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N-Glycosylation as a Tool to Study Antithrombin Secretion, Conformation, and Function.

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dc.contributor.authorÁguila Martínez, Sonia
dc.contributor.authorNoto, Rosina
dc.contributor.authorLuengo-Gil, Ginés
dc.contributor.authorEspín, Salvador
dc.contributor.authorBohdan, Nataliya
dc.contributor.authorMorena Barrio, María Eugenia de la
dc.contributor.authorPeñas, Julia
dc.contributor.authorRodenas, Maria Carmen
dc.contributor.authorVicente García, Vicente
dc.contributor.authorCorral de la Calle, Javier
dc.contributor.authorManno, Mauro
dc.contributor.authorMartínez-Martínez, Irene
dc.contributor.departmentMedicina Interna
dc.date.accessioned2026-02-16T09:59:27Z
dc.date.available2026-02-16T09:59:27Z
dc.date.copyright© 2021 by the authors
dc.date.issued2021-06-06
dc.description.abstractN-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 Nglycosylation 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.
dc.formatapplication/pdf
dc.format.extent12
dc.identifier.citationÁguila, S.; Noto, R.;Luengo-Gil, G.; Espín, S.; Bohdan, N.; de la Morena-Barrio, M.E.; Peñas, J.; Rodenas, M.C.; Vicente, V.; Corral, J.; et al. N-Glycosylation as a Tool to Study Antithrombin Secretion, Conformation, and Function. Int. J. Mol. Sci. 2021, 22, 516.
dc.identifier.doihttps://doi.org/10.3390/ijms22020516
dc.identifier.eissn1422-0067
dc.identifier.issn1661-6596
dc.identifier.urihttp://hdl.handle.net/10201/205222
dc.languageeng
dc.publisherMDPI
dc.relationThis research was funded by Instituto de Salud Carlos III, grant numbers PI17/00050 & FEDER and PI18/00598 & FEDER, and Fundación Séneca, grant number 19873/GERM/15.
dc.relation.publisherversionhttps://www.mdpi.com/1422-0067/22/2/516
dc.rightsAttribution 4.0 International*
dc.rights.accessRightsinfo:eu-repo/semantics/openAccess
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subjectGlycosylation
dc.subjectFolding
dc.subjectAntithrombin
dc.subjectThrombosis
dc.subjectBioengineering
dc.subjectSerpin
dc.subjectCoagulation
dc.subject.odsObjetivo 3: Salud
dc.titleN-Glycosylation as a Tool to Study Antithrombin Secretion, Conformation, and Function.
dc.typeinfo:eu-repo/semantics/article
dc.type.versioninfo:eu-repo/semantics/publishedVersion
dspace.entity.typePublicationes
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relation.isAuthorOfPublication.latestForDiscovery49779dfb-f4b4-4013-9b03-2ad7e3c247b7
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