bluuebunny/crossref_metadata_2025_split huggingface dataset:
Abstract LB-168: Genistein sensitizes radio-resistant cancer cells through regulation of NF-kappaB
Authors: Kim Su-Hyeon , Song Yong-Sang 
Published: February 2011

Abstract
Background: NF-kappaB is a key transcription factor involved in the control of normal cellular and organismal processes, such as immune and inflammatory responses, developmental processes, cellular growth, and apoptosis. However, NF-kappaB is persistently active in a number of disease states, including cancer. It has been reported that chemo- or radio- resistant cancer cells had elevated NF-kappaB activity. Recent studies including ours have showed that genistein, a soy-derived isoflavonoid, has antitumor activity in various cancer cells.
Objective: In this study, we evaluated whether genistein could sensitize ionizing radiation resistance of cervical cancer cells through regulation of NF-kappaB.
Methods: Six cervical cancer cell lines (HeLa, CaSki, C33A, ME180, SiHa, HeLa229) were treated by 20 Gy radiation with 50 M genistein or not. Cell growth rate was measured by MTT assay and protein expression level was analyzed by western blotting. Protein localization was observed by confocal microscopic analysis. NF-kappaB transcriptional activity was measured by luciferase reporter gene assay. NF-kappaB DNA binding activity was evaluated by electophoretic mobility shift assay.
Results: Among six cervical cancer cells, HeLa and HeLa229 cells showed radio-resistance accompanied by elevated NF-kappaB activity. Ionizing radiation induced NF-kappaB nuclear transclocation and stimulated NF-kappaB DNA binding and transcriptional activities. However, pretreatment with genistein inhibited radiation induced transcriptional activity coincident to decreased radio-resistancy. Genistein also inhibited radiation-induced NF-kappaB regulated anti-apoptotic gene expression including c-myc, Survivin, XIAP, Bcl-2, IAP-1, TRAF, A1/Bfl-1 and FLIP.
Conclusion: Taken together, genistein can sensitize radio-resistant cancer cells through regulation of NF-kappaB and could be used as a radio-sensitizer for the treatment of cervical cancer.
Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 101st Annual Meeting of the American Association for Cancer Research; 2010 Apr 17-21; Washington, DC. Philadelphia (PA): AACR; Cancer Res 2010;70(8 Suppl):Abstract nr LB-168.
Abstract LB-172: Transgene presence in patients’ tumors following tumor-targeted nanodelivery
Authors: Pirollo Kathleen F. , Nemunaitis John J. , Senzer Neil N. , Sleer Leanne , Chang Esther H. 
Published: February 2011

Abstract
Discussant: William F. Benedict, UT M. D. Anderson Center, Houston, TX.
Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 101st Annual Meeting of the American Association for Cancer Research; 2010 Apr 17-21; Washington, DC. Philadelphia (PA): AACR; Cancer Res 2010;70(8 Suppl):Abstract nr LB-172.
Abstract LB-18: The Cullin 3 substrate adaptor DIP-2 mediates DAPK ubiquitination to control interferon responses
Authors: Shen Che-Hung , Lee Yu-Ru , Ho Hsuan-Chung , Yuan Wei-Chien , Chen Chun-Hau , Shih Hsiu-Ming , Chen Ruey-Hwa 
Published: February 2011

Abstract
Death-associated protein kinase (DAPK) is a pro-apoptotic, calmodulin-regulated serine/threonine kinase and was originally identified based on its involvement in interferon- -induced cell death. Whether and how interferon-γ-signaling regulates the activity or expression of DAPK remains largely unexplored. In this study, we identify the BTB-Kelch protein DIP2 functions as a negative regulator of DAPK by potentiating the proteosomal degradation of DAPK. DIP2 binds DAPK and Cul3 via its Kelch repeats and BTB domain, respectively. The DIP2-Cul3-ROC1 E3 ligase complex promotes DAPK ubiquitination both in vivo and in vitro, and downregulation of endogenous DIP2 diminishes DAPK ubiquitination and biological functions. The DIP2-dependent DAPK ubiquitination is suppressed in cells receiving either interferon-α or interferon-γ, which induces an enrichment/sequestration of DIP2 in the PML nuclear bodies, thereby separating DIP2 from its substrate DAPK. Through disrupting the interaction of DAPK with its E3 ligase, interferon triggers the stabilization of pro-apoptotic DAPK, which contributes to the cell death-promoting function of interferon. This study not only identifies the DIP2-Cul3-ROC1 complex as an E3 ligase for DAPK ubiquitination, but also reveals the underlying mechanism of DAPK regulation by interferon.
Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 101st Annual Meeting of the American Association for Cancer Research; 2010 Apr 17-21; Washington, DC. Philadelphia (PA): AACR; Cancer Res 2010;70(8 Suppl):Abstract nr LB-18.
Abstract LB-182: Serum amyloid A is elevated in serum of lung cancer patients with poor prognosis
Authors: Cho William Chi Shing , Cheng Wai-wai , Yip Tai-tong , Au Joseph SK 
Published: February 2011

