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Article ; Online: Correction for Lu et al., "Latency-Associated Nuclear Antigen of Kaposi's Sarcoma-Associated Herpesvirus (KSHV) Upregulates Survivin Expression in KSHV-Associated B-Lymphoma Cells and Contributes to Their Proliferation".

Lu, Jie / Verma, Subhash C / Murakami, Masanao / Cai, Qiliang / Kumar, Pankaj / Xiao, Bingyi / Robertson, Erle S

2021 Volume 95, Issue 16, Page(s) e0076121

Language	English
Publishing date	2021-07-26
Publishing country	United States
Document type	Journal Article ; Published Erratum
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.00761-21
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Article ; Online: Kaposi's sarcoma-associated herpesvirus-encoded LANA can induce chromosomal instability through targeted degradation of the mitotic checkpoint kinase Bub1.

Sun, Zhiguo / Xiao, Bingyi / Jha, Hem Chandra / Lu, Jie / Banerjee, Shuvomoy / Robertson, Erle S

Journal of virology

2014 Volume 88, Issue 13, Page(s) 7367–7378

Abstract: Unlabelled: Kaposi's sarcoma-associated herpesvirus (KSHV) has a significant contributory role in the development of three major human neoplastic or lymphoproliferative diseases: Kaposi's sarcoma (KS), primary effusion lymphoma (PEL), and multicentric ... ...

Abstract	Unlabelled: Kaposi's sarcoma-associated herpesvirus (KSHV) has a significant contributory role in the development of three major human neoplastic or lymphoproliferative diseases: Kaposi's sarcoma (KS), primary effusion lymphoma (PEL), and multicentric Castleman's disease (MCD). These diseases are associated with chromosomal instability, a hallmark of human cancer. The latency-associated nuclear antigen (LANA) encoded by KSHV plays a key role in regulating a number of cellular pathways critical for oncogenesis. KSHV LANA alone can induce the development of B-cell hyperplasia and lymphoma in mice expressing LANA. LANA also induces chromosomal instability, thus promoting oncogenesis. However, the precise mechanism underlying LANA-mediated chromosomal instability remains uncharted. Here we report that LANA promoted the induction of chromosomal instability and the formation of micronuclei and multinucleation through its interaction with one of the critical spindle checkpoint proteins, Bub1, and the resulting degradation of Bub1. This interaction occurs through the Knl and kinase domains of Bub1, identified as important for stability and degradation. These results suggest that LANA can dysregulate Bub1 activity, which leads to aberrant chromosome replication and aneuploidy, thus contributing to KSHV-mediated oncogenesis. Importance: This work represents the first set of results identifying a novel mechanism by which LANA, a latency-associated antigen encoded by KSHV, can induce the degradation of Bub1, a spindle checkpoint protein that is important for spindle checkpoint signaling and chromosome segregation. The downregulation of Bub1 mediated by LANA resulted in chromosomal instability, a hallmark of cancer. We further investigated the specific domains of Bub1 that are required for the interaction between LANA and Bub1. The results demonstrated that the Knl and kinase domains of Bub1 are required for the interaction between LANA and Bub1. In addition, we also investigated the mechanism by which LANA promoted Bub1 degradation. Our results showed that LANA interacted physically with the anaphase-promoting complex (APC/C), thus promoting the degradation of Bub1 in a ubiquitin-dependent process.
MeSH term(s)	Animals ; Antigens, Viral/metabolism ; Blotting, Western ; Chromosomal Instability ; Herpesvirus 8, Human/physiology ; Humans ; Immunoprecipitation ; Lymphoma, Primary Effusion/genetics ; Lymphoma, Primary Effusion/metabolism ; Lymphoma, Primary Effusion/virology ; Mice ; Micronuclei, Chromosome-Defective ; Nuclear Proteins/metabolism ; Protein-Serine-Threonine Kinases/metabolism ; Proteolysis ; Sarcoma, Kaposi/genetics ; Sarcoma, Kaposi/metabolism ; Sarcoma, Kaposi/virology ; Tumor Cells, Cultured ; Ubiquitin/metabolism ; Ubiquitination
Chemical Substances	Antigens, Viral ; Nuclear Proteins ; Ubiquitin ; latency-associated nuclear antigen ; BUB1 protein, human (EC 2.7.11.1) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2014-04-16
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.00554-14
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Article: [Ubiquitin-proteasome pathway].

