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  • 1
    Keywords: CANCER ; SURVIVAL ; carcinoma ; Germany ; LUNG ; TOXICITY ; lung cancer ; LUNG-CANCER ; DISEASE ; TIME ; PATIENT ; primary ; QUALITY ; treatment ; STAGE ; DIFFERENCE ; CLINICAL-TRIALS ; RATES ; chemotherapy ; ELDERLY-PATIENTS ; PHASE-III ; MULTICENTER TRIAL ; PLUS VINORELBINE ; QUALITY-OF-LIFE ; SINGLE-AGENT GEMCITABINE
    Abstract: Purpose To evaluate whether cisplatin-based chemotherapy (gemcitabine, vinorelbine, and cisplatin [GVP]) prolongs overall survival in comparison to cisplatin-free chemotherapy (gemcitabine and vinorelbine [GV]) as first-line treatment in patients with advanced non-small-cell lung cancer (NSCLC). Patients and Methods Between September 1999 and June 2001, 300 patients with NSCLC stage 11113 with malignant pleural effusion or stage IV disease were randomly assigned to receive GV (gemcitabine 1000 mg/m(2) + vinorelbine 25 mg/m(2) on days 1 and 8 every 3 weeks) or GVP (gemcitabine 1000 mg/m(2) + vinorelbine 25 mg/m(2) on days I and 8 + cisplatin 75 mg/m(2) on day 2 every 3 weeks). Primary end point of the study was overall survival. Results Two hundred eighty-seven patients (GV, 143 patients; GVP, 144 patients) were eligible for analysis. At the time of analysis, April 15, 2002, 209 patients (GV, 103 patients; GVP, 106 patients) of 287 patients had died (73%). No statistically significant difference was observed for overall survival (P =.73; median survival, 35.9 versus 32.4 weeks; 1-year survival rate, 33.6% versus 27.5%) as well as for event-free survival (P =.35; median time-to-event, 19.3 versus 22.3 weeks) between GV and GVP. Two hundred fourteen patients were assessable for best response. The overall response rates were 13.0% for GV versus 28.3% for GVP (P =.004; complete responders, 0% versus 3.8%; partial responders, 13.0% versus 24.5%). Hematologic and nonhematologic toxicity was significantly lower in the GV treatment arm compared with GVP. No statistically significant difference in quality of life was observed. Conclusion In this phase III study, the cisplatin-based GVP regimen showed no survival benefit as first-line chemotherapy in advanced NSCLC when compared with the cisplatin-free GV regimen, which was substantially better tolerated. (C) 2004 by American Society of Clinical Oncology
    Type of Publication: Journal article published
    PubMed ID: 15197195
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  • 2
    Keywords: CANCER ; EXPRESSION ; tumor ; human ; NEW-YORK ; ENZYMES ; PROTEIN ; PROTEINS ; TUMORS ; RELEASE ; PATIENT ; RESPONSES ; MESSENGER-RNA EXPRESSION ; ANTIGEN ; T cell ; T-CELL ; antibodies ; TARGET ; ASSAY ; poly(ADP-ribose) polymerase ; COLON-CANCER ; CD8(+) ; ELISPOT ; IMMUNE-RESPONSE ; IMMUNOTHERAPY ; DOMAINS ; protein expression ; ONCOLOGY ; RECOMBINANT ; humoral immune response ; SEREX ; LEVEL ; biomarker ; methods ; ASSAYS ; TELOMERASE ACTIVITY ; USA ; B-CELL ; immunology ; quantitative ; ANTIBODY-RESPONSE ; epitope mapping ; HUMAN AUTOANTIBODIES ; HUMAN GASTRIC CARCINOMAS ; POLY(ADENOSINE DIPHOSPHATE-RIBOSE) POLYMERASE ; REPEAT-BINDING FACTOR-1 ; STERILE ALPHA-MOTIF ; telomerase-interacting proteins