Abstract
Discussion
Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 101st Annual Meeting of the American Association for Cancer Research; 2010 Apr 17-21; Washington, DC. Philadelphia (PA): AACR; Cancer Res 2010;70(8 Suppl):Abstract nr LB-182.
Abstract LB-184: Identification of breast cancer susceptibility genes using whole exome sequencing
Authors: Thompson Ella , Ellul Jason , Li Jason , Doyle Maria , Campbell Ian 
Published: February 2011

Abstract
Discussion
Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 101st Annual Meeting of the American Association for Cancer Research; 2010 Apr 17-21; Washington, DC. Philadelphia (PA): AACR; Cancer Res 2010;70(8 Suppl):Abstract nr LB-184.
Abstract LB-195: Anti-CD40 and CpG-ODN enhance the antimelanoma response of hu14.18K322A in vivo.
Authors: Alderson Kory L. , Luangrath Mitchell , Gillies Stephen D. , Navid Fariba , Rakhmilevich Alexander L. , Sondel Paul M. 
Published: February 2011

Abstract
Discussion
Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 101st Annual Meeting of the American Association for Cancer Research; 2010 Apr 17-21; Washington, DC. Philadelphia (PA): AACR; Cancer Res 2010;70(8 Suppl):Abstract nr LB-195.
Abstract LB-198: Collagen remodeling and tissue mechanics at different stages of mammary tumor development
Authors: Yu Hongmei , Weaver Valerie M. 
Published: February 2011

Abstract
Discussion
Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 101st Annual Meeting of the American Association for Cancer Research; 2010 Apr 17-21; Washington, DC. Philadelphia (PA): AACR; Cancer Res 2010;70(8 Suppl):Abstract nr LB-198.
Abstract LB-207: IFN-Γ directly regulates ifi202B expression to maintain CTL proliferation potential and tumor rejection efficacy
Authors: Zimmerman Mary A. , Liu Kebin 
Published: February 2011

Abstract
A common procedure in human cytotoxic T lymphocyte (CTL) adoptive transfer cancer immunotherapy is to propagate tumor-specific CTLs in vitro using anti-CD3 mAb prior to transfer. One of the major impediments of CTL adoptive cancer immunotherapy is lack of CTL persistence in the tumor-bearing host after adoptive transfer. Therefore, maintaining CTL proliferation and persistence in the tumor microenvironment is of great significance in cancer immunotherapy. In this study, we observed that stimulation of tumor-specific CTLs with anti-CD3 mAb results in loss of proliferative potential and poor tumor-rejection efficacy in vivo, whereas, stimulation with tumor-specific antigen maintains CTL proliferative potential and persistence, leading to potent tumor rejection in an experimental lung metastasis mouse model. Analysis of genome-wide gene expression profile revealed that ifi202B, a gene with known function in regulating T cell proliferation and apoptosis, was dramatically up-regulated in antigen-stimulated but not in anti-CD3 mAb-stimulated CTLs. Furthermore, although both antigen- and anti-CD3 mAb-stimulated CTLs express similar level of IFN-Γ receptor, antigen stimulation led to rapid activation of STAT1, a key mediator of the IFN-Γ signaling pathway, whereas anti-CD3 mAb stimulation failed to activate STAT1. We further demonstrated that activated STAT1 binds to the promoter of ifi202b gene in T cells. Taken together, these observations suggest that IFN-Γ produced by the activated CTLs and the IFN-Γ signaling pathway plays a critical role in maintaining CTL proliferation and persistence in the tumor microenvironment through regulating ifi202B.
Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 101st Annual Meeting of the American Association for Cancer Research; 2010 Apr 17-21; Washington, DC. Philadelphia (PA): AACR; Cancer Res 2010;70(8 Suppl):Abstract nr LB-207.
Abstract LB-230: Automating sample preparation for single-cell protein phosphorylation analysis by flow cytometry
Authors: Liu Li , Eluwa Kelechi , Grom Patricia , Yoder Amy , Kowalski Michael , Song Yong , Shankey T. Vincent 
Published: February 2011

