Cell-Surface Heparan Sulfate Proteoglycan Mediates HIV-1 Infection of T-Cell Lines

1993 ◽  
Vol 9 (2) ◽  
pp. 167-174 ◽  
Author(s):  
MAHESH PATEL ◽  
MASAKI YANAGISHITA ◽  
GREGORY RODERIQUEZ ◽  
DUMITH CHEQUER BOU-HABIB ◽  
TAMAS ORAVECZ ◽  
...  
Keyword(s):  
T Cell ◽  
Cell Surface ◽  
Heparan Sulfate ◽  
Cell Lines ◽  
Heparan Sulfate Proteoglycan ◽  
Sulfate Proteoglycan ◽  
T Cell Lines ◽  
Hiv 1

scholarly journals Heparan sulfate proteoglycan on leukemic cells is primarily involved in integrin triggering and its mediated adhesion to endothelial cells.

1996 ◽  
Vol 184 (5) ◽  
pp. 1987-1997 ◽  
Author(s):  
Y Tanaka ◽  
K Kimata ◽  
A Wake ◽  
S Mine ◽  
I Morimoto ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
T Cell ◽  
Cell Surface ◽  
Heparan Sulfate ◽  
Heparan Sulfate Proteoglycan ◽  
Leukemic Cells ◽  
Intercellular Adhesion Molecule ◽  
Proteoglycan Synthesis ◽  
Sulfate Proteoglycan ◽  
Heparin Binding

Leukocyte migration from circulation into tissue depends on leukocyte integrin-mediated adhesion to endothelium, but integrins cannot function until activated. However, it remains to be understood how tumor cells adhere to endothelium and infiltrate into underlying tissue. We studied mechanisms of extravasation of leukemic cells using adult T cell leukemia (ATL) cells and report the following novel features of cell surface heparan sulfate proteoglycan on ATL cells in ATL cell adhesion to endothelium: ATL cells adhere to endothelial cells through already activated integrins without exogenous stimulation; different from any other hematopoietic cells, ATL cells express a characteristic heparan sulfate capable of immobilizing heparin-binding chemokine macrophage inflammatory protein (MIP)-1 beta, a potent T cell integrin trigger, produced by the cells themselves; competitive interruption of endogenous heparan sulfate proteoglycan synthesis reduces cell surface MIP-1 beta and prevents ATL cells from integrin-mediated adhesion to endothelial cells or intercellular adhesion molecule-1 triggered through G-protein. We propose that leukemic cells adhere to endothelial cells through the adhesion cascade, similar to normal leukocyte, and that the cell surface heparan sulfate, particularly on ATL cells, is pivotally involved in chemokine-dependent autocrine stimulation of integrin triggering by immobilizing the chemokine on them.

scholarly journals Molecular cloning of the major cell surface heparan sulfate proteoglycan from rat liver.

1992 ◽  
Vol 267 (6) ◽  
pp. 3894-3900
Author(s):  
A Pierce ◽  
M Lyon ◽  
I.N. Hampson ◽  
G.J. Cowling ◽  
J.T. Gallagher
Keyword(s):  
Cell Surface ◽  
Heparan Sulfate ◽  
Molecular Cloning ◽  
Rat Liver ◽  
Heparan Sulfate Proteoglycan ◽  
Sulfate Proteoglycan

Transient expression of a cell surface heparan sulfate proteoglycan (syndecan) during limb development

1990 ◽  
Vol 140 (1) ◽  
pp. 83-92 ◽  
Author(s):  
Michael Solursh ◽  
Rebecca S. Reiter ◽  
Karen L. Jensen ◽  
Masato Kato ◽  
Merton Bernfield
Keyword(s):  
Cell Surface ◽  
Heparan Sulfate ◽  
Transient Expression ◽  
Limb Development ◽  
Heparan Sulfate Proteoglycan ◽  
Sulfate Proteoglycan ◽  
A Cell

High glucose-mediated loss of cell surface heparan sulfate proteoglycan impairs the endothelial shear stress response

Cytoskeleton ◽  
2010 ◽  
Vol 67 (3) ◽  
pp. 135-141 ◽  
Author(s):  
Jeremy B. Brower ◽  
Jerome H. Targovnik ◽  
Michael R. Caplan ◽  
Stephen P. Massia
Keyword(s):  
Shear Stress ◽  
Stress Response ◽  
Cell Surface ◽  
Heparan Sulfate ◽  
High Glucose ◽  
Heparan Sulfate Proteoglycan ◽  
Sulfate Proteoglycan ◽  
Endothelial Shear Stress ◽  
Shear Stress Response

Release of Hydrogen Peroxide from Human T Cell Lines and Normal Lymphocytes Co-Infected with Hiv-1 and Mycoplasma

1995 ◽  
Vol 23 (3) ◽  
pp. 197-212 ◽  
Author(s):  
J. Chochola ◽  
A. D. Strosberg ◽  
M. Stanislawski
Keyword(s):  
Hydrogen Peroxide ◽  
T Cell ◽  
Cell Lines ◽  
Human T Cell ◽  
T Cell Lines ◽  
Hiv 1

scholarly journals Genogroup II Noroviruses Efficiently Bind to Heparan Sulfate Proteoglycan Associated with the Cellular Membrane

2004 ◽  
Vol 78 (8) ◽  
pp. 3817-3826 ◽  
Author(s):  
Masaru Tamura ◽  
Katsuro Natori ◽  
Masahiko Kobayashi ◽  
Tatsuo Miyamura ◽  
Naokazu Takeda
Keyword(s):  
Cell Surface ◽  
Heparan Sulfate ◽  
Cellular Membrane ◽  
Heparan Sulfate Proteoglycan ◽  
Sulfate Proteoglycan ◽  
Sulfated Glycosaminoglycan ◽  
The Family ◽  
Sulfated Derivative ◽  
Causative Agents

ABSTRACT Norovirus (NV), a member of the family Caliciviridae, is one of the important causative agents of acute gastroenteritis. In the present study, we found that virus-like particles (VLPs) derived from genogroup II (GII) NV were bound to cell surface heparan sulfate proteoglycan. Interestingly, the VLPs derived from GII were more than ten times likelier to bind to cells than were those derived from genogroup I (GI). Heparin, a sulfated glycosaminoglycan, and suramin, a highly sulfated derivative of urea, efficiently blocked VLP binding to mammalian cell surfaces. The reagents known to bind to cell surface heparan sulfate, as well as the enzymes that specifically digest heparan sulfate, markedly reduced VLP binding to the cells. Treatment of the cells with chlorate revealed that sulfation of heparan sulfate plays an important role in the NV-heparan sulfate interaction. The binding efficiency of NV to undifferentiated Caco-2 (U-Caco-2) cells differed largely between GI NV and GII NV, whereas the efficiency of binding to differentiated Caco-2 (D-Caco-2) cells did not differ significantly between the two genogroups, although slight differences between strains were observed. Digestion with heparinase I resulted in a reduction of up to 90% in U-Caco-2 cells and a reduction of up to only 50% in D-Caco-2 cells, indicating that heparan sulfate is the major binding molecule for U-Caco-2 cells, while it contributed to only half of the binding in the case of D-Caco-2 cells. The other half of those VLPs was likely to be associated with H-type blood antigen, suggesting that GII NV has two separate binding sites. The present study is the first to address the possible role of cell surface glycosaminoglycans in the binding of recombinant VLPs of NV.

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