Xiao, Bing-Yi / Li, Gui-Yuan

Zhong nan da xue xue bao. Yi xue ban = Journal of Central South University. Medical sciences

2004 Volume 29, Issue 2, Page(s) 230–232

MeSH term(s)	Animals ; Cardiomyopathies/metabolism ; Humans ; Inflammation/metabolism ; Neoplasms/metabolism ; Proteasome Endopeptidase Complex/metabolism ; Signal Transduction ; Ubiquitin/metabolism
Chemical Substances	Ubiquitin ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	Chinese
Publishing date	2004-04
Publishing country	China
Document type	Journal Article ; Review
ZDB-ID	2168533-2
ISSN	1672-7347
ISSN	1672-7347
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Zs.B 2681: Show issues

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Article ; Online: Melatonin synergizes the chemotherapeutic effect of 5-fluorouracil in colon cancer by suppressing PI3K/AKT and NF-κB/iNOS signaling pathways.

Gao, Yue / Xiao, Xiangsheng / Zhang, Changlin / Yu, Wendan / Guo, Wei / Zhang, Zhifeng / Li, Zhenglin / Feng, Xu / Hao, Jiaojiao / Zhang, Kefang / Xiao, Bingyi / Chen, Miao / Huang, Wenlin / Xiong, Shunbin / Wu, Xiaojun / Deng, Wuguo

Journal of pineal research

2017 Volume 62, Issue 2

Abstract: 5-Fluorouracil (5-FU) is one of the most commonly used chemotherapeutic agents in colon cancer treatment, but has a narrow therapeutic index limited by its toxicity. Melatonin exerts antitumor activity in various cancers, but it has never been combined ... ...

Abstract	5-Fluorouracil (5-FU) is one of the most commonly used chemotherapeutic agents in colon cancer treatment, but has a narrow therapeutic index limited by its toxicity. Melatonin exerts antitumor activity in various cancers, but it has never been combined with 5-FU as an anticolon cancer treatment to improve the chemotherapeutic effect of 5-FU. In this study, we assessed such combinational use in colon cancer and investigated whether melatonin could synergize the antitumor effect of 5-FU. We found that melatonin significantly enhanced the 5-FU-mediated inhibition of cell proliferation, colony formation, cell migration and invasion in colon cancer cells. We also found that melatonin synergized with 5-FU to promote the activation of the caspase/PARP-dependent apoptosis pathway and induce cell cycle arrest. Further mechanism study demonstrated that melatonin synergized the antitumor effect of 5-FU by targeting the PI3K/AKT and NF-κB/inducible nitric oxide synthase (iNOS) signaling. Melatonin in combination with 5-FU markedly suppressed the phosphorylation of PI3K, AKT, IKKα, IκBα, and p65 proteins, promoted the translocation of NF-κB p50/p65 from the nuclei to cytoplasm, abrogated their binding to the iNOS promoter, and thereby enhanced the inhibition of iNOS signaling. In addition, pretreatment with a PI3K- or iNOS-specific inhibitor synergized the antitumor effects of 5-FU and melatonin. Finally, we verified in a xenograft mouse model that melatonin and 5-FU exerted synergistic antitumor effect by inhibiting the AKT and iNOS signaling pathways. Collectively, our study demonstrated that melatonin synergized the chemotherapeutic effect of 5-FU in colon cancer through simultaneous suppression of multiple signaling pathways.
MeSH term(s)	Animals ; Antineoplastic Combined Chemotherapy Protocols/pharmacology ; Apoptosis/drug effects ; Blotting, Western ; Cell Line, Tumor ; Cell Movement/drug effects ; Cell Proliferation/drug effects ; Chromatin Immunoprecipitation ; Colonic Neoplasms/pathology ; Drug Synergism ; Fluorouracil/pharmacology ; Humans ; Immunohistochemistry ; Melatonin/pharmacology ; Mice ; Mice, Nude ; Microscopy, Confocal ; NF-kappa B/metabolism ; Nitric Oxide Synthase Type II/metabolism ; Phosphatidylinositol 3-Kinases/metabolism ; Proto-Oncogene Proteins c-akt/metabolism ; Signal Transduction/drug effects ; Xenograft Model Antitumor Assays
Chemical Substances	NF-kappa B ; Nitric Oxide Synthase Type II (EC 1.14.13.39) ; Phosphatidylinositol 3-Kinases (EC 2.7.1.-) ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1) ; Melatonin (JL5DK93RCL) ; Fluorouracil (U3P01618RT)
Language	English
Publishing date	2017-03
Publishing country	England
Document type	Journal Article
ZDB-ID	632697-3
ISSN	1600-079X ; 0742-3098
ISSN (online)	1600-079X
ISSN	0742-3098
DOI	10.1111/jpi.12380
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Zs.A 2114: Show issues

