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dc.contributor.authorDimitrievska, S.
dc.contributor.authorWeyers, A.
dc.contributor.authorLin, T.
dc.contributor.authorCai, C.
dc.contributor.authorWu, W.
dc.contributor.authorTuggle, C.T.
dc.contributor.authorSundaram, S.
dc.contributor.authorBalestrini, J.L.
dc.contributor.authorSlattery, D.
dc.contributor.authorTchouta, L.
dc.contributor.authorKyriakides, T.R.
dc.contributor.authorTarbell, J.M.
dc.contributor.authorLinhardt, Robert J.
dc.contributor.authorNiklason, L.E.
dc.date2016
dc.date.accessioned2022-06-23T04:20:07Z
dc.date.available2022-06-23T04:20:07Z
dc.date.issued2016
dc.identifier.citationNew functional tools for anti-thrombogenic activity assessment of live surface glycocalyx, S. Dimitrievska, A. Weyers, T. Lin, C. Cai, W. Wu, C. T. Tuggle, S. Sundaram, J. L. Balestrini, D. Slattery, L. Tchouta, T. R. Kyriakides, J. M. Tarbell, R.J. Linhardt, L. E. Niklason, Arteriosclerosis, Thrombosis, and Vascular Biology, 36, 1847-1853, 2016.
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5345
dc.identifier.urihttps://doi.org/10.1161/ATVBAHA.116.308023
dc.descriptionArteriosclerosis, Thrombosis, and Vascular Biology, 36, 1847-1853
dc.descriptionNote : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
dc.description.abstractObjective: It is widely accepted that the presence of a glycosaminoglycan-rich glycocalyx is essential for endothelialized vasculature health; in fact, a damaged or impaired glycocalyx has been demonstrated in many vascular diseases. Currently, there are no methods that characterize glycocalyx functionality, thus limiting investigators' ability to assess the role of the glycocalyx in vascular health. Approach and results: We have developed novel, easy-to-use, in vitro assays that directly quantify live endothelialized surface's functional heparin weights and their anticoagulant capacity to inactivate Factor Xa and thrombin. Using our assays, we characterized 2 commonly used vascular models: native rat aorta and cultured human umbilical vein endothelial cell monolayer. We determined heparin contents to be ≈10 000 ng/cm(2) on the native aorta and ≈10-fold lower on cultured human umbilical vein endothelial cells. Interestingly, human umbilical vein endothelial cells demonstrated a 5-fold lower anticoagulation capacity in inactivating both Factor Xa and thrombin relative to native aortas. We verified the validity and accuracy of the novel assays developed in this work using liquid chromatography-mass spectrometry analysis. Conclusions: Our assays are of high relevance in the vascular community because they can be used to establish the antithrombogenic capacity of many different types of surfaces such as vascular grafts and transplants. This work will also advance the capacity for glycocalyx-targeting therapeutics development to treat damaged vasculatures.
dc.languageen_US
dc.language.isoENG
dc.publisherAmerican Heart Association (AHA) Journals and Wiley
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleNew functional tools for anti-thrombogenic activity assessment of live surface glycocalyx
dc.typeArticle
dcterms.accessRightsA full text version is available in DSpace@RPI
dcterms.isVersionOfhttps://doi.org/10.1161/ATVBAHA.116.308023
dc.rights.holderIn Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/
dc.creator.identifierhttps://orcid.org/0000-0003-2219-5833
dc.relation.departmentThe Linhardt Research Labs.
dc.relation.departmentThe Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)


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