Heparan sulfate proteoglycans

The intima of the arterial wall contains hyaluronic acid and chondroitin sulfate, dermatan sulfate, and heparan sulfate proteoglycans. Of these proteoglycans, dermatan sulfate binds plasma low-density lipoproteins. In addition, dermatan sulfate appears to be the major GAG synthesized by arterial smooth muscle cells. Because it is these cells that profiferate in atherosclerotic lesions in arteries, dermatan sulfate may play an important role in development of the atherosclerotic plaque. 

Oravecz T, Pall M, Wang J, Roderiquez G, Ditto M, Norcross MA. Regulation of anti-HIV-1 activity of RANTES by heparan sulfate proteoglycans. J Immunol 1997 159(9) 4587 1592. 

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. 

Alvarez-Dominguez, C., Vazquez-Boland, J. A., Carrasco-Martin, E., Lopez-Mato, P., and Leyva-Cobain, E. (1997). Host cell heparan sulfate proteoglycans mediate attachment and entry of Listeria monocytongenes, and the listerial surface protein ActA is involved in heparan sulfate receptor recognition. Infect. Immun. 65, 78-88. 

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. 

Marty C, Meylan C, Schott H, et al. Enhanced heparan sulfate proteoglycan-mediated uptake of cell-penetrating peptide-modified liposomes. Cell Mol Life Sci 2004 61 (14) 1785-1794. 

The rationale for this type of contrast agent is to use the endogenous metabolic pathway of lipid metabolism in the liver for the transport of iodinated substances. Chylomicron remnants are naturally occurring lipoproteins in the blood that are responsible for the transport of lipids into the liver. Three different mechanisms for this transport are discussed direct uptake by the low-density lipoprotein receptor transport to the low-density lipoprotein receptor-related protein (LRP) mediated by heparan sulfate proteoglycan (HSPG) or direct HSPG-LRP uptake and direct HSPG uptake. One of the prerequisites for particles to be transported by these mechanisms is a mean diameter of less than 100-300 run. 

Murthy, K. H., et al. (2001). Crystal structure of a complement control protein that regulates both pathways of complement activation and binds heparan sulfate proteoglycans. Cell 104,301-311. 

Stow JL, de Almeida JB, Narula N, Holtzman EJ, Ercolani L, Ausiello DA (1991) A heterotrimeric G protein, G alpha i-3, on Golgi membranes regulates the secretion of a heparan sulfate proteoglycan in LLC-PKl epithelial cells. J Cell Biol 114 1113-1124... 

This pentasaccharide sequence induces a conformational change in AT III which probably causes the complex to be more accessible to the active site of the proteases. The most relevant protease affected by the pentasaccharide 3 is factor Xa, but factor Xlla and plasma kallikrein activities can also be potentiated. Sequence 3 occurs in heparin as well as in various heparan sulfate proteoglycans of different origin including the vascular endothelium. 

Summerford, C., and R.I Samnlski, Membrane-associated heparan sulfate proteoglycan is a receptor for adeno-associated virus type 2 virions. J Virol, 1998. 72(2) 1438-45. 

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

Whereas LPL predominantly hydrolyzes triglycerides in chylomicrons and VLDL, it has been shown that HL primarily hydrolyzes triglycerides and phospholipids from small VLDL, IDL, and HDL [82]. Like LPL, HL binds to the endothelium through heparan sulfate proteoglycans and is released upon heparin administration because of its higher affinity for heparin than for the endogenous heparan sulfate proteoglycans. Intravenous injection of a heparin bolus displaces the HL enzyme into postheparin plasma, where its activity can be quantified. 

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. 

Iozzo, R.V. (2001) Heparan sulfate proteoglycans intricate molecules with intriguing functions. J. Clin. Invest. 108, 165-167. 

Kawashima, H., Watanabe, N., Hirose, M., Sun, X., Atarashi, K., Kimura, T., Shikata, K., Matsuda, M., Ogawa, D., Heljasvaara, R., Rehn, M., Pihlajaniemi, T., and Miyasaka, M. (2003). Collagen XVIII, a basement membrane heparan sulfate proteoglycan, interacts with L-selectin and monocyte chemoattractant protein-1. / Biol. Chem. 278, 13069-13076. 

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. 

The reason(s) observed in our studies for the preferential transduction of the proximal tubule and intercalated cells is not entirely clear. Several possible mechanisms may be implicated. The early steps of AAV infection involve attachment to a variety of cell surface receptors (heparan sulfate proteoglycan, fibroblast growth factor receptor, and av-/ 5 integrin) followed by a clathrin-dependent... 

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