Abstract
Protein phosphorylation plays essential roles in regulating cellproliferation, differentiation and other cellular processes. Aberrant regulation of protein kinases, can drive malignancy through inappropriate cell growth and survival signals. Understanding the phosphorylation status of specific cellular proteins in cancer has proven valuable in developing targeted therapies and assays to identify specific drug responses in individual cancer patients.
The ability to analyze cells at the single cell level allows flow cytometry to measure protein phosphorylation in rare subsets of cells in complex populations such as blood or bone marrow specimens. However, sample preparation for protein phosphorylation analysis by flow cytometry can be technically challenging, time-consuming, and subject to error when performed manually. Furthermore, the procedure demands strict control of experimental conditions such as time and temperature due to the dynamic nature of protein phosphorylation. In this report, we describe an automated sample preparation method using a @Biomek® NXP Span-8 work-station to monitor the phosphorylation status of ERK and p38 MAPK in human peripheral blood monocytes. The method allows automation of sample preparation steps, including 1) ERK/p38 MAPK stimulation, 2) fixation, 3) erythrocyte lysis, 4) cell permeabilization, and, 5) staining with phospho-specific and cell surface marker antibodies. Using this approach, we were able to observe p38 MAPK and ERK activation in CD14+ monocytes following lipopolysaccharide (LPS) or phorbol-12-myristate-13 acetate (PMA) treatment. The automated sample preparation workstation is capable of processing 48 samples in approximately 2.5 hours.
Note: *Method cited Not for Clinical purposes. @For Laboratory Use Only; not for use in diagnostic procedures.
Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 101st Annual Meeting of the American Association for Cancer Research; 2010 Apr 17-21; Washington, DC. Philadelphia (PA): AACR; Cancer Res 2010;70(8 Suppl):Abstract nr LB-230.
Abstract LB-245: Nuclear translocation of HO-1 in prostate cancer. Role beyond heme degradation
Authors: Gueron Geraldine , Ferrando Mercedes , Elguero Belen , Salles Angeles , Meiss Roberto , Colombo Lucas , Curino Alejandro , Facchinetti Maria Marta , Navone Nora , De Siervi Adriana , Vazquez Elba 
Published: February 2011

Abstract
Prostate cancer (PCa) is the second leading cause of cancer-associated death in men. The metastatic spread of PCa cells and the ability to survive when reaching the metastatic nitch is affected by growth factors, chemokines, angiogenic factors and hormones. Heme oxygenase-1 (HO-1), the inducible isoform of the rate-limiting enzyme in heme degradation, counteracts oxidative and inflammatory damage. Here we investigated its nuclear translocation in androgen sensitive (MDAPCa2b and LNCaP) and insensitive (PC3) PCa cell lines. Our results show that endogenous levels of HO-1 are markedly lower in PC3 compared to MDAPCa2b and LNCaP. Hemin treatment, a potent and specific inducer of HO-1, increased protein levels with a resulting nuclear translocation in PCa cell lines. Stable transfection of HO-1 in PC3 (PC3HO-1) also showed a significant nuclear translocation. Furthermore, human prostate cancer PC3HO-1 cells growing subcutaneously in athymic nude mice showed significant HO-1 nuclear staining (detected by immunohistochemsitry and immunofluorescence) compared to PC3pcDNA3 xenografts. Using RT-qPCR-generated gene array we observed a set of inflammatory and angiogenic genes up- or down-regulated in response to HO-1 overexpression, identifying VEGFA as a novel downstream target of HO-1. HO-1 modulation limited the metastatic potential of neoplastic cells by down-regulating VEGFA production. An in vivo angiogenic assay also demonstrated that PC3HO-1 tumors presented less neovascularization than tumors derived from control cells, giving further evidence to support HO-1 anti-angiogenic function. These results implicate for the first time HO-1 in the regulation of key proinflammatory factors, involved in PCa progression. Taken together our results suggest that HO-1 may be a potential target for therapeutic interventions.
Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 101st Annual Meeting of the American Association for Cancer Research; 2010 Apr 17-21; Washington, DC. Philadelphia (PA): AACR; Cancer Res 2010;70(8 Suppl):Abstract nr LB-245.
Abstract LB-25: Regulation of Np63α by IκB kinase-β
Authors: Chatterjee Aditi , Chang Xiaofei , Sen Tanusree , Ravi Rajani , Bedi Atul , Sidransky David 
Published: February 2011

