No abstract available.
Cytodiagnosis* ; Immunohistochemistry* ; Nuclear Proteins* ; Nuts* ; Testis*

High expression of Fightless I (FLII) is associated to multiple tumors. Based on our previous study that FLII might be involved in the nuclear export, we assessed the possible interaction of FLII with the nuclear envelop associating proteins Importin β and Nup88. We first constructed GST-FLII, GST-LRR recombinant plasmids and transformed them into the Rosetta strain to produce GST-FLII, GST-LRR fusion protein. After purification of these proteins, GST-pull down, as well as co-immunoprecipitation, were used to test the interaction of FLII with Importin β and Nup88. FLII interacted with Importin β and Nup88, and FLII LRR domain is responsible for these interactions. Thus, FLII may play a role in nuclear export through interaction with Importin β and Nup88.
Humans ; Microfilament Proteins ; metabolism ; Nuclear Pore Complex Proteins ; metabolism ; Receptors, Cytoplasmic and Nuclear ; metabolism ; Recombinant Fusion Proteins ; metabolism ; beta Karyopherins ; metabolism

Proliferating cell nuclear ntigen (FCNA) iis a nuclear protein that is syntheaimd in late Gl and S phases of cell cycle and is correlated with the cell proliferative stale. The recent study demonstrated that FCNA functions in 13NA replication. The present study evaluated proliferetive iindices (PI) for the assessment of tumor proliferation and for investigating prognostic significancx, in cervical tumors. lmmunohiatoehemical PCNA staining was perfurmed in formalin-fixed paraffin-embedded cervical tissues via the avidin-biotin-complex immunoperoxidase methad. Mean PI was 36.03+/-5.14% in normaI controls, as compared to 66.19+/-11.36% in cerviml intraepithelial neoplasia. and 63.19+/-10.94% in invasive cervical cancer. Our results showed no significant correlation between Pll and histological type. Among invasive cervical cancer (24 cases), PI waa 64.43+/-10.94% in squamoua cell carcinoma and 59.00+/-4.10% in adenocarcinoma. There was no eipiifiant relationship between Fl and clinical etage, and between PI and lesion size. This study auggeste that Pl may not serve as a new prognostie factor in cervical tumors.
Adenocarcinoma ; Cell Cycle ; Nuclear Proteins ; Proliferating Cell Nuclear Antigen* ; S Phase ; Uterine Cervical Neoplasms

PURPOSE: Assessment of the proliferative ability of cancer cells is necessary not only for the biologic characterization of tumors, but also for the selection of treatment and evaluation of prognosis. Recently, there have been several studies examining the proliferative activity of various malignant tumors using immunohistochemical methods. PCNA is a nuclear protein related to the cell cycle and found with high expression in proliferative tissues, including cancers. METHODS: In our study, to evaluate whether PCNA expression was useful as a prognostic factor in patients with papillary thyroid carcinoma, we quantitated the immunohistochemical expression of PCNA in the formalin-fixed paraffin embedded tissue from 55 patients with papillary thyroid carcinoma and correlated the results with established clinicopathologic parameters. RESULTS: The results were as follows. 1) PCNA expression in papillary thyroid carcinoma did not correlate with the age, sex or metastatic L/N activity of the patient, nor with the size, invasion, or recurrence of the tumor. 2) There was a close relationship between the expression rate of PCNA in thyroid tumor cells and that in metastatic L/N cells (p=0.056, in p<0.1). 3) The expression of PCNA in the metastatic L/N (+) group was higher than in the metastatic L/N (+) group (p=0.045). CONCLUSION: It is suggested that PCNA expression is not an appropriate prognostic factor in papillary thyroid carcinoma.
Cell Cycle ; Humans ; Nuclear Proteins ; Paraffin ; Prognosis ; Proliferating Cell Nuclear Antigen* ; Recurrence ; Thyroid Gland* ; Thyroid Neoplasms*

Nuclear protein-1 (NUPR1) is a small nuclear protein that is responsive to various stress stimuli. Although NUPR1 has been associated with cancer development, its expression and roles in cholangiocarcinoma have not yet been described. In the present study, we found that NUPR1 was over-expressed in human cholangiocarcinoma tissues, using immunohistochemistry. The role of NUPR1 in cholangiocarcinoma was examined by its specific siRNA. NUPR1 siRNA decreased proliferation, migration and invasion of human cholangiocarcinoma cell lines (HuCCT1 and SNU1196 cells). From these results, we conclude that NUPR1 is over-expressed in cholangiocarcinoma and regulates the proliferation and motility of cancer cells.
Cell Line ; Cholangiocarcinoma ; Humans ; Immunohistochemistry ; Nuclear Proteins ; RNA, Small Interfering

