ArticleInternational journal of molecular sciences2021
N-Glycosylation as a Tool to Study Antithrombin Secretion, Conformation, and Function.
Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 25 citations in OpenAlex.
- Clinical and functional characterization of a novel heterozygous mutation c.473T > A (p.Leu158Gln) in the SERPINC1 gene causing recurrent arteriovenous thrombophilia.Thrombosis journal · 2025Article
- Identification of two point mutations associated with inherited antithrombin deficiency.Thrombosis journal · 2024Article
- Clinical and Molecular Characterization of Nine Novel Antithrombin Mutations.International journal of molecular sciences · 2024Article
- Scalable production of tissue-like vascularized liver organoids from human PSCs.Experimental & molecular medicine · 2023Article
- Identification and characterization of two SERPINC1 mutations causing congenital antithrombin deficiency.Thrombosis journal · 2023Article
- Active antithrombin glycoforms are selectively physiosorbed on plasma extracellular vesicles.Journal of extracellular biology · 2022Article
- Different N-Glycosylation Sites Reduce the Activity of Recombinant DSPAα2.Current issues in molecular biology · 2022Article
- The introduction of an N-glycosylation site into prochymosin greatly enhances its production and secretion by Pichia pastoris.Microbial cell factories · 2022Article
- Anticoagulant SERPINs: Endogenous Regulators of Hemostasis and Thrombosis.Frontiers in cardiovascular medicine · 2022Review
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 2 countries.
Funding
Abstract
N-linked glycosylation is a crucial post-translational modification involved in protein folding, function, and clearance. N-linked glycosylation is also used therapeutically to enhance the half-lives of many proteins. Antithrombin, a serpin with four potential N-glycosylation sites, plays a pivotal role in hemostasis, wherein its deficiency significantly increases thrombotic risk. In this study, we used the introduction of N-glycosylation sites as a tool to explore what effect this glycosylation has on the protein folding, secretion, and function of this key anticoagulant. To accomplish this task, we introduced an additional N-glycosylation sequence in each strand. Interestingly, all regions that likely fold rapidly or were surrounded by lysines were not glycosylated even though an N-glycosylation sequon was present. The new sequon in the strands of the A- and B-sheets reduced secretion, and the B-sheet was more sensitive to these changes. However, the mutations in the strands of the C-sheet allowed correct folding and secretion, which resulted in functional variants. Therefore, our study revealed crucial regions for antithrombin secretion and could potentially apply to all serpins. These results could also help us understand the functional effects of natural variants causing type-I deficiencies.
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Registered trials
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