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Article ; Online: Kaposi's sarcoma herpesvirus upregulates Aurora A expression to promote p53 phosphorylation and ubiquitylation.

Cai, Qiliang / Xiao, Bingyi / Si, Huaxin / Cervini, Amanda / Gao, Jianming / Lu, Jie / Upadhyay, Santosh K / Verma, Suhbash C / Robertson, Erle S

PLoS pathogens

2012 Volume 8, Issue 3, Page(s) e1002566

Abstract: Aberrant expression of Aurora A kinase has been frequently implicated in many cancers and contributes to chromosome instability and phosphorylation-mediated ubiquitylation and degradation of p53 for tumorigenesis. Previous studies showed that p53 is ... ...

Abstract	Aberrant expression of Aurora A kinase has been frequently implicated in many cancers and contributes to chromosome instability and phosphorylation-mediated ubiquitylation and degradation of p53 for tumorigenesis. Previous studies showed that p53 is degraded by Kaposi's sarcoma herpesvirus (KSHV) encoded latency-associated nuclear antigen (LANA) through its SOCS-box (suppressor of cytokine signaling, LANA(SOCS)) motif-mediated recruitment of the EC(5)S ubiquitin complex. Here we demonstrate that Aurora A transcriptional expression is upregulated by LANA and markedly elevated in both Kaposi's sarcoma tissue and human primary cells infected with KSHV. Moreover, reintroduction of Aurora A dramatically enhances the binding affinity of p53 with LANA and LANA(SOCS)-mediated ubiquitylation of p53 which requires phosphorylation on Ser215 and Ser315. Small hairpin RNA or a dominant negative mutant of Aurora A kinase efficiently disrupts LANA-induced p53 ubiquitylation and degradation, and leads to induction of p53 transcriptional and apoptotic activities. These studies provide new insights into the mechanisms by which LANA can upregulate expression of a cellular oncogene and simultaneously destabilize the activities of the p53 tumor suppressor in KSHV-associated human cancers.
MeSH term(s)	Antigens, Viral/genetics ; Antigens, Viral/metabolism ; Aurora Kinases ; Cell Line, Tumor ; Gene Expression Regulation, Viral ; Herpesvirus 8, Human/genetics ; Herpesvirus 8, Human/metabolism ; Humans ; Leukocytes, Mononuclear/metabolism ; Leukocytes, Mononuclear/pathology ; Leukocytes, Mononuclear/virology ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Phosphorylation ; Protein-Serine-Threonine Kinases/genetics ; Protein-Serine-Threonine Kinases/metabolism ; RNA Interference ; Transcription, Genetic ; Transfection ; Tumor Suppressor Protein p53/genetics ; Tumor Suppressor Protein p53/metabolism ; Ubiquitination ; Up-Regulation
Chemical Substances	Antigens, Viral ; Nuclear Proteins ; Tumor Suppressor Protein p53 ; latency-associated nuclear antigen ; Aurora Kinases (EC 2.7.11.1) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2012-03-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7366
ISSN (online)	1553-7374
ISSN	1553-7366
DOI	10.1371/journal.ppat.1002566
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Epstein-Barr virus nuclear antigen 3C stabilizes Gemin3 to block p53-mediated apoptosis.

