WordNet

executed with proper legal authority; "a binding contract"
the protective covering on the front, back, and spine of a book; "the book had a leather binding" (同)book binding, cover, back
strip sewn over or along an edge for reinforcement or decoration
the capacity to attract and hold something
a polysaccharide produced in basophils (especially in the lung and liver) and that inhibits the activity of thrombin in coagulation of the blood; it (trade names Lipo-Hepin and Liquaemin) is used as an anticoagulant in the treatment of thrombosis and in heart surgery (同)Lipo-Hepin, Liquaemin
convert into a sulfate
a salt or ester of sulphuric acid (同)sulphate
any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"

PrepTutorEJDIC

義務的な,拘束力ある / 〈U〉しばること;〈C〉しばる物 / 〈C〉製本,装丁 / 〈U〉縁(‘ふち')取り材料
ヘバリン(肝臓などにあり血液の凝固を防ぐ物質)
蛋白(たんばく)質

UpToDate Contents

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1. 止血の概要 overview of hemostasis
2. ヘパリン起因性血小板減少症 heparin induced thrombocytopenia
3. ヘパリンおよび低分子ヘパリンの治療使用 therapeutic use of heparin and low molecular weight heparin
4. 血管内皮機能および血栓溶解療法の基本的メカニズム vascular endothelial function and fundamental mechanisms of fibrinolysis thrombolysis
5. 抗リン脂質抗体症候群の病因 pathogenesis of the antiphospholipid syndrome

English Journal

Mapping of heparin/heparan sulfate binding sites on αvβ3 integrin by molecular docking.

Ballut L, Sapay N, Chautard E, Imberty A, Ricard-Blum S.Author information UMR 5086 CNRS-Université Lyon 1, Institut de Biologie et Chimie des Protéines, 7 passage du Vercors, 69367 Lyon Cedex 07, France.AbstractHeparin/heparan sulfate interact with growth factors, chemokines, extracellular proteins, and receptors. Integrins are αβ heterodimers that serve as receptors for extracellular proteins, regulate cell behavior, and participate in extracellular matrix assembly. Heparin binds to RGD-dependent integrins (αIIbβ3, α5β1, αvβ3, and αvβ5) and to RGD-independent integrins (α4β1, αXβ2, and αMβ2), but their binding sites have not been located on integrins. We report the mapping of heparin binding sites on the ectodomain of αvβ3 integrin by molecular modeling. The surface of the ectodomain was scanned with small rigid probes mimicking the sulfated domains of heparan sulfate. Docking results were clustered into binding spots. The best results were selected for further docking simulations with heparin hexasaccharide. Six potential binding spots containing lysine and/or arginine residues were identified on the ectodomain of αvβ3 integrin. Heparin would mostly bind to the top of the genu domain, the Calf-I domain of the α subunit, and the top of the β subunit of RGD-dependent integrins. Three spots were close enough from each other on the integrin surface to form an extended binding site that could interact with heparin/heparan sulfate chains. Because heparin does not bind to the same integrin site as protein ligands, no steric hindrance prevents the formation of ternary complexes comprising the integrin, its protein ligand, and heparin/heparan sulfate. The basic amino acid residues predicted to interact with heparin are conserved in the sequences of RGD-dependent but not of RGD-independent integrins suggesting that heparin/heparan sulfate could bind to different sites on these two integrin subfamilies.
Journal of molecular recognition : JMR.J Mol Recognit.2013 Feb;26(2):76-85. doi: 10.1002/jmr.2250.
Heparin/heparan sulfate interact with growth factors, chemokines, extracellular proteins, and receptors. Integrins are αβ heterodimers that serve as receptors for extracellular proteins, regulate cell behavior, and participate in extracellular matrix assembly. Heparin binds to RGD-dependent integr
PMID 23334915

Biophysical characterization of glycosaminoglycan-IL-7 interactions using SPR.

Zhang F, Liang X, Pu D, George KI, Holland PJ, Walsh ST, Linhardt RJ.Author information Department of Chemical and Biological Engineering, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USA. zhangf2@rpi.eduAbstractGlycosaminoglycans (GAGs) interact with a number of cytokines and growth factors thereby playing an essential role in the regulation of many physiological processes. These interactions are important for both normal signal transduction and the regulation of the tissue distribution of cytokines/growth factors. In the present study, we employed surface plasmon resonance (SPR) spectroscopy to dissect the binding interactions between GAGs and murine and human forms of interleukin-7 (IL-7). SPR results revealed that heparin binds with higher affinity to human IL-7 than murine IL-7 through a different kinetic mechanism. The optimal oligosaccharide length of heparin for the interactions to human and murine IL-7 involves a sequence larger than a tetrasaccharide. These results further demonstrate that while IL-7 is principally a heparin/heparan sulfate binding protein, it also interacts with dermatan sulfate, chondroitin sulfates C, D, and E, indicating that this cytokine preferentially interacts with GAGs having a higher degree of sulfation.
Biochimie.Biochimie.2012 Jan;94(1):242-9. doi: 10.1016/j.biochi.2011.10.015. Epub 2011 Nov 6.
Glycosaminoglycans (GAGs) interact with a number of cytokines and growth factors thereby playing an essential role in the regulation of many physiological processes. These interactions are important for both normal signal transduction and the regulation of the tissue distribution of cytokines/growth
PMID 22085638

On the specificity of heparin/heparan sulfate binding to proteins. Anion-binding sites on antithrombin and thrombin are fundamentally different.

Mosier PD, Krishnasamy C, Kellogg GE, Desai UR.Author information Department of Medicinal Chemistry and Institute of Structural Biology and Drug Discovery, Virginia Commonwealth University, Richmond, Virginia, United States of America.AbstractBACKGROUND: The antithrombin-heparin/heparan sulfate (H/HS) and thrombin-H/HS interactions are recognized as prototypic specific and non-specific glycosaminoglycan (GAG)-protein interactions, respectively. The fundamental structural basis for the origin of specificity, or lack thereof, in these interactions remains unclear. The availability of multiple co-crystal structures facilitates a structural analysis that challenges the long-held belief that the GAG binding sites in antithrombin and thrombin are essentially similar with high solvent exposure and shallow surface characteristics.
PloS one.PLoS One.2012;7(11):e48632. doi: 10.1371/journal.pone.0048632. Epub 2012 Nov 12.
BACKGROUND: The antithrombin-heparin/heparan sulfate (H/HS) and thrombin-H/HS interactions are recognized as prototypic specific and non-specific glycosaminoglycan (GAG)-protein interactions, respectively. The fundamental structural basis for the origin of specificity, or lack thereof, in these inte
PMID 23152789