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Cell surfaces, heparan sulfate

Valenzuela-Femandez A, Palanche T, Amara A, et al. Optimal inhibition of X4 HIV isolates by the CXC chemokine stromal cell-derived factor 1 alpha requires interaction with cell surface heparan sulfate proteoglycans. J Biol Chem 2001 276(28) 26550-26558. [Pg.294]

Fleckenstein, J. M., Holland, J. T., and Hasty, D. L. (2002). Interaction of an outer membrane protein of enterotoxigenic Escherichia coli with cell surface heparan sulfate proteoglycans. Infect. Immun. 70,1530-1537. [Pg.145]

Yanagishita, M. and Hascall, V. C. (1992). Cell surface heparan sulfate proteoglycans. J. Biol. Chem. 267, 9451-9454. [Pg.30]

Bernfleld, M., Gotte, M., Park, P.W., Reizes, O., Fitzgerald, M.L., Lincecum, J., Zako, M. (1999) Functions of cell surface heparan sulfate proteoglycans. Annu. Rev. Biochem. 68, 729-777. Extensive review of the biological roles of heparan sulfate. [Pg.269]

R.W. Mahley and Z.S. Ji, Remnant lipoprotein metabolism key pathways involving cell-surface heparan sulfate proteoglycans and apolipoprotein E, J. Lipid Res. 40 (1999) 1-16. [Pg.310]

Gallo, R.L., Ono, M Povsic, T., et al. (1994) Syndecans, cell surface heparan sulfate proteoglycans, are induced by a proline-rich antimicrobial peptide from wounds. Proc. Natl. Acad. Sci. USA 91,11035-11039. [Pg.155]

Laterra, J., Silbert, J. E., and Culp, L. A., Cell surface heparan sulfate mediates some adhesive responses to glycosaminoglycan-binding matrices including fibronectin. J. Cell Biol. 96, 112-121 (1983). [Pg.163]

Already in 1965, Ryser and Hancock provided evidence that histones and polyamino acids could greatly enhance albumin uptake by cultured tumor cells (6). More recently, several polybasic peptides (so-called protein transduction domains, PTDs or cell-penetrating peptides, CPPs) have been shown to efficiently mediate uptake of nucleic acids, bioactive peptides, phage particles, and liposomes into a wide variety of mammalian cells. The initially proposed ability of CPPs to penetrate plasma membranes via a temperature-independent, non-endocytotic pathway was later shown to be a fixation artifact, and it is currently widely accepted that CPP-mediated macromolecular delivery follows energy-dependent endocytotic pathways that in most cases depend on the expression of cell-surface heparan sulfate proteoglycans (HSPGs) (7). [Pg.5]

Patel, M., Yanagishita, M., Roderiquez, G., Bou-Habib, D. C., Oravecz, T., Hascall, V. C., and Norcross, M. A. (1993) Cell-surface heparan sulfate proteoglycan mediates HIV-1 infection of T-cell lines. AIDS Res Hum Retroviruses 9, 167-174. [Pg.112]

Brauker JH, Wang JL Nonlysosomal processing of cell-surface heparan sulfate proteoglycans. / Biol Chem 262 13093-13101,1987. [Pg.193]

Recently a decasaccharide sequence from cell surface heparan sulfate was found to interact with lipoprotein lipase [225], an enzyme previously shown to bind to heparan sulfate on the surface of endothelial cells [226]. [Pg.24]

Luster, A.D., S.M. Greenberg, and P. Leder. The IP-10 chemokine binds to a specific cell surface heparan sulfate site shared with platelet factor 4 and inhibits endothelial cell proliferation. J Exp Med 182 219-31, 1995. [Pg.149]

Antithrombin has been shown to promote the release of prostacyclin from endothelial cells [74] and to attenuate ischemia-induced leukocyte extravasation [75]. In addition, chemotactic effects of AT on neutrophils and signaling via interaction with cell-surface heparan sulfate proteoglycans... [Pg.1007]

Giuseppetti, J.M., McCarthy, J.B. and Letourneau, P.C. (1994) Isolation and partial characterization of cell-surface heparan sulfate proteoglycan from embryonic rat spinal cord. J. Neurosci. Res. 37 584-595. [Pg.392]

Sarafanov AG, Ananyeva NM, Shima M, et al Cell surface heparan sulfate proteoglycans (HSPGs) par-... [Pg.160]

Yanagishita, M., and Hascall, V. C., 1992. Cell surface heparan sulfate proteoglycans./. Biol. Chem. 267 9451-9454. lozzo, R. V., 1999. The biology of small leucine-rich proteoglycans Functional network of interactive proteins./ Biol. Chem. 274 18843—18846. [Pg.316]

Apolipoprotein E (apoE) is an important lipid transport protein in human plasma and brain. It mediates hepatic clearance of remnant lipoproteins as a high-affin-ity ligand for the low-density lipoprotein receptor (LDLR) family, including LDLR, LDLR-related protein (LRP), and cell surface heparan sulfate PGs (71). In the liver, heparan sulfate PGs facilitate the interaction of remnant particles with LRP, which is known as the heparan sulfate PG-LRP pathway, in which apoE initially interacts... [Pg.240]

Barth H, Schafer C, Adah MI, Zhang F, Linhardt RJ, Toyoda H, Kinoshita-Toyoda A, Toida T, Van Kuppevelt TH, Depla E, Von Weizsacker F, Blum HE, Baumert TF. Cellular binding of hepatitis C virus envelope glycoprotein E2 requires cell surface heparan sulfate. J Biol Chem 2003 278 41003-41012. [Pg.247]

Ji ZS, Pitas RE, Mahley RW. Differential cellular accumulation/retention of apolipoprotein E mediated by cell surface heparan sulfate proteoglycans. Apo-lipoproteins E3 and E2 greater than e4. J Biol Chem 1998 273 13452-13460. [Pg.249]


See other pages where Cell surfaces, heparan sulfate is mentioned: [Pg.118]    [Pg.289]    [Pg.220]    [Pg.220]    [Pg.339]    [Pg.302]    [Pg.8]    [Pg.9]    [Pg.451]    [Pg.807]    [Pg.275]    [Pg.322]    [Pg.322]    [Pg.139]    [Pg.1428]    [Pg.316]    [Pg.58]    [Pg.237]    [Pg.241]    [Pg.243]    [Pg.12]   
See also in sourсe #XX -- [ Pg.545 ]




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Cell Surface Heparan Sulfate Proteoglycans

Cell surface

Functions of Cell Surface Heparan Sulfate Proteoglycans

Heparan

Heparan sulfate

Part-time Cell Surface Heparan Sulfate Proteoglycans

Surface sulfate

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