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001-es BibID:	BIBFORM115154
035-os BibID:	(cikkazonosító)4845 (Scopus)85112582716 (WOS)000689890600001
Első szerző:	Járvás Gábor (vegyészmérnök)
Cím:	Modification of Hemodialysis Membranes for Efficient Circulating Tumor Cell Capture for Cancer Therapy / Jarvas Gabor, Szerenyi Dora, Tovari Jozsef, Takacs Laszlo, Guttman Andras
Dátum:	2021
ISSN:	1420-3049
Megjegyzések:	It is well known that more than 90% of cancer deaths are due to metastases. However, the entire tumorigenesis process is not fully understood, and it is evident that cells spreading from the primary tumor play a key role in initiating the metastatic process. Tumor proliferation and invasion also elevate the concentration of regular and irregular metabolites in the serum, which may alter the normal function of the entire human homeostasis and possibly causes cancer metabolism syndrome, also referred to as cachexia. Methods: We report on the modification of commercially available hemodialysis membranes to selectively capture circulating tumor cells from the blood stream by means of immobilized human anti?EpCAM antibodies on the inner surface of the fibers. All critical steps are described that required in situ addition of the immuno?affinity feature to hemodialyzer cartridges in order to capture EpCAM positive circulating tumor cells, which represents ~80% of cancer cell types. Results: The cell capture efficiency of the suggested technology was demonstrated by spiking HCT116 cancer cells both into buffer solution and whole blood and run through on the modified cartridge. Flow cytometry was used to quantitatively evaluate the cell clearance performance of the approach. Conclusions: The suggested modification has no significant effect on the porous structure of the hemodialysis membranes; it keeps its cytokine removal capability, addressing cachexia simultaneously with CTC removal.
Tárgyszavak:	Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Capture Circulating tumor cell Hemodialysis Therapy
Megjelenés:	Molecules. - 26 : 16 (2021), p. 1-11. -
További szerzők:	Szerényi Dóra Tóvári József Takács László (1955-) (orvos) Guttman András (1954-) (vegyészmérnök)
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM106825
035-os BibID:	(cikkazonosító)8192 (scopus)85143597041 (wos)000896340300001
Első szerző:	Torok Rebeka
Cím:	The Effect of Sample Glucose Content on PNGase F-Mediated N-Glycan Release Analyzed by Capillary Electrophoresis / Torok Rebeka, Auer Felicia, Farsang Robert, Jona Eszter, Jarvas Gabor, Guttman Andras
Dátum:	2022
ISSN:	1420-3049
Megjegyzések:	Protein therapeutics have recently gained high importance in general health care along with applied clinical research. Therefore, it is important to understand the structure?function relationship of these new generation drugs. Asparagine-bound carbohydrates represent an important critical quality attribute of therapeutic glycoproteins, reportedly impacting the efficacy, immunogenicity, clearance rate, stability, solubility, pharmacokinetics and mode of action of the product. In most instances, these linked N-glycans are analyzed in their unconjugated form after endoglycosidase-mediated release, e.g., PNGase F-mediated liberation. In this paper, first, N-glycan release kinetics were evaluated using our previously reported in-house produced 6His-PNGase F enzyme. The resulting deglycosylation products were quantified by sodium dodecyl sulfate capillary gel electrophoresis to determine the optimal digestion time. Next, the effect of sample glucose content was investigated as a potential endoglycosidase activity modifier. A comparative Michaelis-Menten kinetics study was performed between the 6His-PNGase F and a frequently employed commercial PNGase F product with and without the presence of glucose in the digestion reaction mixture. It was found that 1 mg/mL glucose in the sample activated the 6His-PNGase F enzyme, while did not affect the release efficiency of the commercial PNGase F. Capillary isoelectric focusing revealed subtle charge heterogeneity differences between the two endoglycosidases, manifested by the lack of extra acidic charge variants in the cIEF trace of the 6His-PNGase F enzyme, which might have possibly influenced the glucose-mediated enzyme activity differences.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk
Megjelenés:	Molecules. - 27 : 23 (2022), p. 1-8. -
További szerzők:	Auer, Felicia Farsang Róbert Jóna Eszter Járvás Gábor (1982-) (vegyészmérnök) Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:	UNKP-22-3-I Egyéb
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM099697
035-os BibID:	(cikkazonosító)6399 (WoS)000718435900001 (Scopus)85117579488
Első szerző:	Török Rebeka
Cím:	N-Glycosylation Profiling of Human Blood in Type 2 Diabetes by Capillary Electrophoresis : a Preliminary Study / Torok Rebeka, Horompoly Klaudia, Szigeti Marton, Guttman Andras, Vitai Marta, Koranyi Laszlo, Jarvas Gabor
Dátum:	2021
ISSN:	1420-3049
Megjegyzések:	Currently, diagnosing type 2 diabetes (T2D) is a great challenge. Thus, there is a need to find rapid, simple, and reliable analytical methods that can detect the disease at an early stage. The aim of this work was to shed light on the importance of sample collection options, sample preparation conditions, and the applied capillary electrophoresis bioanalytical technique, for a highresolution determination of the N-glycan profile in human blood samples of patients with type 2 diabetes (T2D). To achieve the profile information of these complex oligosaccharides, linked by asparagine to hIgG in the blood, the glycoproteins of the samples needed to be cleaved, labelled, and purified with sufficient yield and selectivity. The resulting samples were analyzed by capillary electrophoresis, with laser-induced fluorescence detection. After separation parameter optimization, the capillary electrophoresis technique was implemented for efficient N-glycan profiling of whole blood samples from the diabetic patients. Our results revealed that there were subtle differences between the N-glycan profiles of the diabetic and control samples; in particular, two N-glycan structures were identified as potential glycobiomarkers that could reveal significant changes between the untreated/treated type 2 diabetic and control samples. By analyzing the resulting oligosaccharide profiles, clinically relevant information was obtained, revealing the differences between the untreated and HMG-CoA reductase-inhibitor-treated diabetic patients on changes in the N-glycan profile in the blood. In addition, the information from specific IgG N-glycosylation profiles in T2D could shed light on underlying inflammatory pathophysiological processes and lead to drug targets.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk N-glycan type 2 diabetes capillary electrophoresis biomarker blood collecting tubes
Megjelenés:	Molecules. - 26 : 21 (2021), p. 1-11. -
További szerzők:	Horompoly Klaudia Szigeti Márton (1986-) (környezetmérnök) Guttman András (1954-) (vegyészmérnök) Vitai Márta (1961-) (okleveles vegyész) Korányi László Járvás Gábor (1982-) (vegyészmérnök)
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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