scholarly journals The Diagnostic Value of Nuclear Matrix Proteins in Bladder Cancer in the Aspect of Environmental Risk from Carcinogens

2017 ◽  
Vol 2017 ◽  
pp. 1-11 ◽  
Author(s):  
Beata Szymańska ◽  
Ewa Sawicka ◽  
Anna Guzik ◽  
Romuald Zdrojowy ◽  
Anna Długosz
Keyword(s):  
Bladder Cancer ◽  
Environmental Risk ◽  
Nuclear Matrix ◽  
Matrix Protein ◽  
Causative Factor ◽  
Tumor Stage ◽  
Diagnostic Value ◽  
Matrix Proteins ◽  
Slow Acetylators ◽  
Nuclear Matrix Proteins

Background. The interaction of environmental factors with genetic susceptibility and detoxification level seems to be an important causative factor in bladder cancer (BC). The aim of this study was to look for a BC marker panel which reflects the environmental risk. The nuclear matrix protein 22 (NMP22), bladder cancer-4 (BLCA-4), and total level proteins NMP22 and BLCA-4 (NMBL) in BC patients with genetic predisposition NAT2 (classified as slow acetylators, SA), DNA damage (8-OHdG), and detoxification by isoenzyme GSTπ activity were measured. Materials and Methods. The urine and blood from 91 BC patients and controls were examined, also according to tumor stage (T) and grade (G). The participants completed a questionnaire in order to evaluate environmental risk. Results. Most patients (75.3%) were previous or actual smokers. The levels of 8-OHdG, NMP22, BLCA-4, NMBL, and GSTπ were significantly higher in BC (p≤0.001). The majority of patients (59.3%) were slow acetylators (SA). The highest BLCA-4/8-OHdG correlation was observed in total BC and SA smokers. Conclusions. The total pool of nuclear matrix proteins in the urine (NMBL) has a higher diagnostic value in bladder cancer than single proteins. The particular value of BLCA-4 and GSTπ in the aspect of environmental risk was noted.

scholarly journals Ultrastructural localization of nuclear matrix proteins in HeLa cells using silver-enhanced ultra-small gold probes.

1991 ◽  
Vol 39 (8) ◽  
pp. 1035-1045 ◽  
Author(s):  
A de Graaf ◽  
P M van Bergen en Henegouwen ◽  
A M Meijne ◽  
R van Driel ◽  
A J Verkleij
Keyword(s):  
Hela Cells ◽  
Nuclear Matrix ◽  
Matrix Protein ◽  
Ultrastructural Localization ◽  
Matrix Proteins ◽  
Cell Permeabilization ◽  
Immunogold Staining ◽  
Thin Sections ◽  
Nuclear Matrix Proteins ◽  
Dna And Rna

We describe a method for immunogold staining of nuclear matrix proteins using ultra-small gold particles. The nuclear matrix of HeLa cells is obtained by two fractionation steps: (a) cell permeabilization with Triton X-100 to isolate the cytoskeleton, and (b) nuclease digestion followed by an incubation in 0.25 M ammonium sulfate to isolate the nuclear matrix. To prevent redistribution of internal matrix proteins during nuclear matrix preparation, pre-fixation with 0.1% acrolein was performed. Under this condition up to 80% of protein and 90% of DNA and RNA could be removed on nuclear matrix isolation, without redistribution of internal nuclear matrix proteins. For immunogold labeling, 1-nm gold probes appeared to be required to obtain optimal penetration into the nucleus. These particles can be visualized after silver enhancement. After gold labeling the matrices are stained, embedded in Epon, and ultra-thin sections are prepared for examination in the electron microscope. The applicability of this method is examplified by the localization of a 125 KD internal nuclear matrix protein and the lamins A and C in nuclear matrix preparations of HeLa cells.

scholarly journals Developmental association of the beta-galactoside-binding protein galectin-1 with the nuclear matrix of rat calvarial osteoblasts

