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001-es BibID:	BIBFORM023718
035-os BibID:	(cikkazonosító)M111.010298 (WoS)000298290300017 (Scopus)83055168546
Első szerző:	Guergova-Kuras, Mariana
Cím:	Discovery of lung cancer biomarkers by profiling the plasma proteome with monoclonal antibody libraries / Mariana Guergova-Kuras, István Kurucz, William Hempel, Nadege Tardieu, János Kádas, Carole Malderez-Bloes, Anne Jullien, Yann Kieffer, Marina Hincapie, András Guttman, Eszter Csánky, Balázs Dezső, Barry L. Karger, László Takács
Dátum:	2011
ISSN:	1535-9476 1535-9484
Megjegyzések:	A challenge in the treatment of lung cancer is the lack of early diagnostics. Here, we describe the application of monoclonal antibody (mAb) proteomics for discovery of a panel of biomarkers for early detection (stage I) of non small cell lung cancer (NSCLC). We produced large monoclonal antibody libraries directed against the natural form of protein antigens present in the plasma of NSCLC patients. Plasma biomarkers associated with the presence of lung cancer were detected via high throughput ELISA. Differential profiling of plasma proteomes of four clinical cohorts, totalling 301 patients with lung cancer and 235 healthy controls, identified 13 lung cancer associated (p<0.05) monoclonal antibodies. The mAbs recognize five different cognate proteins identified using immunoprecipitation followed by mass spectrometry. Four of the five antigens were present in non-small cell lung cancer cells in-situ. The approach is capable of generating independent antibodies against different epitopes of the same proteins, allowing fast translation to multiplexed sandwich assays. Based on these results, we have verified in two independent clinical collections a panel of five biomarkers for classifying patient disease status with a diagnostics performance of 77% sensitivity and 87% specificity. Combining CYFRA, an established cancer marker, with the panel resulted in a performance of 83 % sensitivity at 95 % specificity for stage I NSCLC.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk
Megjelenés:	Molecular and Cellular Proteomics. - 10 : 12 (2011), p. 1-14. -
További szerzők:	Kurucz István Hempel, William Tardieu, Nadège Kádas János (1976-) (molekuláris biológus, biokémikus, kertészmérnök) Malderez-Bloes, Carole Jullien, Anne Kieffer, Yann Hincapie, Marina Guttman András (1954-) (vegyészmérnök) Csánky Eszter (1959-) (tüdőgyógyász, klinikai immunológus, allergológus) Karger, Barry Takács László (1955-) Dezső Balázs (1951-) (pathológus)
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat DOI
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001-es BibID:	BIBFORM069265
Első szerző:	Wang, Dongdong
Cím:	Antigen Identification and Characterization of Lung Cancer Specific Monoclonal Antibodies Produced by mAb Proteomics / Wang Dongdong, Hincapie Marina, Guergova-Kuras Mariana, Kadas Janos, Takacs Laszlo, Karger Barry L.
Dátum:	2010
ISSN:	1535-3893
Megjegyzések:	A mass spectrometric (MS)-based strategy for antigen (Ag) identification and characterization of globallyproduced monoclonal antibodies (mAbs) is described. Mice were immunized with a mixture of nativeglycoproteins, isolated from the pooled plasma of patients with nonsmall cell lung cancer (NSCLC), togenerate a library of IgG-secreting hybridomas. Prior to immunization, the pooled NSCLC plasma wassubjected to 3-sequential steps of affinity fractionation, including high abundant plasma proteindepletion, glycoprotein enrichment, and polyclonal antibody affinity chromatography normalization.In this paper, to demonstrate the high quality of the globally produced mAbs, we selected 3 mAbs ofhigh differentiating power against a matched, pooled normal plasma sample. After production of largequantities of the mAbs from ascites fluids, Ag identification was achieved by immunoaffinity purification,SDS-PAGE, Western blotting, and MS analysis of in-gel digest products. One antigen was found to becomplement factor H, and the other two were mapped to different subunits of haptoglobin (Hpt). The2 Hpt mAbs were characterized in detail to assess the quality of the mAbs produced by the globalstrategy. The affinity of one of the mAbs to the Hpt native tetramer form was found to have a KD ofroughly 10-9 M and to be 2 orders of magnitude lower than the reduced form, demonstrating thepower of the mAb proteomics technology in generating mAbs to the natural form of the proteinsin blood. The binding of this mAb to the -chain of haptoglobin was also dependent on glycosylationon this chain. The characterization of mAbs in this work reveals that the global mAb proteomicsprocess can generate high-quality lung cancer specific mAbs capable of recognizing proteins intheir native state.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban monoclonal antibody mAb proteomics antibody characterization glycoprotein haptoglobin conformational epitope lung cancer
Megjelenés:	Journal Of Proteome Research. - 9 : 4 (2010), p. 1834-1842. -
További szerzők:	Hincapie, Marina Guergova-Kuras, Mariana Kádas János (1976-) (molekuláris biológus, biokémikus, kertészmérnök) Takács László (1955-) Karger, Barry
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