Počet záznamů: 1
Protein and Site Specificity of Fucosylation in Liver-Secreted Glycoproteins
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SYSNO ASEP 0440676 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Protein and Site Specificity of Fucosylation in Liver-Secreted Glycoproteins Tvůrce(i) Pompach, Petr (MBU-M) RID, ORCID
Ashline, David J. (US)
Brnáková, Z. (US)
Benicky, J. (US)
Sanda, M. (US)
Goldman, R. (US)Celkový počet autorů 6 Zdroj.dok. Journal of Proteome Research. - : American Chemical Society - ISSN 1535-3893
Roč. 13, č. 12 (2014), s. 5561-5569Poč.str. 9 s. Jazyk dok. eng - angličtina Země vyd. US - Spojené státy americké Klíč. slova fucose ; glycoproteins ; liver ; site specificity Vědní obor RIV CE - Biochemie CEP LH13051 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy GAP206/12/0503 GA ČR - Grantová agentura ČR Institucionální podpora MBU-M - RVO:61388971 UT WOS 000346039400024 Anotace Chronic liver diseases are a serious health problem worldwide. One of the frequently reported glycan alterations in liver disease is aberrant fucosylation, which was suggested as a marker for noninvasive serologic monitoring. We present a case study that compares site specific glycoforms of four proteins including haptoglobin, complement factor H, kininogen-1, and hemopexin isolated from the same patient. Our exoglycosidase-assisted LC-MS/MS analysis confirms the high degree of fucosylation of some of the proteins but shows that microheterogeneity is protein- and site-specific. MSn analysis of permethylated detached glycans confirms the presence of LeY glycoforms on haptoglobin, which cannot be detected in hemopexin or complement factor H; all three proteins carry Lewis and H epitopes. Core fucosylation is detectable in only trace amounts in haptoglobin but with confidence on hemopexin and complement factor H, where core fucosylation of the bi-antennary glycans on select glycopeptides reaches 15-20% intensity. These protein-specific differences in fucosylation, observed in proteins isolated from the same patient source, suggest that factors other than up-regulation of enzymatic activity regulate the microheterogeneity of glycoforms. This has implications for selection of candidate proteins for disease monitoring and suggests that site-specific glycoforms have structural determinants, which could lead to functional consequences for specific subsets of proteins or their domains. Pracoviště Mikrobiologický ústav Kontakt Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Rok sběru 2015
Počet záznamů: 1