1998 ◽  
Vol 111 (20) ◽  
pp. 3035-3043 ◽  
Author(s):  
J.Y. Choi ◽  
A.J. van Wijnen ◽  
F. Aslam ◽  
J.D. Leszyk ◽  
J.L. Stein ◽  
...  
Keyword(s):  
Nuclear Matrix ◽  
Osteoblast Differentiation ◽  
Matrix Protein ◽  
Binding Protein ◽  
Protein Composition ◽  
Matrix Proteins ◽  
Specific Gene ◽  
Two Dimensional Gel Electrophoresis ◽  
Nuclear Matrix Proteins ◽  
Differential Retention

The protein composition of the nuclear matrix changes significantly as the osteoblast matures from a proliferating pre-osteoblast to an osteocyte embedded in a mineralized matrix. These matrix protein are the result of developmental stage-specific gene expression during osteoblast differentiation. To isolate nuclear matrix proteins unique to the bone phenotype we analyzed nuclear matrix preparations from cultures of rat calvarial osteoblasts by high resolution two-dimensional gel electrophoresis at two different stages: proliferation (day 3) and differentiation (day 18, mineralized). We characterized one protein (14 kDa; pI 5.0), that was detectable only in the nuclear matrix of differentiated osteoblasts. By mass spectrometry and microsequencing, this protein was identified as the beta -galactoside-binding protein galectin-1. Both immunofluorescence staining of nuclear matrix preparations with the galectin-1 antibody and western blot analysis of subcellular fractions confirmed that galectin-1 is only associated with the nuclear matrix in differentiated osteoblasts as the result of differential retention. Galectin-1 protein and mRNA are present throughout osteoblast differentiation. Galectin-1 is present in the cytoplasmic and nuclear fractions in both proliferating and differentiated osteoblasts. However, its only stable binding is to the nuclear matrix of the differentiated osteoblast; but, in proliferating osteoblasts, galectin-1 is not retained in the nuclear matrix. Taken together, our results suggest that developmental association of galectin-1 with the nuclear matrix reflects differential subnuclear binding of galectin-1 during osteoblast differentiation.

scholarly journals MspI8, the repetitive sequence specifically interacting with nuclear matrix of rat testis cells.

1994 ◽  
Vol 41 (4) ◽  
pp. 459-466 ◽  
Author(s):  
J Rzeszowska-Wolny ◽  
J Rogoliński
Keyword(s):  
Nuclear Matrix ◽  
Gel Electrophoresis ◽  
Matrix Protein ◽  
Repetitive Sequences ◽  
Matrix Proteins ◽  
Nuclear Matrix Proteins ◽  
Rat Testis ◽  
The Matrix ◽  
Matrix Bound

The nuclear matrix bound DNA fraction of rat testis showed enrichment in repetitive sequences found in the 450 bp band after gel electrophoresis of the MspI digested rat DNA. DNA fragments isolated from this band were cloned. DNA of the clone pMspI8 showed homology to some representatives of rat LINE sequence family, and complexed in vitro more efficiently with testes nuclear matrix proteins than with yeast ARS1 sequence containing the matrix association region (MAR) or DNA from an other clone, MspI19. Western blot analysis showed that MspI8 sequence interacts with testes matrix protein of about 120 kDa.

scholarly journals The role of the BLCA-4 nuclear matrix protein in bladder cancer

2017 ◽  
Vol 71 (1) ◽  
pp. 0-0
Author(s):  
Beata Szymańska ◽  
Anna Długosz
Keyword(s):  
Bladder Cancer ◽  
Nuclear Matrix ◽  
Oxidative Dna Damage ◽  
Matrix Protein ◽  
High Specificity ◽  
Diagnostic Value ◽  
Nuclear Matrix Protein ◽  
Noninvasive Methods ◽  
Urine Sediment ◽  
Genotoxic Compounds

