SPR Biosensor Probing the Interactions between TIMP-3 and Heparin/GAGs
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. View Full-Text
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Zhang, F.; Lee, K.B.; Linhardt, R.J. SPR Biosensor Probing the Interactions between TIMP-3 and Heparin/GAGs. Biosensors 2015, 5, 500-512.
Zhang F, Lee KB, Linhardt RJ. SPR Biosensor Probing the Interactions between TIMP-3 and Heparin/GAGs. Biosensors. 2015; 5(3):500-512.Chicago/Turabian Style
Zhang, Fuming; Lee, Kyung B.; Linhardt, Robert J. 2015. "SPR Biosensor Probing the Interactions between TIMP-3 and Heparin/GAGs." Biosensors 5, no. 3: 500-512.