نتایج جستجو برای: heparin binding hemagglutinin

تعداد نتایج: 449543  

Journal: :Circulation research 2006
Errol S Wijelath Salman Rahman Mayumi Namekata Jacqueline Murray Tomoaki Nishimura Zohreh Mostafavi-Pour Yatin Patel Yasuo Suda Martin J Humphries Michael Sobel

We describe extracellular interactions between fibronectin (Fn) and vascular endothelial growth factor (VEGF) that influence integrin-growth factor receptor crosstalk and cellular responses. In previous work, we found that VEGF bound specifically to fibronectin (Fn) but not vitronectin or collagens. Herein we report that VEGF binds to the heparin-II domain of Fn and that the cell-binding and VE...

Journal: :Blood 2005
Weiqing Zhang Richard Swanson Gonzalo Izaguirre Yan Xiong Lester F Lau Steven T Olson

The heparin-binding site of antithrombin is shown here to play a crucial role in mediating the antiangiogenic activity of conformationally altered cleaved and latent forms of the serpin. Blocking the heparin-binding site of cleaved or latent antithrombin by complexation with a high-affinity heparin pentasaccharide abolished the serpin's ability to inhibit proliferation, migration, capillary-lik...

2018
Julie Eberle Davis Ravi Kumar Gundampati Srinivas Jayanthi Joshua Anderson Abigail Pickhardt Bhanu prasanth Koppolu David A. Zaharoff Thallapuranam Krishnaswamy Suresh Kumar

Acidic human fibroblast growth factor (hFGF1) plays a key role in cell growth and proliferation. Activation of the cell surface FGF receptor is believed to involve the glycosaminoglycan, heparin. However, the exact role of heparin is a subject of considerable debate. In this context, in this study, the correlation between heparin binding affinity and cell proliferation activity of hFGF1 is exam...

Journal: :Blood 2002
Milena A Gebska Ian Titley Hugh F Paterson Ricardo M Morilla Derek C Davies Alicja M Gruszka-Westwood Vijay V Kakkar Suzanne Eccles Michael F Scully

During cell death of human cultured leukocytes (Jurkat, HL-60, THP-1, U937) and freshly prepared leukocytes, we observed a greater than 100-fold increase in the affinity of apoptotic and necrotic cells for fluorescein isothiocyanate (FITC)-heparin in comparison with live cells. Binding of FITC-heparin was reversed in the presence of high ionic strength, unlabeled heparan sulfate, and heparin an...

Journal: :Investigative ophthalmology & visual science 2005
V John Hindson John T Gallagher Willi Halfter Paul N Bishop

PURPOSE The extracellular matrix glycoprotein opticin is a small leucine-rich repeat proteoglycan/protein family member that was discovered associated with vitreous humor collagen fibrils. Opticin is present throughout the vitreous, but is particularly concentrated at the internal limiting lamina, where it colocalizes with type XVIII collagen. The present study investigated whether opticin inte...

Journal: :Journal of virology 2003
A Kern K Schmidt C Leder O J Müller C E Wobus K Bettinger C W Von der Lieth J A King J A Kleinschmidt

Infection of cells with adeno-associated virus (AAV) type 2 (AAV-2) is mediated by binding to heparan sulfate proteoglycan and can be competed by heparin. Mutational analysis of AAV-2 capsid proteins showed that a group of basic amino acids (arginines 484, 487, 585, and 588 and lysine 532) contribute to heparin and HeLa cell binding. These amino acids are positioned in three clusters at the thr...

Journal: :The Journal of biological chemistry 1994
K Mizuno H Inoue M Hagiya S Shimizu T Nose Y Shimohigashi T Nakamura

Hepatocyte growth factor (HGF) has a strong affinity for heparin. About one fourth of HGF secreted from MRC-5 human embryonic lung fibroblast cells was found to be associated with heparin and heparan sulfate proteoglycan on the cell surface and extracellular matrix. To identify heparin-binding sites within the HGF molecule, we constructed variously deleted mutant HGFs and examined their binding...

Journal: :The Journal of biological chemistry 1992
M Sobel D F Soler J C Kermode R B Harris

Human von Willebrand factor, a plasma glycoprotein which plays a critical role in regulating hemostasis, binds heparin, but the physiological importance and mode of this interaction is poorly understood. Using the motif of an amino acid sequence of a consensus heparin binding synthetic peptide, a 23-residue sequence (Tyr565-Ala587) of human von Willebrand factor was identified that retains the ...

Journal: :Arteriosclerosis 1989
A D Cardin H J Weintraub

Forty-nine regions in 21 proteins were identified as potential heparin-binding sites based on the sequence organizations of their basic and nonbasic residues. Twelve known heparin-binding sequences in vitronectin, apolipoproteins E and B-100, and platelet factor 4 were used to formulate two search strings for identifying potential heparin-binding regions in other proteins. Consensus sequences f...

Journal: :Chemistry & biology 2007
Jose L de Paz Christian Noti Friederike Böhm Sabine Werner Peter H Seeberger

Heparin is a highly sulfated polysaccharide that regulates a variety of cellular processes by interaction with a host of proteins. We report the preparation of synthetic heparin oligosaccharide glycodendrimers and their use as heparin mimetics to regulate heparin-protein interactions. The multivalent display of sugar epitopes mimics the naturally occurring glycans found on cell surfaces and enh...

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