Further insight into the roles of the glycans attached to human blood protein C inhibitor

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Protein C inhibitor (PCI) is a 57-kDa glycoprotein that exists in many tissues and secretions in human. As a member of the serpin superfamily of proteins it displays unusually broad protease specificity. PCI is implicated in the regulation of a wide range of processes, including blood coagulation, fertilization, prevention of tumors and pathogen defence. It has been reported that PCI isolated from human blood plasma is highly heterogeneous, and that this heterogeneity is caused by differences in N-glycan structures, N-glycosylation occupancy, and the presence of two forms that differ by the presence or absence of 6 amino acids at the amino-terminus. In this study we have verified that such heterogeneity exists in PCI purified from single individuals, and that individuals of two different ethnicities possess a similar PCI pattern, verifying that the micro-heterogeneity is conserved among humans. Furthermore, we have provided experimental evidence that PCI in both individuals is O-glycosylated on Thr20 with a core type 1 O-glycan, which is mostly NeuAcGalGalNAc. Modeling suggested that the O-glycan attachment site is located in proximity to several ligand-binding sites of the inhibitor. (C) 2010 Elsevier Inc. All rights reserved.


  • Wei Sun
  • Simon Parry
  • Wimal Ubhayasekera
  • Ake Engstrom
  • Anne Dell
  • Sophia Schedin-Weiss
Enheter & grupper

Ämnesklassifikation (UKÄ) – OBLIGATORISK

  • Biologiska vetenskaper


Sidor (från-till)198-202
TidskriftBiochemical and Biophysical Research Communications
StatusPublished - 2010
Peer review utfördJa