Regulation Activity of Heparin in Complement System

Authors
Yu, H.
Edens, R.E.
Linhardt H.Yu, R.J.
Edens, R.E.
Linhardt, Robert J.
ORCID
https://orcid.org/0000-0003-2219-5833
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Other Contributors
Issue Date
2005
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
Degree
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Full Citation
Regulation Activity of Heparin in Complement System H.Yu, R.E. Edens, R. J. Linhardt, inin the Chemistry and Biology of Heparin and Heparan Sulfate, Elsevier Ltd., Oxford, H. G. Garg, R. J. Linhardt, and C. A. Hales (Eds.), Chapter 11, pp.313-343, 2005.
Abstract
Heparin (HP) can bind to a variety of proteins, including growth factors, pro-inflammatory chemokines and cytokines, extracellular matrix proteins, and complement proteins. HP has a variety of biological activities, many of which are of interest because of their potential therapeutic utility. By regulating the activity of HP-binding proteins, HP and the related glycosaminoglycan (GAG), heparan sulfate (HS), can influence various biological processes giving HP therapeutic applications as an antithrombotic, antiatherosclerotic, anticomplement, antiinfective, anticancer, and anti-inflammatory agent. Monosaccharide and disaccharides with structural similarities to dextran did not cause a detectable decrease in C3b-factor H binding, while sugar polymers caused large decreases in the affinity between C3b and factor H as a result of the polysaccharide occupying the binding site in C3b or in factor H, preventing their interaction. HP and the structurally similar HS regulate multiple steps in the complement system including ones in both the classical and alternative pathways. Quantitative data in the form of association rates, dissociation rates, and affinity constants for complex formation are provided for many of these interactions.
Description
in the Chemistry and Biology of Heparin and Heparan Sulfate, Elsevier Ltd., Oxford, H. G. Garg, R. J. Linhardt, and C. A. Hales (Eds.), Chapter 11, pp.313-343
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.
Department
The Linhardt Research Labs.
The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
Publisher
Relationships
The Linhardt Research Labs Online Collection
Rensselaer Polytechnic Institute, Troy, NY
https://harc.rpi.edu/
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