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master's thesis
Strukturna analiza N-glikanskog profila staničnih linija HepG2 i 1.1B4 HILIC-UPLC-FLR-MS/MS metodom
Zagreb: University of Zagreb, Faculty of Pharmacy and Biochemistry, 2019. urn:nbn:hr:163:744165
Šoić, Dinko
University of Zagreb
Faculty of Pharmacy and Biochemistry
Department of biochemistry and molecular biology

Institutional repository: Repository of Faculty of Pharmacy and Biochemistry University of Zagreb

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Šoić, D. (2019). Strukturna analiza N-glikanskog profila staničnih linija HepG2 i 1.1B4 HILIC-UPLC-FLR-MS/MS metodom (Master's thesis). Zagreb: University of Zagreb, Faculty of Pharmacy and Biochemistry. Retrieved from https://urn.nsk.hr/urn:nbn:hr:163:744165

Šoić, Dinko. "Strukturna analiza N-glikanskog profila staničnih linija HepG2 i 1.1B4 HILIC-UPLC-FLR-MS/MS metodom." Master's thesis, University of Zagreb, Faculty of Pharmacy and Biochemistry, 2019. https://urn.nsk.hr/urn:nbn:hr:163:744165

Šoić, Dinko. "Strukturna analiza N-glikanskog profila staničnih linija HepG2 i 1.1B4 HILIC-UPLC-FLR-MS/MS metodom." Master's thesis, University of Zagreb, Faculty of Pharmacy and Biochemistry, 2019. https://urn.nsk.hr/urn:nbn:hr:163:744165

Šoić, D. (2019). 'Strukturna analiza N-glikanskog profila staničnih linija HepG2 i 1.1B4 HILIC-UPLC-FLR-MS/MS metodom', Master's thesis, University of Zagreb, Faculty of Pharmacy and Biochemistry, accessed 25 November 2024, https://urn.nsk.hr/urn:nbn:hr:163:744165

Šoić D. Strukturna analiza N-glikanskog profila staničnih linija HepG2 i 1.1B4 HILIC-UPLC-FLR-MS/MS metodom [Master's thesis]. Zagreb: University of Zagreb, Faculty of Pharmacy and Biochemistry; 2019 [cited 2024 November 25] Available at: https://urn.nsk.hr/urn:nbn:hr:163:744165

D. Šoić, "Strukturna analiza N-glikanskog profila staničnih linija HepG2 i 1.1B4 HILIC-UPLC-FLR-MS/MS metodom", Master's thesis, University of Zagreb, Faculty of Pharmacy and Biochemistry, Zagreb, 2019. Available at: https://urn.nsk.hr/urn:nbn:hr:163:744165

Metadata
TitleStrukturna analiza N-glikanskog profila staničnih linija HepG2 i 1.1B4 HILIC-UPLC-FLR-MS/MS metodom
Title (english)Structural analysis of N-glycane profile in HepG2 and 1.1B4 cell lines using HILIC-UPLC-FLR-MS/MS method
AuthorDinko Šoić
MentorToma Keser (mentor)
Committee memberToma Keser (predsjednik povjerenstva)
Committee memberBiljana Nigović (član povjerenstva)
Committee memberTamara Pavić (član povjerenstva)
GranterUniversity of Zagreb
Faculty of Pharmacy and Biochemistry
(Department of biochemistry and molecular biology)
Zagreb
Defense date and country2019-05-29, Croatia
Scientific / art field,
discipline and subdiscipline		BIOMEDICINE AND HEALTHCARE
Pharmacy
Pharmacy
Abstract
Glikozilacija je najčešća i najkompleksnija modifikacija proteina te kao takva ima presudnu ulogu na konačna svojstva i funkcije glikoproteina. Budući da se sinteza glikana ne odvija po predlošku već je izrazito osjetljiva na okolišne uvjete i patofiziološke procese, dijagnostički potencijal glikana sve se više istražuje. Zbog velike potrebe za jednostavnošću i lakoćom manipuliranja, kao modeli u biomedicinskim istraživanjima naširoko se koriste stanične linije. Detaljna karakterizacija njihovog glikanskog profila izrazito je važna za utvrđivanje uspješnosti korištenog modela u glikomskim istraživanjima. U ovom su radu analizirani N-glikani staničnih linija HepG2 i 1.1B4 HILIC-UPLC-FLR-MS/MS metodom. Rezultati rada prikazani su asigniranim FLR kromatogramima i tablicama sa strukturnim prikazom glikanskih pikova. U staničnoj liniji HepG2 utvrđena su 47 glikanska pika, odnosno njih 46 u liniji 1.1B4. Glikanski profili staničnih linija uvelike su se preklapali, uz nekoliko karakterističnih struktura za svaku liniju. Iako je većina struktura pripadala kompleksnom tipu, najintenzivniji pikovi sadržavali su oligomanozni tip glikana. Dobiveni glikanski profili razlikuju se od onih plazmatskih upravo po velikom udjelu oligomanoznog tipa N-vezanih glikana, kao i po prisutnosti paucimanoznih struktura.
Abstract (english)
Glycosylation is the most common and complex modification of proteins and as such has a key role in shaping the final properties and functions of glycoproteins. Since glycan synthesis is not template-driven, but is instead strongly affected by environmental factors and pathophysiological processes, the diagnostic potential of glycans is being thoroughly researched. Due to the strong need for simplicity and ease of manipulation, cell lines are widely used as models in biomedicinal research. Detailed characterization of their glycane profile is extremely important for determining the success of the model used in glycome research. This thesis analyzed N-glycans of HepG2 and 1.1B4 cell lines using HILIC-UPLC-FLR-MS/MS method. The results are presented as assigned FLR chromatograms and tables with the structural representation of the glycan peaks. In the HepG2 cell line there were 47 glycane peaks determined, while in the 1.1B4 line there were 46 peaks respectively. The glycan profiles of the cell lines vastly overlapped, with several characteristic structures for each line. Although most structures belonged to a complex type, the most intense peaks contained a high-mannose type of glycans. The obtained glycane profiles differ from those of the plasma precisely due to the large proportion of high-mannose type of N-linked glycans, as well as the presence of the paucimannose structures.
Keywords
Keywords (english)
Languagecroatian
URN:NBNurn:nbn:hr:163:744165
Study programmeTitle: Pharmacy
Study programme type: university
Study level: integrated undergraduate and graduate
Academic / professional title: magistar/magistra farmacije (magistar/magistra farmacije)
Type of resourceText
File originBorn digital
Access conditionsOpen access
Terms of useLicence In copyright icon
Created on2020-02-24 10:37:31