PURPOSE: The early carcinogenic effect of N-nitrosomorpholine (NNM) on acquisition of increased survival and growth was investigated using ex vivo culture of 5th to 10th week rat liver hepatocytes after NNM treatment. MATERIALS AND METHODS: Rats were fed with NNM (200 mg/l). Hepatocytes were isolated by two step perfusion techniques and grown on tissue culture. These ex vivo hepatocytes were then subjected to analysis of growth related signal molecules resided in nucleoli. RESULTS: One of the most characteristic differences of the NNM-treated liver from normal liver was genesis of megahepatocytes. These megahepatocytes survived approximately 2~3 times as long as normal hepatocytes in ex vivo conditions. There was also a significant increase in various nucleolar proteins, including Erk1/2, p38, hsp72 and nucleophosmin (B23). CONCLUSION: At promotion stage of tumorigenesis induced by NNM, it was possible to isolate and characterize abnormal hepatocytes. These abnormal hepatocytes showed increased survival in in vitro (ex vivo) than normal hepatocytes, although they were not immortal.
Animals ; Carcinogenesis ; Hepatocytes* ; Liver ; Nuclear Proteins ; Perfusion ; Rats*

Highly expressed in cancer (Hec 1), locating at centromere during cell mitosis, plays an important role in the pathway of spindle checkpoint. Hec 1-Nuf 2 complex is the structural basis for the recruitment of Mad 1/Mad 2 complex of spindle checkpoint. Hec 1 can interact with the subunit of 26S proteasome and inhibit the degradation of cyclins. It was initially identified as a protein interacting with Rb by yeast two-hybridization assay. Rb interacts with Hec 1 to regulate the binding ability of Smc 1 with DNA and participates in the regulation of M phase. Hec 1 mainly expresses at G2/M phase and functions through the phosphorylation by kinase Nek 2. Hec 1 is over expressed in some cancer cell lines and amplified in tumor tissues. The dysfunction of Hec 1 gene may cause severe impediment of chromosome separation and finally lead to chromosome instability, which is closely associated with the occurrence and development of tumors. Therefore, Hec 1 may become a new target of tumor gene therapy.
Chromosomal Instability ; Humans ; Neoplasms ; genetics ; Nuclear Proteins ; genetics

OBJECTIVETo investigate NPM1 gene mutations in patients with primary myelodysplastic syndromes (MDS) and the clinical characteristics of patients with NPM1 mutants.

METHODSGenomic DNA corresponding to exon 12 of NPM1 gene was amplified by polymerase chain reaction (PCR) in 232 patients with primary MDS. Identification of mutants was by direct sequencing and classification of mutation types by sequencing followed by plasmid cloning.

RESULTSNPM1 mutants were found in 9 patients (3.9%). All the mutants were type A. As compared with those with NPM1 wild type, patients with the mutant were of lower ANC \[0.60 (0.12 - 2.91) × 10(9)/L vs 1.02 (0 - 10.23) × 10(9)/L, P = 0.046\], higher blast percent in bone marrow \[0.050 (0 - 0.090) vs 0.025 (0 - 0.190), P = 0.035\], decreased BFU-E \[0 (0 - 0)/10(5) BMMNC vs 6 (0 - 40)/10(5) BMMNC, P = 0.038\] and increased serum vitamin B(12) \[936.40 (373.80 - 2400.00) pmol/L vs 557.85 (17.00 - 3032.10) pmol/L, P = 0.045\] The chromosomal karyotypes of patients with NPM1 mutant were predominantly normal.

CONCLUSIONMDS patients with NPM1 gene mutations have some unique clinical and laboratory features. The results give new hint for the pathogenesis of MDS development and progression.

Nucleolar phosphoprotein (nucleophosmin 1, NPM1), also known as B23, N038, is located in the nucleolar particles of a multifunctional protein widely expressed in various types of cells. At present, a number of studies found that the NPM1 gene mutation is the most frequent acquired molecular genetic abnormalities in acute myeloid leukemia (AML), especially in normal karyotype AML (nk-AML). NPM1 mutation is a special subgroup in AML, which has relatively unique clinical features, and is the independent prognostic indicators of AML. Research on NPM1 mutation has an important clinical significance in the diagnosis, treatment and prognosis judgment of AML patients. This article reviews the discovery of NPM1 gene mutation in AML in recent years, including structure and physiological functions of NPM1 gene, NPM1 gene mutation in AML, detection methods of NPM1 gene mutation, and so on.
Humans ; Leukemia, Myeloid, Acute ; genetics ; Mutation ; Nuclear Proteins ; genetics

No abstract available.
Multiple Myeloma* ; Oncogene Proteins* ; Oncogenes* ; Proliferating Cell Nuclear Antigen*