SPR Biosensor Probing the Interactions between TIMP-3 and Heparin/GAGs
AuthorZhang, Fuming; Lee, Kyung Bok; Linhardt, Robert J.
SubjectBiology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
Full CitationSPR Biosensor Probing the Interactions between TIMP-3 and Heparin/GAGs, F. Zhang, K.B. Lee, R. J. Linhardt Biosensors, 5, 500-512, 2015
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AbstractTissue inhibitor of metalloproteinases-3 (TIMP-3) belongs to a family of proteins that regulate the activity of matrix metalloproteinases (MMPs), which can process various bioactive molecules such as cell surface receptors, chemokines, and cytokines. Glycosaminoglycans (GAGs) interact with a number of proteins, thereby playing an essential role in the regulation of many physiological/patho-physiological processes. Both GAGs and TIMP/MMPs play a major role in many cell biological processes, including cell proliferation, migration, differentiation, angiogenesis, apoptosis, and host defense. In this report, a heparin biosensor was used to map the interaction between TIMP-3 and heparin and other GAGs by surface plasmon resonance spectroscopy. These studies show that TIMP-3 is a heparin-binding protein with an affinity of ~59 nM. Competition surface plasmon resonance analysis indicates that the interaction between TIMP-3 and heparin is chain-length dependent, and N-sulfo and 6-O-sulfo groups (rather than the 2-O-sulfo groups) in heparin are important in the interaction of heparin with TIMP-3. Other GAGs (including chondroitin sulfate (CS) type E (CS-E)and CS type B (CS-B)demonstrated strong binding to TIMP-3, while heparan sulfate (HS), CS type A (CSA), CS type C (CSC), and CS type D (CSD) displayed only weak binding affinity.;
DescriptionBiosensors, 5, 500-512; Note : 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.
DepartmentThe Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
PublisherMultidisciplinary Digital Publishing Institute (MDPI)
RelationshipsThe Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; Biosensors; https://harc.rpi.edu/;
AccessCC BY — Creative Commons Attribution; A full text version is available in DSpace@RPI; Open Access;
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