Cai, Qiliang / Guo, Yi / Xiao, Bingyi / Banerjee, Shuvomoy / Saha, Abhik / Lu, Jie / Glisovic, Tina / Robertson, Erle S

publication RETRACTED

PLoS pathogens

2011 Volume 7, Issue 12, Page(s) e1002418

Abstract: The Epstein-Barr nuclear antigen 3C (EBNA3C), one of the essential latent antigens for Epstein-Barr virus (EBV)-induced immortalization of primary human B lymphocytes in vitro, has been implicated in regulating cell proliferation and anti-apoptosis via ... ...

Abstract	The Epstein-Barr nuclear antigen 3C (EBNA3C), one of the essential latent antigens for Epstein-Barr virus (EBV)-induced immortalization of primary human B lymphocytes in vitro, has been implicated in regulating cell proliferation and anti-apoptosis via interaction with several cellular and viral factors. Gemin3 (also named DDX20 or DP103) is a member of DEAD RNA helicase family which exhibits diverse cellular functions including DNA transcription, recombination and repair, and RNA metabolism. Gemin3 was initially identified as a binding partner to EBNA2 and EBNA3C. However, the mechanism by which EBNA3C regulates Gemin3 function remains unclear. Here, we report that EBNA3C directly interacts with Gemin3 through its C-terminal domains. This interaction results in increased stability of Gemin3 and its accumulation in both B lymphoma cells and EBV transformed lymphoblastoid cell lines (LCLs). Moreover, EBNA3C promotes formation of a complex with p53 and Gemin3 which blocks the DNA-binding affinity of p53. Small hairpin RNA based knockdown of Gemin3 in B lymphoma or LCL cells remarkably attenuates the ability of EBNA3C to inhibit the transcription activity of p53 on its downstream genes p21 and Bax, as well as apoptosis. These findings provide the first evidence that Gemin3 may be a common target of oncogenic viruses for driving cell proliferation and anti-apoptotic activities.
MeSH term(s)	Antigens, Viral/genetics ; Antigens, Viral/metabolism ; Apoptosis/physiology ; B-Lymphocytes/metabolism ; B-Lymphocytes/virology ; Blotting, Western ; Cell Line, Tumor ; DEAD Box Protein 20/genetics ; DEAD Box Protein 20/metabolism ; Epstein-Barr Virus Infections/genetics ; Epstein-Barr Virus Infections/metabolism ; Epstein-Barr Virus Nuclear Antigens ; Fluorescent Antibody Technique ; Gene Expression Regulation, Neoplastic/genetics ; Gene Knockdown Techniques ; Herpesvirus 4, Human/genetics ; Herpesvirus 4, Human/metabolism ; Humans ; Immunoprecipitation ; Real-Time Polymerase Chain Reaction ; Reverse Transcriptase Polymerase Chain Reaction ; Transfection ; Tumor Suppressor Protein p53/genetics ; Tumor Suppressor Protein p53/metabolism
Chemical Substances	Antigens, Viral ; EBNA-3C, epstein-barr virus ; Epstein-Barr Virus Nuclear Antigens ; TP53 protein, human ; Tumor Suppressor Protein p53 ; DEAD Box Protein 20 (EC 3.6.1.-)
Language	English
Publishing date	2011-12-08
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Retracted Publication
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7366
ISSN (online)	1553-7374
ISSN	1553-7366
DOI	10.1371/journal.ppat.1002418
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Article ; Online: Bub1 and CENP-F can contribute to Kaposi's sarcoma-associated herpesvirus genome persistence by targeting LANA to kinetochores.

Xiao, Bingyi / Verma, Subhash C / Cai, Qiliang / Kaul, Rajeev / Lu, Jie / Saha, Abhik / Robertson, Erle S

Journal of virology

2010 Volume 84, Issue 19, Page(s) 9718–9732

Abstract: The latency-associated nuclear antigen (LANA) encoded by Kaposi's sarcoma-associated herpesvirus (KSHV) is critical for segregation of viral episomes to progeny nuclei and allows for maintenance of the viral genome in newly divided daughter cells. LANA ... ...

