Institute of Biochemistry, Faculty of Biosciences, Pharmacy and Psychology, University of Leipzig, 04103 Leipzig, Germany.
Institute of Bioanalytical Chemistry, Center for Biotechnology and Biomedicine, University of Leipzig, 04103 Leipzig, Germany.
Biochim Biophys Acta Proteins Proteom. 2017 Sep;1865(9):1188-1194. doi: 10.1016/j.bbapap.2017.06.020. Epub 2017 Jun 29.
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.
Vaspin 是一种糖蛋白，在靠近反应中心环的天冬酰胺残基处有三个预测的糖基化位点，接近在丝氨酸蛋白酶抑制剂功能所必需的构象变化中起重要作用的结构域。在这项研究中，我们研究了人 vaspin 的糖基化及其对与 vaspin 功能相关的生化特性的影响。我们表明 vaspin 在所有三个位点都被修饰，生化数据表明糖基化不会阻碍靶蛋白酶激肽释放酶 7 的抑制。尽管与肝素的结合亲和力略有降低，但在肝素存在的情况下，蛋白酶抑制反应仍然显著加速。糖基化不影响热稳定性。
