forced the scientists to search for new unfailing diagnostic and therapeutic methods that will improve treatment effects. There are biochemical cancer markers as cancer procoagulant (CP) and cathepsin D which may be used to this end. The aim of the study was to evaluate the activity of the cancer procoagulant and cathepsin D in the blood serum in patients with superficial bladder cancer. The venous blood samples were from 15 patients with microscopically proved superficial bladder carcinoma (i.e. study group) and 15 normal volunteers as a control group. The serum blood CP activity was determined by the Gordon-Benson's coagulation method and expressed by the clotting time in seconds (s) while the cathepsin D activity was determined by the Folin-Ciocalteau's method and expressed by a quantity of released tyrosine in nmol/ml per 4 hours. The CP activity in serum of patients with superficial bladder cancer was increased in statistically way as compared to the non-cancer controls (p<0.0001). The cathepsin D activity in blood serum of the study group was also enhanced as compared to the control group and the said values differed statistically (p<0.0351). It appears to be justifiable to apply the determination of the CP and cathepsin D activity in blood serum for the diagnostics of superficial bladder cancer.


Assuntos
Biomarcadores Tumorais/sangue , Carcinoma/sangue , Catepsina D/sangue , Cisteína Endopeptidases/sangue , Proteínas de Neoplasias/sangue , Neoplasias da Bexiga Urinária/sangue , Idoso , Estudos de Casos e Controles , Feminino , Humanos , Masculino , Pessoa de Meia-Idade
19.
Arch Immunol Ther Exp (Warsz) ; 52(4): 277-83, 2004.
Artigo em Inglês | MEDLINE | ID: mdl-15467492

RESUMO

INTRODUCTION: The aim of the study was to evaluate the prevalence of anti-Chlamydia trachomatis (C.trachomatis) antibodies in serum and expressed prostatic secretion (EPS) in chronic prostatitis. MATERIALS AND METHODS: Thirty-six patients with chronic prostatitis were examined. The presence of C. trachomatis was determined in urethral smears and EPS. Specific antibodies were determined in the serum (IgM, IgA, IgG) and in the EPS (IgA, IgG). In the direct diagnosis of chlamydial infection, the direct immunofluorescence method and the ligase chain reaction were employed, and for the serological diagnosis, the immunoenzymatic method. RESULTS: C. trachomatis infection was detected in the urethra of 3 (8.3%) patients and in the prostatic gland of 3 (8.3%) patients; only one of these patients was found to have C. trachomatis in both the urethra and the EPS. In the control group, C. trachomatis was detected in the urethra of 1/50 (2%) of the men, but the EPS of all of them was free of C. trachomatis. Specific IgM antibodies were found in 7 (19.4%), IgA in 9 (25%), and IgG in 18 (50%) of the patients' serum, whereas IgAs were detected in 12 (33.3%) and IgGs in 13 (36.1%) of the patients' EPS. In the control group, anti-C. trachomatis antibodies of the IgG were detected in the serum of 2/35 (5.7%) of the men, whereas in the EPS neither IgA nor IgG antibodies were detected in any of these patients. CONCLUSIONS: Serological tests of the serum and EPS are useful as a complementary method in the diagnosis of chronic prostatitis.


Assuntos
Anticorpos Antibacterianos/sangue , Infecções por Chlamydia/imunologia , Chlamydia trachomatis/imunologia , Prostatite/microbiologia , Adolescente , Adulto , Infecções por Chlamydia/diagnóstico , Humanos , Masculino , Pessoa de Meia-Idade , Prostatite/diagnóstico , Testes Sorológicos , Uretra/citologia , Uretra/microbiologia
20.
Eur Urol ; 45(1): 77-81; discussion 81, 2004 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-14667520

RESUMO

OBJECTIVE: A new surgical method of treating Peyronie's disease consisting in intracavernosal excision of the plaque is presented. MATERIAL AND METHODS: The operation was performed on 16 men aged from 34 to 65 years (mean 50.2 years). The angle of penile curvature was 30 degrees to 60 degrees. Thirteen (81.25%) had impaired intercourse because of penile deformity and in 3 (18.75%) patients it was prevented by marked penile curvature. The mean quality of life score (QoL) was evaluated as 4.8. The operation consists in incising the corpus cavernosum parallel to the plaque and through this incision removing the plaque from the inside without incising or replacing the underlaying tunica albuginea. RESULTS: Follow-up examinations made after 3, 6 and 12 months revealed normal, painless erection in all the patients. In 2 (12.5%) intercourse was impaired only by persistent penile curvature of over 20 degrees. Mean QoL score -1.1. CONCLUSIONS: In our opinion intracavernosal plaque excision is a simple method, easier to perform and less invasive than the operative methods applied to date. It eliminates the pain, does not result in a shortening of the penis, loss of sensation or erectile dysfunction. It ensures a considerable improvement in the QoL of the patients treated.


Assuntos
Induração Peniana/cirurgia , Pênis/cirurgia , Procedimentos Cirúrgicos Urológicos Masculinos/métodos , Adulto , Idoso , Humanos , Masculino , Pessoa de Meia-Idade
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