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1

Center for Biotechnology and Interdisciplinary Studies, Department of Chemical and Biological Engineering, Rensselaer Polytechnic Institute, Troy, NY 12180, USA

2

Department of Biochemistry, College of Medicine, Konyang University, Konyang Hospital, Daejeon 302-718, Korea

3

Center for Biotechnology and Interdisciplinary Studies, Department of Chemistry and Chemical Biology, Rensselaer Polytechnic Institute, Troy, NY 12180, USA

4

Departments of Biomedical Engineering, and Biological Sciences, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USA





*

Authors to whom correspondence should be addressed.



Academic Editors: Nicole Jaffrezic-Renault and Carole Chaix

Abstract Tissue 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-Eand CS type B CS-Bdemonstrated 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

Keywords: heparin; glycosaminoglycans; TIMP-3; binding; surface plasmon resonance heparin; glycosaminoglycans; TIMP-3; binding; surface plasmon resonance





Autor: Fuming Zhang 1,* , Kyung Bok Lee 2 and Robert J. Linhardt 1,3,4,*

Fuente: http://mdpi.com/



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