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dc.contributor.authorQiu, Hongyan
dc.contributor.authorJin, Lan
dc.contributor.authorChen, Jian
dc.contributor.authorShi, Min
dc.contributor.authorShi, Feng
dc.contributor.authorWang, Mansen
dc.contributor.authorLi, Daoyuan
dc.contributor.authorXu, Xiaohui
dc.contributor.authorSu, Xinhuan
dc.contributor.authorYin, Xianlun
dc.contributor.authorLi, Wenhua
dc.contributor.authorZhou, Xiaoming
dc.contributor.authorLinhardt, Robert J.
dc.contributor.authorWang, Zhe
dc.contributor.authorChi, Lianli
dc.contributor.authorZhang, Qunye
dc.date2020
dc.date.accessioned2022-06-27T15:41:32Z
dc.date.available2022-06-27T15:41:32Z
dc.date.issued2020-04-01
dc.identifier.citationComprehensive glycomic analysis reveals that human serum albumin glycation specifically affects the pharmacokinetics and efficacy of different anticoagulant drugs in diabetes, H. Qiu, L. Jin, J. Chen, M. Shi, F. Shi, M. Wang, D. Li, X. Xu, X. Su, X. Yin, W. Li, X. Zhou, R. J. Linhardt, Z. Wang, L.Chi, Q. Zhang, Diabetes, 69, 760-770, 2020.
dc.identifier.issn1939327X
dc.identifier.issn121797
dc.identifier.urihttps://doi.org/10.2337/db19-0738
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5504
dc.descriptionDiabetes, 69, 760-770
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.abstractLong-term hyperglycemia in patients with diabetes leads to human serum albumin (HSA) glycation, which may impair HSA function as a transport protein and affect the therapeutic efficacy of anticoagulants in patients with diabetes. In this study, a novel mass spectrometry approach was developed to reveal the differences in the profiles of HSA glycation sites between patients with diabetes and healthy subjects. K199 was the glycation site most significantly changed in patients with diabetes, contributing to different interactions of glycated HSA and normal HSA with two types of anticoagulant drugs, heparin and warfarin. An in vitro experiment showed that the binding affinity to warfarin became stronger when HSA was glycated, while HSA binding to heparin was not significantly influenced by glycation. A pharmacokinetic study showed a decreased level of free warfarin in the plasma of diabetic rats. A preliminary retrospective clinical study also revealed that there was a statistically significant difference in the anticoagulant efficacy between patients with diabetes and patients without diabetes who had been treated with warfarin. Our work suggests that larger studies are needed to provide additional specific guidance for patients with diabetes when they are administered anticoagulant drugs or drugs for treating other chronic diseases.
dc.description.sponsorshipNational Natural Science Foundation of China
dc.languageen_US
dc.language.isoENG
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofDiabetes
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleComprehensive glycomic analysis reveals that human serum albumin glycation specifically affects the pharmacokinetics and efficacy of different anticoagulant drugs in diabetes
dc.typeArticle
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.2337/db19-0738
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)
rpi.description.pages760-770
rpi.description.volume69


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