Abstract
The p53 family (p53, p73, p63) plays an instrumental role in the cellular stress response, including induction of cell cycle arrest and apoptosis in response to DNA damage. In addition to p63 and p73 isotypes capable of transactivating downstream target gene expression (TA isotypes), both genes also express dominant negative inhibitory isoforms, such as ΔNp63α. ΔNp63 is degraded in response to DNA damaging agents, thereby enabling an effective cellular response to genotoxic agents. Here, we identify a key molecular mechanism underlying the regulation of ΔNp63α expression in response to extrinsic stimuli, such as chemotherapeutic agents or TNF-α. We show that ΔNp63α interacts with IκB kinase (IKK), a multisubunit protein kinase that consists of two catalytic subunits, IKKα and IKKβ, and a regulatory subunit, IKKγ (NEMO-NF-κB essential modifier). We find that IKK kinase promotes ubiquitin-mediated proteasomal degradation of ΔNp63α, whereas a kinase-deficient mutant IKK -K44A fails to do so. Cytokine- or chemotherapy-induced stimulation of IKKβ leads to degradation of ΔNp63α and augments trans-activation of p53 family-induced genes involved in the cellular response to DNA damage. Conversely, inhibition of IKKβ with a NEMO-binding peptide or siRNA-mediated silencing IKKβ expression attenuates cytokine- or chemotherapy induced degradation of ΔNp63α. These data demonstrate that IKKβ plays an essential role in regulating ΔNp63α in response to extrinsic stimuli. Our findings suggest that the activation of IKK may be a mechanism by which levels of ΔNp63α are reduced, thereby rendering the cells susceptible to cell death in the face of cellular stress or DNA damage.
Note: This abstract was not presented at the AACR 101st Annual Meeting 2010 because the presenter was unable to attend.
Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 101st Annual Meeting of the American Association for Cancer Research; 2010 Apr 17-21; Washington, DC. Philadelphia (PA): AACR; Cancer Res 2010;70(8 Suppl):Abstract nr LB-25.
Abstract LB-260: Sensitivity of breast cancer stem cells to TRA-8 anti-DR5 monoclonal antibody
Authors: Joshi Angelina I. Londoño , Oliver Patsy G. , Forero Andres , LoBuglio Albert F. , Buchsbaum Donald J. 
Published: February 2011

Abstract
Breast cancer stem cells (BrCSC) are reported to be responsible for self-replication, treatment resistance, and metastases. Doubly enriched populations of BrCSC have been isolated using combined stem cell markers for CD44+/CD24- and increased levels of ALDEFLUOR® positivity based on aldehyde dehydrogenase enzyme activity. We have examined the sensitivity of doubly enriched populations of BrCSC isolated from basal-like breast cancer cell lines as regards anti-DR5 agonistic monoclonal antibody (TRA-8) mediated cytotoxicity. Methods: BrCSC were isolated and characterized from basal breast cancer cell lines (SUM159, SUM149, HCC38 and 2LMP) based on the intracellular accumulation of ALDEFLUOR® reagent and CD44+/CD24- surface expression by flow cytometry. DR5 expression on the BrCSC subpopulation, in vitro cytotoxicity after 24 h exposure to TRA-8, and caspase activation after TRA-8 exposure were evaluated. The effects of TRA-8 on secondary tumorosphere formation were also investigated. Results: Unsorted basal-like cell lines were highly sensitive to TRA-8 mediated cytotoxicity with IC50 values of 0.7-3.0 ng/ml. Doubly enriched CD44+/CD24−/ALDEFLUOR+ BrCSC from these cell lines exhibited comparable DR5 expression and were similarly highly sensitive to TRA-8 induced cytotoxicity with rapid induction of caspase 3 and 8 cleavage. Secondary tumorosphere formation was greater than 90% inhibited by TRA-8 exposure. An agonistic anti-DR4 monoclonal antibody (2E12) had no effect, and TRAIL was only partially inhibitory to secondary tumorosphere formation at equimolar concentrations. TRA-8 effect on BrCSC tumorigenicity will be presented. These studies suggest that TRA-8 may be an effective targeted therapy directed at BrCSC in basal-like breast cancer patients.
Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 101st Annual Meeting of the American Association for Cancer Research; 2010 Apr 17-21; Washington, DC. Philadelphia (PA): AACR; Cancer Res 2010;70(8 Suppl):Abstract nr LB-260.
Abstract LB-27: Systematic identification of genes contained the translational regulation element IRES in the cancer development
Authors: Tseng Joseph Ta-Chien 
Published: February 2011