Bladder cancer (BC) affects usually older people. According to information provided by the National Cancer Registry in 2012. BC was the 4th, in terms of illness, cancer in men and 11th in women. Early diagnosis of bladder cancer is important because detected later has worse prognosis.Diagnosis of bladder cancer is not simple and it is still very invasive. Usually the cystoscopy or endoscopic bladder biopsy with histopathological evaluation and cytology of urine sediment is used. This prompted researchers to look for alternative noninvasive methods of diagnosis of bladder cancer. Recently, it was described the group of six proteins (BLCA) specific for BC, with special attention to BLCA-4.BLCA-4 belongs to the nuclear matrix protein and has a high specificity for this type of cancer however the value of this marker in BC diagnosis is not yet established. Oxidative DNA damage play an important role in the pathogenesis of some human diseases, including cancer. Determination of 8-hydroxy-2’deoksyguanozyne (8-OHdG) is currently used in the evaluation of genotoxic damage.The aim of the work was to review information on BLCA-4, its function in the process of BC carcinogenesis and diagnostic value also in exposure to genotoxic compounds measured by 8-hydroxy-2’deoksyguanozyne (8-OHdG) level.

984: Variability in the Performance of Nuclear Matrix Protein 22 in the Detection of Bladder Cancer

2006 ◽  
Vol 175 (4S) ◽  
pp. 317-317
Author(s):  
Shahrokh F. Shariat ◽  
Michael Marberger ◽  
Yair Lotan ◽  
Marta Sanchez-Carbayo ◽  
Craig D. Zippe ◽  
...  
Keyword(s):  
Bladder Cancer ◽  
Nuclear Matrix ◽  
Matrix Protein ◽  
Nuclear Matrix Protein

Differentiation-Specific Nuclear Matrix Proteins Cross-linked to DNA bycis-Diammine Dichloroplatinum

1998 ◽  
Vol 238 (1) ◽  
pp. 216-219 ◽  
Author(s):  
Elena Mattia ◽  
Margherita Eufemi ◽  
Silvia Chichiarelli ◽  
Mara Ceridono ◽  
Anna Ferraro
Keyword(s):  
Nuclear Matrix ◽  
Matrix Proteins ◽  
Nuclear Matrix Proteins

Diagnostic accuracy of NMP-52, NMP-22 and urine cytology in the diagnosis of bladder cancer

2021 ◽  
Vol 16 (10) ◽  
pp. 59-62
Author(s):  
Mohamed J. Saadh
Keyword(s):  
Bladder Cancer ◽  
Nuclear Matrix ◽  
Diagnostic Performance ◽  
Matrix Protein ◽  
Urinary Cytology ◽  
Significant Relation ◽  
Nuclear Matrix Protein ◽  
Diagnostic Efficacy ◽  
Noninvasive Biomarkers ◽  
New Biomarkers

Bladder cancer (BC) is the most important tumor problem of urologic cancer. Therefore, noninvasive urinary biomarkers were used for diagnosis of BC. However, the new biomarkers failed to reach higher accuracy. The aim of this study was to assess the diagnostic efficacy of nuclear matrix protein-22 (NMP- 22), nuclear matrix protein-52 (NMP-52), urinary cytology and to investigate combinations of urine NMP-52 with urinary cytology as noninvasive biomarkers to increase diagnostic performance of bladder cancer at different grades and stages. Overall, there were 156 subjects (62 BC, 54 cystitis patients and 40 healthy volunteers). The NMP-22 and NMP-52 were quantified in urine samples by ELISA. The urinary cytology is used by some physicians routinely for diagnosis of BC. The sensitivity and specificity for NMP-52 were 94% and 82%, for NMP-22 69% and 80.8% and for cytology 56% and 94.6% respectively and also, both urinary NMP-22 and NMP-52 have extremely significant relation (p<0.0001) to BC vs. healthy individuals and cystitis patients. Moreover, the combination of NMP- 52 with urinary cytology could predict all BC stages and grade with 95.6% sensitivity and 94.3% specificity. In conclusion, NMP-52 and urinary cytology in combination improve diagnostic performance for BC detection in different pathological types.

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