ArticleProtein and peptide letters2025
Enhancing Tissue Factor Production: The Role of N-Glycosylation and ERAD Pathway Modulation.
Article in Protein and peptide letters, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed.
- CORT silencing impairs migration and invasion: validation of a glycosylation-based risk model (CORT/LPAR5/CEBPA/MYH10/MAGEA11) in osteosarcoma.European journal of medical research · 2026Article
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Authors and funding
5 authors.
Funding
Abstract
backgroundTissue Factor (TF) is a crucial transmembrane glycoprotein that triggers blood coagulation upon vascular or tissue injury by binding to plasma factors VII and VIIa. In recent years, the demand for TF has rapidly increased due to its pivotal role in preoperative coagulation tests. However, large-scale production of TF remains challenging despite successful recombinant expression, as incorrect post-translational modifications adversely affect TF activity.
objectiveThis study aims to investigate the role of post-translational modifications, specifically N-glycosylation, in TF activity and stability. Additionally, it explores strategies to enhance TF production by reducing its degradation through genetic modulation.
methodsWe compared TF activity derived from human cells and E. coli to assess the impact of post-translational modifications. Furthermore, we examined the effect of N-glycosylation on TF function. To address TF degradation, we knocked out the HRD1 gene, a key component of the endoplasmic- reticulum-associated degradation (ERAD) pathway, and evaluated its impact on TF stability and activity.
resultsTF produced in human cells exhibited higher activity than TF expressed in E. coli, emphasizing the importance of post-translational modifications. Specifically, N-glycosylation was found to influence TF activity and stability. Additionally, we observed that knocking out the HRD1 gene effectively reduced TF degradation without compromising its activity.
conclusionOur findings underscore the crucial role of N-glycosylation in TF function and stability. Moreover, the modulation of the ERAD pathway through knocking out HRD1 presents a promising approach for enhancing TF production. These insights could contribute to the large-scale manufacturing of functionally active TF for clinical and research applications.
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Identifiers
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.