Heparin binding

Pentosan polysulfate Inhibits heparin-binding growth factors... 

Like VEGF165, native VEGF is a heparin-binding homodimeric glycoprotein of 45 kDa. In contrast, VEGFi2i lacks heparin-binding properties. VEGF i89... 

Neuropilin-1 (NRP1), a molecule that had been previously shown to be implicated in axon guidance as a receptor for members of collapsin/semaphorin family, has been characterized as a which interacts with the heparin-binding VEGF isoforms. 

Kim J. Han L Kim Y. et al. C-terminal heparin-binding domain of fibronectin regulates integrin-mediated cell spreading but not the activation of mitogen-activated protein kinase / / Biochem. J. 2001. V. 360. P. 239-245. 

Margalit H. Fisher N. Ben-Sasson S.A. (1993) Comparative analysis of structurally defined heparin binding sequences reveals a distinct spatial distribution of basic residues // J. Biol. Chem V. 268. P.19228-19231. 

Burgess WH, Maciag T (1989) The heparin-binding (fibroblast) growth-factor family of proteins. Annu Rev Biochem 58 575-606... 

Rajangam K, Beharma HA, Hui MJ et al (2006) Heparin binding nanostructures to promote growth of blood vessels. Nano Lett 6 2086-2090... 

Sobel M, Soler DF, Kermode JC, Harris RB. Localization and characterization of a heparin binding domain peptide of human von Willebrand factor. J Biol Chem 1992 267 8857-8862. 

Johnson Z, Kosco-Vilbois MH, Herren S, et al. Interference with heparin binding and oligomerization creates a novel anti-inflammatory strategy targeting the che-mokine system. J Immunol 2004 173 5776-85. 

Mayo KH, Ilyina E, Roongta V, et al. Heparin binding to platelet factor-4. An NMR and site-directed mutagenesis study arginine residues are crucial for binding. Biochem J 1995 312 357-65. 

Campanella GS, Lee EM, Sun J, Luster AD. CXCR3 and heparin binding sites of the chemokine IP-10 (CXCL10). J Biol Chem 2003 278 17066-74. 

Although the order of affinity of PF-4 for different glycosaminogly-cans, and dissociation of their complexes with salts, are typical of nonspecific, electrostatic interactions, PF-4 is not strictly a cationic protein.452 It is probable that heparin binds to clusters of basic amino acids (two lysine pairs) near the carboxyl terminal of a polypeptide chain that has an overall preponderance of acidic amino acid residues.457 High-molecular-weight heparin species can bind two PF-4 molecules, with formation of complexes 10 to 100 times as strong as those with antithrombin.217... 

One of the first practical applications for these fluorescent labelled heparins was to examine the heparin binding behavior of different proteins and peptides under study in our laboratories. To this end we used a modification of the dot-blot assay described by Hirose and colleagues (13). F-D labelled heparin (-1 fluorescein/heparin) was radiolabelled with 125Iodine using iodobeads, to a specific activity of approximately 0.5 x 106 cpm/pg. Solutions of proteins with known heparin-binding capacities were dotted on nitrocellulose paper. A series of replicates... 

The fluorescent labelling of heparin with F-D by this technique did not observably alter the biologic activity of the heparin as regards to its binding to antithrombin and catalysis of antithrombin s neutralization of activated coagulation factors. F-D labelled heparins also bound to other known heparin-binding proteins in a saturable and reversible manner, as demonstrated by the dot-blot assay technique (Figure 6). 

Leung L Saigo K., Grant D. Heparin binds to human monocytes and modulates their procoagulant activities and secretory phenotypes. Effect of histidine-rich glycoprotein. Blood 1989 73, 177-84. 

Shackelton LM, Mann DM, Millis AJ 1995 Identification of a 38kDa heparin-binding glycoprotein (gp38k) in differentiating vascular smooth muscle cells as a member of a group of proteins associated with tissue remodeling. J Biol Chem 270 13076—13083... 

Browning, PJ, Roberts, DD, Zabrenetzky, V, Bryant, J, Kaplan, M, Washington, RH, Panet, A, Gallo, RC, and Vogel, T, 1994. Apolipoprotein E (ApoE), a novel heparin-binding protein inhibits the development of Kaposi s sarcoma-like lesions in BALB/c nu/nu mice. J Exp Med 180, 1949-1954. 

Heparin is a carbohydrate-based (glycosaminoglycan) anticoagulant associated with many tissues, but mainly found stored intracellularly as granules in mast cells that line the endothelium of blood vessels. Upon release into the bloodstream, heparin binds to and thereby activates an additional plasma protein, namely antithrombin. The heparin-antithrombin complex then binds a number of activated clotting factors (including Ha, IXa, Xa, XIa and Xlla), thereby inactivating them. The heparin now disassociates from the complex and combines with another antithrombin molecule, thereby initiating another turn of this inhibitory cycle. 

Hung, S.I., et al. Transient expression of Yml, a heparin-binding lectin, during developmental hematopoiesis and inflammation, J. Leukoc. Biol., 72, 72, 2002. 

Other recent NMR investigations of the interaction between heparin polymers and different protein receptors have focused on the heparin binding to full-length Tau systems.29 In this particular example, the strength and location of the interactions was investigated, as well as the structural consequences derived from this important molecular interaction. 

Fromm, J.R., R.E. Hileman, E.E. Caldwell, J.M. Weiler, and R.J. Linhardt. 1997. Pattern and spacing of basic amino acids in heparin binding sites. Arch Biochem Biophys 343 92-100. 

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