Abstract	The latency-associated nuclear antigen (LANA) encoded by Kaposi's sarcoma-associated herpesvirus (KSHV) is critical for segregation of viral episomes to progeny nuclei and allows for maintenance of the viral genome in newly divided daughter cells. LANA binds to KSHV terminal repeat (TR) DNA and simultaneously associates with chromatin-bound cellular proteins. This process tethers the viral episomes to host chromosomes. However, the mechanism of tethering is complex and involves multiple protein-protein interactions. Our previous proteomics studies which showed the association of LANA with centromeric protein F (CENP-F) prompted us to further study whether LANA targets centromeric proteins for persistence of KSHV episomes during cell division. Here we show that LANA colocalized with CENP-F as speckles, some of which are paired at centromeric regions of a subset of chromosomes in KSHV-infected JSC-1 cells. We also confirm that both the amino and carboxy termini of LANA can bind to CENP-F. Moreover, LANA associated with another kinetochore protein, Bub1 (budding uninhibited by benzimidazole 1), which is known to form a complex with CENP-F. Importantly, we demonstrated the dynamic association of LANA and Bub1/CENP-F and the colocalization between Bub1, LANA, and the KSHV episome tethered to the host chromosome using fluorescence in situ hybridization (FISH). Knockdown of Bub1 expression by lentivirus-delivered short hairpin RNA (shRNA) dramatically reduced the number of KSHV genome copies, whereas no dramatic effect was seen with CENP-F knockdown. Therefore, the interaction between LANA and the kinetochore proteins CENP-F and Bub1 is important for KSHV genome tethering and its segregation to new daughter cells, with Bub1 potentially playing a more critical role in the long-term persistence of the viral genome in the infected cell.
MeSH term(s)	Antigens, Viral/chemistry ; Antigens, Viral/genetics ; Antigens, Viral/metabolism ; Base Sequence ; Cell Line ; Chromosomal Proteins, Non-Histone/antagonists & inhibitors ; Chromosomal Proteins, Non-Histone/genetics ; Chromosomal Proteins, Non-Histone/metabolism ; Gene Knockdown Techniques ; Genome, Viral ; Herpesvirus 8, Human/genetics ; Herpesvirus 8, Human/pathogenicity ; Herpesvirus 8, Human/physiology ; Host-Pathogen Interactions ; Humans ; In Vitro Techniques ; Kinetochores/metabolism ; Kinetochores/virology ; Microfilament Proteins/antagonists & inhibitors ; Microfilament Proteins/genetics ; Microfilament Proteins/metabolism ; Mitosis ; Models, Biological ; Nuclear Proteins/chemistry ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Plasmids/genetics ; Protein Interaction Mapping ; Protein-Serine-Threonine Kinases/antagonists & inhibitors ; Protein-Serine-Threonine Kinases/genetics ; Protein-Serine-Threonine Kinases/metabolism ; RNA, Small Interfering/genetics
Chemical Substances	Antigens, Viral ; Chromosomal Proteins, Non-Histone ; Microfilament Proteins ; Nuclear Proteins ; RNA, Small Interfering ; centromere protein F ; latency-associated nuclear antigen ; BUB1 protein, human (EC 2.7.11.1) ; Bub1 spindle checkpoint protein (EC 2.7.11.1) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2010-07-21
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.00713-10
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Article ; Online: Latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus (KSHV) upregulates survivin expression in KSHV-Associated B-lymphoma cells and contributes to their proliferation.

Lu, Jie / Verma, Subhash C / Murakami, Masanao / Cai, Qiliang / Kumar, Pankaj / Xiao, Bingyi / Robertson, Erle S

Journal of virology

2009 Volume 83, Issue 14, Page(s) 7129–7141

Abstract: Survivin is a master regulator of cell proliferation and cell viability and is highly expressed in most human tumors. The molecular network linked to survivin expression in tumors has not been completely elucidated. In this study, we show that latency- ... ...

