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PubMed2006

Prognostic value of cytology, nuclear matrix protein 22 (NMP22) test, and urinary bladder cancer II (UBC II) test in early recurrent transitional cell carcinoma of the bladder.

This study addresses the diagnostic value of the Nuclear Matrix Protein 22 (NMP22) test and the Urinary Bladder Cancer (UBC II) test, in comparison to bladder wash cytology for the detection of early recurrence of bladder cancer. Patients with transitional cell carcinoma of the bladder (TCC, n = 60) and patients with benign urological diseases (n = 30) were included in this study. Voided urine samples were divided into 2 aliquots: aliquot 1 was assayed for NMP22 and aliquot 2 was tested for UBC II. Saline bladder washings were used for cytologic examination. Urine samples from TCC patients were collected before transurethral resection and on postoperative day 10. On day 10, 15 NMP22 results and 7 UBC II results exceeded the normal ranges; 4 of the cytology samples were positive for malignancy. Based on cystoscopic findings at 3 mo post-resection, 21 of the cases were classified as early recurrence; 11 of the early recurrences had been in the elevated NMP22 group, 4 in the elevated UBC II group, and 3 in the positive cytology group at 10 days post-resection. The NMP22 test gave the highest sensitivity for detecting early recurrent tumors (11 of 21, 52%). Such high sensitivity did not occur with the UBC II test (4 of 21, 19%) or cytology (3 of 21, 14%). These differences were significant (p = 0.024 and 0.009, respectively). Thus, the NMP22 test showed superiority over the other tests for detection of early recurrence of bladder cancer.

Adult↗
PubMed1989

A novel phospholipase A2 associated with nuclear matrix: stimulation of the activity and modulation of the Ca2+ dependency by polyphosphoinositides.

Neutral phospholipase A2 activity, which hydrolyzed phosphatidylcholine and phosphatidylethanolamine with the same efficiency, was identified in the nuclear matrix prepared from purified nuclei of rat ascites hepatoma cells (AH 7974). The enzyme activity was optimal at pH 7.0 and required Ca2+ absolutely. Concentrations of Ca2+ for a maximal and a half-maximal activation were 1.10(-2) and 1.10(-3) M, respectively, and little activity was detected at Ca2+ concentrations lower than 1.10(-5) M. Addition of acidic phospholipids markedly stimulated the enzyme activity, and further, lowered the minimum Ca2+ concentration required for activation. In particular, the polyphosphoionositides phosphatidylinositol 4-monophosphate and 4,5-diphosphate were most effective. These two polyphosphoinositides lowered the Ca2+ concentration required for half-maximal activation to 10(-5) M and dramatically stimulated the activity at that Ca2+ concentration (greater than 30-fold). The neutral phospholipase A2 activity such as characterized in the present study was very low in the other subcellular fractions including mitochondria, microsome, plasma membrane and cytosol.

Animals↗
PubMed1988

Identification of numatrin, the nuclear matrix protein associated with induction of mitogenesis, as the nucleolar protein B23. Implication for the role of the nucleolus in early transduction of mitogenic signals.

We have previously described and characterized a nuclear protein at 40 kDa/pI 5 termed "numatrin" which is tightly bound to the nuclear matrix. We demonstrated that a rapid increase in the synthesis of numatrin at early G1 phase is closely correlated with receptor-mediated induction of cellular proliferation by various mitogens and that elevated amounts of numatrin are found in tumor cells, suggesting that numatrin may have an important role in regulation of cellular growth in normal and malignant cells. Further experiments were undertaken to compare the biochemical characteristics of numatrin to those of other known proteins that are associated with cellular mitogenesis. Comparison of the electrophoretic mobility of numatrin with the proliferation cell nuclear antigen/cyclin showed that these proteins are not identical. However, numatrin had an identical electrophoretic migration on two-dimensional gel electrophoresis to that of a previously described nucleolar protein B23. The tryptic digest peptide map of 125I-labeled B23 was identical to that of numatrin on two-dimensional thin layer electrophoresis/chromatography. Labeling of cells with 32P further showed that numatrin is a major phosphoprotein as previously reported for protein B23. Using the protocol for purification of B23, we purified numatrin from nucleoli of HL-60 cells and produced two polyclonal antibodies (303 and 339) to this protein. We further show that numatrin is recognized by anti-B23 monoclonal antibody as well as by polyclonal antibodies 303 and 339 in enzyme-linked immunosorbent assay. Conversely, these anti-numatrin polyclonal antibodies cross-react with protein B23 as shown in immunoblot analysis. These results, taken collectively, prove that numatrin is identical to the nucleolar protein B23 and thus suggest that protein B23 and events which occur at the nucleolus might have an important role in early transduction of mitogenic signals at the G1 phase of the cell cycle.

