Further insight into the roles of the glycans attached to human blood protein C inhibitor
(2010) In Biochemical and Biophysical Research Communications 403(2). p.198-202- Abstract
- 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... (More)
- 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1831246
- author
- Sun, Wei ; Parry, Simon ; Ubhayasekera, Wimal LU ; Engstrom, Ake ; Dell, Anne and Schedin-Weiss, Sophia
- organization
- publishing date
- 2010
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Micro-heterogeneity, Mass spectrometry, O-glycosylation, Protein C, inhibitor, Serpin
- in
- Biochemical and Biophysical Research Communications
- volume
- 403
- issue
- 2
- pages
- 198 - 202
- publisher
- Elsevier
- external identifiers
-
- wos:000285534500008
- scopus:78649907006
- ISSN
- 1090-2104
- DOI
- 10.1016/j.bbrc.2010.11.005
- language
- English
- LU publication?
- yes
- id
- c429e75c-7988-4fff-9be2-62700a660d05 (old id 1831246)
- date added to LUP
- 2016-04-01 15:04:31
- date last changed
- 2022-01-28 03:59:39
@article{c429e75c-7988-4fff-9be2-62700a660d05,
abstract = {{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.}},
author = {{Sun, Wei and Parry, Simon and Ubhayasekera, Wimal and Engstrom, Ake and Dell, Anne and Schedin-Weiss, Sophia}},
issn = {{1090-2104}},
keywords = {{Micro-heterogeneity; Mass spectrometry; O-glycosylation; Protein C; inhibitor; Serpin}},
language = {{eng}},
number = {{2}},
pages = {{198--202}},
publisher = {{Elsevier}},
series = {{Biochemical and Biophysical Research Communications}},
title = {{Further insight into the roles of the glycans attached to human blood protein C inhibitor}},
url = {{http://dx.doi.org/10.1016/j.bbrc.2010.11.005}},
doi = {{10.1016/j.bbrc.2010.11.005}},
volume = {{403}},
year = {{2010}},
}