Abstract	Survivin is a master regulator of cell proliferation and cell viability and is highly expressed in most human tumors. The molecular network linked to survivin expression in tumors has not been completely elucidated. In this study, we show that latency-associated nuclear antigen (LANA), a multifunctional protein of Kaposi's sarcoma-associated herpesvirus (KSHV) that is found in Kaposi's sarcoma tumors, upregulates survivin expression and increases the proliferation of KSHV-infected B cells. Analysis of pathway-specific gene arrays showed that survivin expression was highly upregulated in BJAB cells expressing LANA. The mRNA levels of survivin were also upregulated in HEK 293 and BJAB cells expressing LANA. Similarly, protein levels of survivin were significantly higher in LANA-expressing, as well as KSHV-infected, cells. Survivin promoter activity assays identified GC/Sp1 and p53 cis-acting elements within the core promoter region as being important for LANA activity. Gel mobility shift assays revealed that LANA forms a complex with Sp1 or Sp1-like proteins bound to the GC/Sp1 box of the survivin promoter. In addition, a LANA/p53 complex bound to the p53 cis-acting element within the survivin promoter, indicating that upregulation of survivin expression can also occur through suppression of p53 function. Furthermore, immunohistochemistry analyses revealed that survivin expression was upregulated in KSHV-associated Kaposi's sarcoma tissue, suggesting that LANA plays an important role in the upregulation of survivin expression in KSHV-infected endothelial cells. Knockdown of survivin expression by lentivirus-delivered small hairpin RNA resulted in loss of cell proliferation in KSHV-infected cells. Therefore, upregulation of survivin expression in KSHV-associated human cells contributes to their proliferation.
MeSH term(s)	Antigens, Viral/genetics ; Antigens, Viral/metabolism ; Cell Line ; Cell Proliferation ; Gene Expression Regulation ; Herpesvirus 8, Human/genetics ; Herpesvirus 8, Human/metabolism ; Humans ; Inhibitor of Apoptosis Proteins ; Lymphoma, B-Cell/genetics ; Lymphoma, B-Cell/metabolism ; Lymphoma, B-Cell/physiopathology ; Lymphoma, B-Cell/virology ; Microtubule-Associated Proteins/genetics ; Microtubule-Associated Proteins/metabolism ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Promoter Regions, Genetic ; Protein Binding ; Sarcoma, Kaposi/genetics ; Sarcoma, Kaposi/metabolism ; Sarcoma, Kaposi/physiopathology ; Sarcoma, Kaposi/virology ; Sp1 Transcription Factor/genetics ; Sp1 Transcription Factor/metabolism ; Survivin ; Tumor Suppressor Protein p53/genetics ; Tumor Suppressor Protein p53/metabolism ; Up-Regulation
Chemical Substances	Antigens, Viral ; BIRC5 protein, human ; Inhibitor of Apoptosis Proteins ; Microtubule-Associated Proteins ; Nuclear Proteins ; Sp1 Transcription Factor ; Survivin ; Tumor Suppressor Protein p53 ; latency-associated nuclear antigen
Language	English
Publishing date	2009-05-13
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.00397-09
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Article: [Analysis of splicing variants in NASG 3'UTR, down-regulated in nasopharyngeal carcinoma, and its expression in multiple cancer tissues].

Zhang, Bi-Cheng / Zhu, Shi-Guo / Xiang, Juan-Juan / Zhou, Ming / Nie, Xin-Min / Xiao, Bing-Yi / Li, Xiao-Ling / Li, Gui-Yuan

Ai zheng = Aizheng = Chinese journal of cancer

2003 Volume 22, Issue 5, Page(s) 477–480

Abstract: Background & objective: NASG gene, a tissue-specific gene of human nasopharyngeal epithelium was isolated by suppression subtractive hybridization. This study was designed to analyze splicing variants in NASG 3'untranslated region (UTR) and its ... ...