Antibodies↗
PubMed1988

Location and methylation pattern of a nuclear matrix associated region in the human pro alpha 2(I) collagen gene.

Using both a 25 mM Lithium di-iodosalicylic acid (LIS) and a 2M NaCl extraction procedure to extract nuclear matrices from white cells we have identified a 0.9 kb nuclear matrix associated region (MAR) in the human pro alpha 2(I) collagen gene. The MAR is located towards the 3' coding end of the gene, it is completely associated with the matrix in transcriptionally inactive white cells but is incompletely associated with the matrix in transcriptionally active fibroblasts. Furthermore the methylation state of the fibroblast gene in the region coinciding with the MAR showed unique differences when compared to adjacent sites in the fibroblast gene and corresponding sites of the white cell gene.

Cell Nucleus↗
PubMed1996

The nuclear matrix protein p255 is a highly phosphorylated form of RNA polymerase II largest subunit which associates with spliceosomes.

The monoclonal antibody CC-3 recognizes a phosphodependent epitope on a 255 kDa nuclear matrix protein (p255) recently shown to associate with splicing complexes as part of the [U4/U6.U5] tri-snRNP particle [Chabot et al. (1995) Nucleic Acids Res. 23, 3206-3213]. In mouse and Drosophila cultured cells the electrophoretic mobility of p255, faster in the latter species, was identical to that of the hyperphosphorylated form of RNA polymerase II largest subunit (IIo). The CC-3 immunoreactivity of p255 was abolished by 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole, which is known to cause the dephosphorylation of the C-terminal domain of subunit IIo by inhibiting the TFIIH-associated kinase. The identity of p255 was confirmed by showing that CC-3-immunoprecipitated p255 was recognized by POL3/3 and 8WG16, two antibodies specific to RNA polymerase II largest subunit. Lastly, the recovery of RNA polymerase II largest subunit from HeLa splicing mixtures was compromised by EDTA, which prevents the interaction of p255 with splicing complexes and inhibits splicing. Our results indicate that p255 represents a highly phosphorylated form of RNA polymerase II largest subunit physically associated with spliceosomes and possibly involved in coupling transcription to RNA processing.

3T3 Cells↗
PubMed1999

Urinary nuclear matrix protein 22 as a new marker for the screening of urothelial cancer in patients with microscopic hematuria.

PURPOSE: The aim of the present study was to determine the clinical usefulness of nuclear matrix protein 22 (NMP22) as a new urinary marker for the screening of urothelial cancer in patients with microscopic hematuria, especially in comparison with that of voided urine cytology. METHODS: Patients with microscopic hematuria detected at a health examination, who were advised by a consulted urologist to have a cystoscopical examination, were asked to enter this study. Urine samples were collected before cystoscopy and divided into two portions for NMP22 test and voided urine cytology. RESULTS: Of the 309 patients with microscopic hematuria, 22 cases (7.1%) of urothelial cancer and one case of prostate cancer were detected. For the other cases, 128 (41.4%) were of benign diseases and 158 (51.1%) were designated as having no evidence of disease (NED). The median NMP22 values for urothelial cancer, other diseases and NED were 35.5, 6.7 and 6.0 U/mL, respectively, with 95% confidence intervals of 19.9-228.2, 5.1-9.3 and 5.4-7.2, respectively. The sensitivity of the NMP22 test for urothelial cancer was 90.9% (20/22), whereas the sensitivity of voided urine cytology was only 54.5% (12/22). CONCLUSIONS: The present study indicates that urinary NMP22 is a useful tool for the screening of urothelial cancer in patients with microscopic hematuria.

Adult↗
PubMed1985

Nuclear development in locust fat body: the influence of juvenile hormone on inclusion bodies and the nuclear matrix.

