- AutorIn
- Kathrin Oertwig
- David Ulbricht
- Stefanie Hanke
- Jan Pippel
- Kathrin Bellmann-Sickert
- Norbert Sträter
- John T. Heiker
- Titel
- Glycosylation of human vaspin (SERPINA12) and its impact on serpin activity, heparin binding and thermal stability
- Zitierfähige Url:
- https://nbn-resolving.org/urn:nbn:de:bsz:15-qucosa2-334280
- Quellenangabe
- Biochimica et Biophysica Acta (BBA) : Proteins and Proteomics
Verlag: Elsevier
Erscheinungsjahr: 2017
Jahrgang: 1865
Heft: 9
Seiten: 1188-1194
ISSN: 1570-9639 - Erstveröffentlichung
- 2017
- Abstract (EN)
- Vaspin is a glycoprotein with three predicted glycosylation sites at asparagine residues located in proximity to the reactive center loop and close to domains that play important roles in conformational changes underlying serpin function. In this study, we have investigated the glycosylation of human vaspin and its effects on biochemical properties relevant to vaspin function. We show that vaspin is modified at all three sites and biochemical data demonstrate that glycosylation does not hinder inhibition of the target protease kallikrein 7. Although binding affinity to heparin is slightly decreased, the protease inhibition reaction is still significantly accelerated in the presence of heparin. Glycosylation did not affect thermal stability.
- Andere Ausgabe
- Link zur Originalpublikatiion
Link: https://www.sciencedirect.com/science/article/pii/S1570963917301413?via%3Dihub
DOI: /10.1016/j.bbapap.2017.06.020 - Freie Schlagwörter (EN)
- Adipokine, Glycosylation, Kallikrein 7, Serine protease, Serpin, Vaspin
- Klassifikation (DDC)
- 572
- Version / Begutachtungsstatus
- angenommene Version / Postprint / Autorenversion
- URN Qucosa
- urn:nbn:de:bsz:15-qucosa2-334280
- Veröffentlichungsdatum Qucosa
- 06.03.2019
- Dokumenttyp
- Artikel
- Sprache des Dokumentes
- Englisch