Abstract	Background & objective: NASG gene, a tissue-specific gene of human nasopharyngeal epithelium was isolated by suppression subtractive hybridization. This study was designed to analyze splicing variants in NASG 3'untranslated region (UTR) and its expression profiling in multiple cancer tissues. Methods: The PCR primers were designed in NASG 3'UTR around the splicing variants and reverse transcription-polymerase chain reaction (RT-PCR) was performed. The PCR products were separated and sequenced. The expression patterns of NASG were detected by RT-PCR among nasopharyngeal carcinoma (NPC) cell line HNE1, primary human embryo nasopharyngeal epithelial cells, NPC biopsies, and normal adult nasopharyngeal epithelial tissues. Its expression profiling in multiple cancer tissues were tested by cancer profiling array hybridization. Results: There were three splicing variants in NASG 3'UTR. NASG was identified to be down-regulated in NPC cell line HNE1 and 71% of the NPC biopsies, but up-regulated in 25% lung of the cancer biopsies, and not express in other cancer tissues and normal tissues. Conclusion: There were three splicing variants in NASG 3'UTR. Its abnormal expression may be an important molecular event in NPC and lung cancer.
MeSH term(s)	3' Untranslated Regions/genetics ; Adult ; Alternative Splicing ; Base Sequence ; DNA, Neoplasm/analysis ; Down-Regulation ; Gene Expression Regulation, Neoplastic ; Glycoproteins/genetics ; Glycoproteins/metabolism ; Humans ; Molecular Sequence Data ; Nasopharyngeal Neoplasms/genetics ; Nasopharyngeal Neoplasms/metabolism ; Neoplasm Proteins/genetics ; Neoplasm Proteins/metabolism ; Phosphoproteins/genetics ; Phosphoproteins/metabolism ; Sequence Analysis, DNA
Chemical Substances	3' Untranslated Regions ; BPIFA1 protein, human ; DNA, Neoplasm ; Glycoproteins ; Neoplasm Proteins ; Phosphoproteins
Language	Chinese
Publishing date	2003-05
Publishing country	China
Document type	English Abstract ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1045160-2
ISSN	1944-446X ; 1000-467X
ISSN (online)	1944-446X
ISSN	1000-467X
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Zs.A 6213: Show issues

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Article: [Expression of a new cloned nitroreductase gene NOR1 and purification of expressed product].

Nie, Xin-Min / Xiao, Bing-Yi / Li, Xiao-Ling / Zhang, Bi-Cheng / Li, Wei-Fang / Wang, Rong / Cao, Li / Li, Gui-Yuan

Ai zheng = Aizheng = Chinese journal of cancer

2003 Volume 22, Issue 2, Page(s) 136–139

Abstract: Background & objective: NOR(1)is a good candidate of tumor suppressor/susceptibility gene associated with nasopharyngeal carcinoma. This study was designed to construct the prokaryotic expression vector and to investigate the expression of ... ...

Abstract	Background & objective: NOR(1)is a good candidate of tumor suppressor/susceptibility gene associated with nasopharyngeal carcinoma. This study was designed to construct the prokaryotic expression vector and to investigate the expression of nitroreductase gene NOR(1)in Escherichia coli and to purify expressed product. Methods: Total RNA was subtracted from normal nasopharyngeal carcinoma tissue. The full length of NOR(1)gene was amplified by reverse transcription-polymerase chain reaction (RT-PCR) and digested with BamHIand XhoI restriction endonucleases. The plasmid pGEX-4T-2 was also digested with BamHI and XhoI,then the NOR(1)gene was inserted into vector pGEX-4T-2. The recombinant expression vector pGEX-4T-2/NOR(1)was identified by sequencing and digested with restriction enzymes. E.coli Jm105 transformed with the recombinant plasmid was induced by IPTG to express GST fusion protein. The result was confirmed by Western blot analysis and the purified targeted protein was obtained by affinity chromatography. Results: The 1.25kb NOR(1)gene was successfully isolated. After induction, a new anticipated protein of 74 kDa appeared on sodium dodecylsulfate polyacrylamide gel electrophoresis (SDS-PAGE). It existed not only in supernatant but also in precipitation of broken bacteria. The result was confirmed by Western blot analysis,and the purified targeted protein was obtained by affinity chromatography. Conclusion: The successes in construction of expression vector of NOR(1), expression and purification of GST/NOR(1)fusion protein make it possible to prepare for the polyantibodies for NOR(1).
MeSH term(s)	Cloning, Molecular ; Escherichia coli/genetics ; Humans ; Nitroreductases/biosynthesis ; Nitroreductases/genetics ; Nitroreductases/isolation & purification ; Recombinant Proteins/biosynthesis
Chemical Substances	Recombinant Proteins ; Nitroreductases (EC 1.7.-)
Language	Chinese
Publishing date	2003-02
Publishing country	China
Document type	English Abstract ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1045160-2
ISSN	1944-446X ; 1000-467X
ISSN (online)	1944-446X
ISSN	1000-467X
Database	MEDical Literature Analysis and Retrieval System OnLINE

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