2. Academic Validation
  3. Glycosylation of human vaspin (SERPINA12) and its impact on serpin activity, heparin binding and thermal stability

Glycosylation of human vaspin (SERPINA12) and its impact on serpin activity, heparin binding and thermal stability

  • Biochim Biophys Acta Proteins Proteom. 2017 Sep;1865(9):1188-1194. doi: 10.1016/j.bbapap.2017.06.020.
Kathrin Oertwig 1,  David Ulbricht 1,  Stefanie Hanke 2,  Jan Pippel 2,  Kathrin Bellmann-Sickert 1,  Norbert Sträter 2,  John T Heiker 3
Affiliations

Affiliations

  • 1 Institute of Biochemistry, Faculty of Biosciences, Pharmacy and Psychology, University of Leipzig, 04103 Leipzig, Germany.
  • 2 Institute of Bioanalytical Chemistry, Center for Biotechnology and Biomedicine, University of Leipzig, 04103 Leipzig, Germany.
  • 3 Institute of Biochemistry, Faculty of Biosciences, Pharmacy and Psychology, University of Leipzig, 04103 Leipzig, Germany. Electronic address: [email protected].
PMID: 28668641 DOI: 10.1016/j.bbapap.2017.06.020
Abstract

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.

Keywords

Adipokine; Glycosylation; Kallikrein 7; Serine protease; Serpin; Vaspin.

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