Abstract
Internal Ribosome Entry Site (IRES) is a cis-acting element located at the 5′ untranslated region to regulate the protein translation. Translation by internal ribosome entry was first identified in picornaviruses, but a number of cellular mRNAs containing IRESs have subsequently been found, including basic fibroblast growth factor, c-myc, p53, and HIF-1. Till now, around 80 cellular IRES elements have been identified, almost half found in genes encoding oncogenes, growth factors, and proteins involved in the regulation of apoptosis. This suggests that IRES-dependent translation is an important regulatory mechanism for the maintenance of cellular homeostasis, especially when cap-dependent initiation is inhibited. Therefore, it would be interested to understand how many genes bearing the IRES to elucidate the functional role of IRES. In this study, the pattern search algorithm was used to screen the whole human transcripts to identify the genes bearing the IRES elements. A special phenomenon which multiple IRES structures existed in specific region was found, and this region was named as internal ribosome entry zone (IREZone). The total human transcripts were identified to contain the IRES or IREZone element about 24.8% and 45.6%, respectively. By using bicistronic assay, the activity of IRES zone is higher then the single IRES existed in the 5′UTR of c-jun. Via Ingenuity software, we found that the cancer-related genes carry multiple IRES or IREZone in their 5′UTR. This result indicated these cancer-related genes are more tightly regulated at translational level to express the protein in the right time. And the mis-regulation of these proteins expression may lead to the cancer development.
Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 101st Annual Meeting of the American Association for Cancer Research; 2010 Apr 17-21; Washington, DC. Philadelphia (PA): AACR; Cancer Res 2010;70(8 Suppl):Abstract nr LB-27.
Abstract LB-274: Clinical significance of MUC1, MUC2 and CK17 expression patterns in the diagnosis of pancreatic carcinoma
Authors: Yang Haisu , Tamayo Rosalba , Horten Bruce , DaSilva Moacyr , Gangi Maryann , Vazquez Evelyn , Joseph Daisy , Okamoto Patricia , Scholl Thomas 
Published: February 2011

Abstract
Pancreatic cancer is characterized by aggressive growth and treatment resistance. Identification of unique biomarkers for diagnosis and prognosis is important in the treatment of this disease. In this study, we investigated the expression patterns of MUC1, MUC2 and CK17 in normal tissues as well as metastatic adenocarcinomas by immunohistochemical analysis. Our results clearly show that MUC1 (pan-epithelial membrane mucin), MUC2 (intestinal-type secretory mucin) and CK17 can be utilized as a panel of markers to collectively distinguish pancreatobiliary carcinoma from other primary site carcinomas. That is, tumors originating in the pancreatobiliary system showed an expression pattern of MUC1 (+), MUC2 (-) and CK17 (+). In contrast, tumors that arose from the colorectal region were MUC1 (-), MUC2 (+) and CK17 (-), while those originating from the lung and kidney had a MUC1 (+), MUC2 (-) and CK17 (-) expression profile. More importantly, the MUC1 (+), MUC2 (-) and CK17 (+) result displayed greater sensitivity and specificity than CA19-9, which is the currently accepted and widely used pancreatic tumor marker for the diagnosis of pancreatic cancer. Taken together, our data support an antibody panel that can enhance the current methods for pancreatic cancer diagnosis by specifically identifying the primary tissue of origin from which pancreatic carcinomas are derived.
Note: This abstract was not presented at the AACR 101st Annual Meeting 2010 because the presenter was unable to attend.
Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 101st Annual Meeting of the American Association for Cancer Research; 2010 Apr 17-21; Washington, DC. Philadelphia (PA): AACR; Cancer Res 2010;70(8 Suppl):Abstract nr LB-274.