The hormonal induction of vitellogenesis in insects and in oviparous vertebrates are prime models of gene regulation in eukaryotes. In vertebrates the process is under estrogenic control and normally confined to females, although males can be artificially induced. In locust in contrast, juvenile hormone (JH) is central to fat body development in both males and females, yet the response is strongly sex limited not only for vitellogenin production but also in terms of total protein, DNA and RNA synthesis and nuclear ploidy levels. To differentiate further possible sex and/or JH related developmental aspects in locusts, large-scale nuclear events were examined during normal adult maturation and in animals treated with antiallatropins and JH analogs. Fat body nuclei undergo extensive restructuring during normal development in both sexes. This included progressive nuclear enlargement, accompanied by extensive proliferation of nuclear matrix components and elaboration of complex inclusion bodies (NB). The isolated protein matrix was unusually complex relative to similar structures from vertebrates and the NB were firmly anchored to it. Although matrix proteins were qualitatively similar to those from other sources, as assessed by SDS polyacrylamide gel electrophoresis, several major matrix polypeptides, including lamins A and B, and components greater than 150 kD, fluctuated quantitatively during development and in concert with nuclear enlargement. The number and morphology of the NB were unrelated to sex, but increased in direct proportion to absolute nuclear volumes. All changes were more pronounced in females, where higher ploidy levels, larger nuclei and correspondingly more internal matrix elements occurred. Suppression of JH production by precocene prevented all foregoing nuclear changes, but re-exposure to methoprene rapidly induced normal development. The results are compared to analogous nuclear changes in steroid responsive vertebrate tissues.

Adipose Tissue↗
PubMed1997

[Evaluation of urinary NMP22 (nuclear matrix protein 22) as a diagnostic marker for urothelial cancer--screening for urothelial cancer in patients with microscopic hematuria. NMP Study Group].

This study was undertaken to determine the clinical usefulness of NMP22 (Nuclear Matrix Protein 22) as a urinary marker for the screening of urothelial cancer in patients with microscopic hematuria, especially in comparison with that of voided urine cytology. Urinary NMP22 values were determined for 183 patients with microscopic hematuria by use of a UNMP22 Test kit, which is based on an enzyme-linked immunosorbent assay. All patients were entered in this study before cystoscopy was performed, and were evaluated for NMP22 values and voided urine cytology simultaneously from the same urine samples. Of the 183 patients with microscopic hematuria, 14 cases of urothelial cancer were detected. For the other cases, 65 were of benign diseases and 104 were designated NED (No Evidence of Disease). The median NMP22 values for urothelial cancer, benign diseases, and NED were 26.5 U/ml (95% CI: 18.5-228.2; 4.9 U/ml (95% CI: 3.6-8.3), and 5.9 U/ml (95% CI: 4.8-6.5), respectively. The urinary NMP22 value for urothelial cancer was significantly higher than for benign diseases and NED. When the cut-off value of urinary NMP22 was set at 12 U/ml, the positive rate of NMP22 for urothelial cancer was 85.7%, significantly higher than the 50% positive rate by voided urine cytology. This study indicates that urinary NMP22 is a useful tool for the screening of urothelial cancer in patients with microscopic hematuria.

Adult↗
PubMed1997

[Evaluation of urinary NMP22 (nuclear matrix protein 22) as a diagnostic marker for urothelial cancer--NMP22 as a urinary marker for surveillance of bladder cancer. NMP22 Study Group].

This study was undertaken to determine the clinical usefulness of NMP22 (Nuclear Matrix Protein 22) as a urinary marker for the surveillance of bladder cancer, especially in comparison with that of voided urine cytology. Urinary NMP22 values were determined for 144 patients with histologically diagnosed bladder cancer, 65 patients with other urological cancers, and 171 healthy volunteers by use of a UNMP22 Test kit, which is based on an enzyme-linked immunosorbent assay. All bladder cancer patients were evaluated for urinary NMP22 values and voided urine cytology simultaneously from the same urine samples. Based on the data from the bladder cancer patients and the healthy volunteers, the cut-off value was set at 12 U/ml. The median urinary NMP22 value for the bladder cancer patients was 17.8 U/ml (95% CI: 13.1-29.0). The sensitivities of urinary NMP22 and voided urine cytology were 61.1% (88/144) and 33.8% (48/144), respectively, a significant difference (p < 0.00001). Multivariate analysis revealed that tumor size affected the urinary NMP22 values. The positive rate by tumor size was 42.3%, 59.1%, and 85.0% for tumors of < 10 mm, 10-30 mm, and > 30 mm, respectively. Urinary NMP22 values decreased postoperatively in 82.9% of the patients. The median NMP22 values for prostate cancer and renal cancer were 4.4 U/ml (95% CI: 2.2-6.7) and 6.2 U/ml (95% CI: 3.6-12.5). The positive rates were 24.2% and 31.3%, respectively, both of which were significantly lower than for bladder cancer. Our multicenter study indicates that urinary NMP22 test is more sensitive than voided urine cytology test for the surveillance of bladder cancer.

