N- and O -glycosylation Analysis of Human C1-inhibitor Reveals Extensive Mucin-type O-Glycosylation
Yazarlar (9)
Kathrin Stavenhagen Leids Universitair Medisch Centrum, Hollanda
Doç. Dr. Hacı Mehmet KAYILI Karabük Üniversitesi, Türkiye
Stephanie Holst
Leids Universitair Medisch Centrum, Hollanda
Leids Universitair Medisch Centrum, Hollanda
Carolien A.M. Koeleman
Leids Universitair Medisch Centrum, Hollanda
Leids Universitair Medisch Centrum, Hollanda
Ruchira Engel
Sanquin Research, Hollanda
Sanquin Research, Hollanda
Diana Wouters
Sanquin Research, Hollanda
Sanquin Research, Hollanda
Sacha Zeerleder
Sanquin Research, Hollanda
Sanquin Research, Hollanda
Prof. Dr. Bekir Salih Hacettepe Üniversitesi, Türkiye
Manfred Wuhrer Leids Universitair Medisch Centrum, Hollanda
| Makale Türü |
Özgün Makale
(SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale)
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| Dergi Adı | Molecular and Cellular Proteomics (Q1) | ||
| Dergi ISSN | 1535-9476 Dergi Bilgileri (2018) | ||
| Dergi Tarandığı Indeksler | SCI | ||
| Makale Dili | İngilizce | Basım Tarihi | 06-2018 |
| Kabul Tarihi | – | Yayınlanma Tarihi | 01-06-2018 |
| Cilt / Sayı / Sayfa | 17 / 6 / 1225–1238 | DOI | 10.1074/mcp.RA117.000240 |
| Makale Linki | http://www.mcponline.org/lookup/doi/10.1074/mcp.RA117.000240 | ||
| UAK Araştırma Alanları |
Analitik Kimya
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| Özet |
| Human C1-inhibitor (C1-Inh) is a serine protease inhibitor and the major regulator of the contact activation pathway as well as the classical and lectin complement pathways. It is known to be a highly glycosylated plasma glycoprotein. However, both the structural features and biological role of C1-Inh glycosylation are largely unknown. Here, we performed for the first time an in-depth site-specific N- and O-glycosylation analysis of C1-Inh combining various mass spectrometric approaches, including C18-porous graphitized carbon (PGC)-LC-ESI-QTOF-MS/MS applying stepping-energy collision-induced dissociation (CID) and electron-transfer dissociation (ETD). Various proteases were applied, partly in combination with PNGase F and exoglycosidase treatment, in order to analyze the (glyco)peptides. The analysis revealed an extensively O-glycosylated N-terminal region. Five novel and five known O-glycosylation … |
| Anahtar Kelimeler |
| Glycoproteomics | Plasma or serum analysis | Post-translational modifications* | Mass Spectrometry | Glycomics | Glycoproteins* | Complement system | O-glycosylation |
BM Sürdürülebilir Kalkınma Amaçları
| Atıf Sayıları | |
| Web of Science | 54 |
| Scopus | 59 |
| Google Scholar | 76 |