    Abstract: Purpose Tankyrases 1 and 2 are telomere-associated poly(ADP-ribose) polymerases (PARP) that can positively regulate telomere elongation and interact with multiple cellular proteins. Recent reports implicated tankyrases as tumor antigens and potential targets of anticancer treatment. We examined expression of tankyrases in colon tumors and immune response to these enzymes in patients with different types of cancer. Methods mRNA and protein expression was evaluated by quantitative real-time RT-PCR and Western blotting, respectively. Humoral immune response to recombinant tankyrases was investigated by modified enzyme-linked immunoassays. Cellular immune response was analysed by ELISPOT and Cr-51 release assays. Results We found that both mRNA and protein levels of tankyrase 2 (TNKL) are upregulated in colon tumors. In contrast, protein level of tankyrase 1 (TNKS) is downregulated, while mRNA level shows variable changes. More than a quarter of colon cancer patients develop humoral immune response to at least one of the two tankyrases. In this study we mapped common and unique B-cell epitopes located in different domains of the two proteins. Additionally, we present evidence for T-cell responses both to epitopes that are unique for TNKL and to those shared between TNKL and TNKS. Conclusion Our study favors a biomarker usage of antibody response to tankyrases. Spontaneous CD8(+) T-cell responses to these enzymes are rare and further investigation is needed to evaluate tankyrases as potential targets for cancer immunotherapy
    Type of Publication: Journal article published
    PubMed ID: 18026951
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  • 3
    Keywords: CANCER ; CELLS ; EXPRESSION ; tumor ; CELL ; Germany ; MICROSCOPY ; THERAPY ; GENES ; PROTEIN ; cell line ; DIFFERENTIATION ; MOLECULAR CHARACTERIZATION ; MONOCLONAL-ANTIBODY ; TUMORS ; LINES ; PATIENT ; DOMAIN ; ANTIGEN ; ANTIGENS ; CONTRAST ; CELL-LINES ; BREAST ; breast cancer ; BREAST-CANCER ; antibodies ; antibody ; TARGET ; DELETION ; IDENTIFICATION ; immunohistochemistry ; MEMBRANE ; CELL-LINE ; LINE ; VACCINES ; LOCALIZATION ; CANCER-PATIENTS ; IMMUNITY ; IMMUNOTHERAPY ; CANCER PATIENTS ; mutagenesis ; cell lines ; ONCOLOGY ; RECOMBINANT ; LIBRARIES ; development ; LEVEL ; analysis ; NUCLEAR ; tumor antigen ; BREAST-TUMORS ; USA ; CANCERS ; SPECIMENS
    Abstract: Antibody-based cancer immunotherapy relies on the identification and characterization of target antigens and the development of potent antibodies recognizing the target. Here we report the expression analysis and molecular characterization of the differentiation antigen NY-BR-1, which we previously identified by using the SEREX (serological analysis of recombinant cDNA expression libraries) method. Corroborating methodologies, including mRNA quantitation and immunoblotting show that NY-BR-1 is strongly expressed in 〉70% of 129 breast tumors. Application of a NY-BR-1 specific antibody demonstrated NY-BR-1 expression in primary and metastastic breast cancers. In contrast, most of the breast cancer cell lines tested, expressed only low NY-BR-1 levels. Importantly, confocal microscopy revealed that ectopically expressed NY-BR-1 localizes to the cytoplasm and the cell membrane. NY-BR-1 localization in breast cancer specimens was also confirmed by immunohistochemistry. Bioinformatic analysis and deletion mutagenesis further show that NY-BR-1 membrane localization is mediated by 2 cis-active membrane targeting domains. Biochemical surface labeling and FACS analysis of live cells further characterize NY-BR-1 as a transmembrane protein, which can be specifically recognized by the anti-NY-BR-1 antibody on the surface of vital cells. The strong expression of NY-BR-1 in breast tumors, its cytoplasmic and membrane localization and accessibility to an ectopically applied antibody now suggest to pursue NY-BR-1 as a potential target for antibody-based therapies in breast cancer patients. (c) 2007 Wiley-Liss, Inc
    Type of Publication: Journal article published
    PubMed ID: 17330232
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