Adult↗
PubMed1988

Modulation of lymphocyte nuclear matrix organization in vivo by 5,6-dichloro-1-beta-D-ribofuranosyl benzimidazole: an autoradiographic and immunofluorescence study.

Assembly of active nuclei in lymphocytes stimulated by mitogen is paralleled by the elaboration of a structurally and biochemically complex nuclear matrix (NM). To examine the dynamics of individual NM polypeptide components during blastogenesis, we have applied immunofluorescence labelling with anti-NM antibodies to concanavalin A-stimulated mouse splenocytes. Whereas peripherin and PI2 antigens did not reorganize during stimulation, labelling of PI1 and small nuclear ribonucleoprotein (snRNP) antigens increased markedly in intensity and redistributed in concert with the previously reported NM restructuring. Double-labelling showed, furthermore, that snRNPs and the internal staining component of PI1 were largely co-localized. As an approach to studying the role of RNA and RNA synthesis in NM organization, we have further examined the effects of the inhibitor of RNA synthesis, 5,6-dichloro-1-beta-D-ribofuranosyl benzimidazole (DRB), on NM antigen distribution. The rapid inhibition of 3H-uridine incorporation by DRB was accompanied by coordinate aggregation of snRNPs and of the internal PI1 component into large, brightly stained patches. Both 3H-uridine incorporation levels and antigen localization were readily reversed upon removal of DRB. We conclude that NM antigens behave independently during nuclear and NM assembly and that NM organization, as reflected by NM antigen distribution, is modulated by con A- and DRB-induced alterations in RNA synthesis. We propose, furthermore, that the PI1 antigen plays a role in RNA metabolism, and is possibly involved in RNA transport to the nuclear periphery.

Animals↗
PubMed2006

A map of nuclear matrix attachment regions within the breast cancer loss-of-heterozygosity region on human chromosome 16q22.1.

There is abundant evidence that the DNA in eukaryotic cells is organized into loop domains that represent basic structural and functional units of chromatin packaging. To explore the DNA domain organization of the breast cancer loss-of-heterozygosity region on human chromosome 16q22.1, we have identified a significant portion of the scaffold/matrix attachment regions (S/MARs) within this region. Forty independent putative S/MAR elements were assigned within the 16q22.1 locus. More than 90% of these S/MARs are AT rich, with GC contents as low as 27% in 2 cases. Thirty-nine (98%) of the S/MARs are located within genes and 36 (90%) in gene introns, of which 15 are in first introns of different genes. The clear tendency of S/MARs from this region to be located within the introns suggests their regulatory role. The S/MAR resource constructed may contribute to an understanding of how the genes in the region are regulated and of how the structural architecture and functional organization of the DNA are related.

Base Composition↗
PubMed2003

A telomere-binding protein (TRF2/MTBP) from mouse nuclear matrix with motives of an intermediate filament-type rod domain.

In previous work, we identified a telomeric DNA-binding protein (termed telomere-membrane binding protein, MTBP) in the envelope of the frog oocyte nucleus and raised antibodies against it. Here we present immunological evidence which suggests strongly that MTBP is identical with the vertebrate telomeric DNA-binding protein TRF2 (telomere-repeat factor 2). MTBP/TRF2 possesses motif which resembles rod domain characteristic of intermediate filament (IF) proteins as shown by immunological cross-reactivity with characteristic antibodies, as well as amino acid sequence homology. Anti-MTBP antibodies recognised a protein of the same M, as TRF2 in extracts of mouse nuclei and nuclear matrix as shown by ion-exchange chromatography, gel shift assays, and Western blots. This mouse MTBP analogue forms more stable complexes with the vertebrate telomeric DNA fragment (T(2)AG(3))(135) than with the corresponding fragment from Tetrahymena (T(2)G(4))(130). Proteins in each of these complexes are recognised by anti-MTBP antibody. In situ hybridization with the vertebrate telomeric DNA sequence (T(2)AG(3))(135) and immunofluorescence with anti-MTBP antibody had shown earlier that these are co-localised in the nucleus of mouse cells, and here MTBP is shown to be associated with the residual membrane of hepatocyte nuclei using Western blotting and immunofluorescence. Some immunofluorescence signal from MTBP is localized at chromosome extremities on metaphase plates from mouse cell culture, but the main signal is seen in patches scattered around the chromosomes which were identified as remnants of the nuclear envelope by double labelling with antibodies against lamin B. These observations suggest that MTBP/TRF2 is a good candidate for the attachment of telomeres to the nuclear envelope in somatic cells.

Animals↗
PubMed1999

Comparison of the nuclear matrix protein 22 with voided urine cytology and BTA stat test in the diagnosis of transitional cell carcinoma of the bladder.

OBJECTIVE: To assess sensitivity, specificity, accuracy, positive predictive value and negative predictive value of nuclear matrix protein 22 (NMP22) test, BTA stat test and cytology in the urine of patients with a spectrum of urologic conditions, including bladder cancer. METHODS: A total of 140 patients (40 with bladder cancer) provided a urine sample which was divided into appropriate aliquots for each of the tests cited above. The endoscopist, pathologist, cytologist and the person performing BTA stat test and NMP22 test were blinded as to the results of the other tests. RESULTS: Receiver-operating characteristics curve interpretation determined that 12.0 U/ml was an optimal reference value for NMP22 to detect transitional cell carcinoma of the bladder in this patient group. Comparative results demonstrate a clear superiority of NMP22 and BTA stat tests in sensitivity in bladder cancer detection (p < 0.01), while cytology and NMP22 were better than BTA stat test in specificity (p < 0.05). CONCLUSIONS: NMP22 and BTA stat test results represented significant improvement over urinary cytology for detection of transitional cell carcinoma. The sensitivities of NMP22 and BTA stat tests for detection of transitional cell carcinoma in this group of patients were as much as twice that of cytology. When the cutoff value of urinary NMP22 was set at 12.0 U/ml, NMP22 was more accurate than the other tests (p < 0.05).

Aged↗
PubMed2000

Nuclear matrix protein is released from apoptotic white cells during cold (1-6 degrees C) storage of concentrated red cell units and might induce antibody response in multiply transfused patients.

BACKGROUND: A previous study showed that white cells in blood units undergo apoptosis during storage. STUDY DESIGN AND METHODS: The present study attempts to show the release of nuclear matrix protein (NMP) in the supernatants of red cell units and to determine whether antibodies against nuclear components may be present in multiply transfused patients; the methods employed were enzyme-linked immunosorbent assay, flow cytometry, microscopy, immunoblotting, immunofluorescence, and confocal laser-scanning microscopy. RESULTS: NMP is released from white cells in the supernatant of packed red cell units upon cold storage (1-6 degrees C). The concentration of NMP correlates well with the degree of apoptosis, as analyzed by flow cytometry, nuclear dye staining, and DNA gel electrophoresis. Immunofluorescence also shows that white cells undergoing apoptosis (pre-G(1) peak, as seen by propidium iodide staining and flow cytometry) have an NMP content lower than control cells, which confirms an actual release of NMP. Moreover, immunoblotting analysis and immunofluorescent staining showed that, in 4 of 38 multiply transfused patients, autoantibodies against NMPs were present without any clinical or laboratory sign of autoimmune disease. One of the sera, recognizing a 64-kDa NMP, immunostained nuclear dots that were identified as coiled bodies because of their colocalization with p 80 coilin. CONCLUSION: NMP is released in the supernatant of red cell units. The results obtained from patients suggest that nuclear proteins released during apoptosis, once transfused, may induce an immune response in multiply transfused patients.

Antibodies↗
PubMed2002

[Significance of urinary nuclear matrix protein 22 in diagnosis of transitional cell carcinoma of urinary tract].

BACKGROUND & OBJECTIVE: There is no effective non-invasive monitoring method for transitional cell carcinoma of urinary tract(TCCU). It was recently reported that nuclear matrix protein 22(NMP22) could be used to diagnose TCCU. This study was designed to evaluate the significance of NMP22 in TCCU as a new urinary tumor marker and its influence factors. METHODS: The authors detected 87 patients with urinary system disease(including 29 cases with TCCU) with ELISA-NMP agent box. The patients with urinary infection were excluded. RESULTS: The positive value was set at more than 10 u/ml. The sensitivity and specificity of NMP22 on TCCU were 86.2% and 94.3%, respectively (benign diseases of urinary system used as control), with significant advantages over voided-urine cytology (86.2% vs 42.3%, P < 0.001). The main factors that caused false-positive results were urinary infection, the other malignant tumors of urinary system, bowel interposition, and nephrolith. CONCLUSION: Urinary NMP22 is a good tumor marker and could be used an alternation of voided-urine cytology for monitoring and diagnosis of TCCU.

Adult↗