Evidence for transsynaptic regulation of neuronal cell surface heparan sulfate proteoglycan in developing rat superior cervical ganglion

1984 ◽  
Vol 26 (2) ◽  
pp. 127-133 ◽  
Author(s):  
Karen F. Greif ◽  
Holly I. Trenchard
Keyword(s):  
Cell Surface ◽  
Heparan Sulfate ◽  
Superior Cervical Ganglion ◽  
Neuronal Cell ◽  
Heparan Sulfate Proteoglycan ◽  
Sulfate Proteoglycan ◽  
Cervical Ganglion ◽  
Developing Rat

Expression of the cell-surface heparan sulfate proteoglycan syndecan-2 in developing rat anterior pituitary gland

2013 ◽  
Vol 353 (3) ◽  
pp. 473-481 ◽  
Author(s):  
Kotaro Horiguchi ◽  
Rahimi Syaidah ◽  
Ken Fujiwara ◽  
Takehiro Tsukada ◽  
Dini Ramadhani ◽  
...  
Keyword(s):  
Cell Surface ◽  
Pituitary Gland ◽  
Heparan Sulfate ◽  
Anterior Pituitary ◽  
Heparan Sulfate Proteoglycan ◽  
Anterior Pituitary Gland ◽  
Sulfate Proteoglycan ◽  
Developing Rat

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

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

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

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.

scholarly journals Cell-substratum adhesion in chick neural retina depends upon protein-heparan sulfate interactions.

1985 ◽  
Vol 100 (4) ◽  
pp. 1192-1199 ◽  
Author(s):  
G J Cole ◽  
D Schubert ◽  
L Glaser
Keyword(s):  
Cell Surface ◽  
Heparan Sulfate ◽  
Neural Retina ◽  
Heparan Sulfate Proteoglycan ◽  
Retinal Cell ◽  
Sulfate Proteoglycan ◽  
Heparin Binding ◽  
Embryonic Chick ◽  
Retinal Cells ◽  
Inert Surfaces

Embryonic chick neural retina cells in culture release complexes of proteins and glycosaminoglycans, termed adherons, which stimulate cell-substratum adhesion when adsorbed to nonadhesive surfaces. Two distinct retinal cell surface macromolecules, a 170,000-mol-wt glycoprotein and a heparan sulfate proteoglycan; are components of adherons that can independently promote adhesion when coated on inert surfaces. The 170,000-mol-wt polypeptide contains a heparin-binding domain, as indicated by its retention on heparin-agarose columns and its ability to bind [3H]heparin in solution. The attachment of embryonic chick retinal cells to the 170,000-mol-wt protein also depends upon interactions between the protein and the heparan sulfate proteoglycan, since heparan sulfate in solution disrupts adhesion of chick neural retina cells to glass surfaces coated with the 170,000-mol-wt protein. This adhesion is not impaired by chondroitin sulfate or hyaluronic acid, which indicates that inhibition by heparan sulfate is specific. Polyclonal antisera directed against the cell surface heparan sulfate proteoglycan also inhibit attachment of retinal cells to the 170,000-mol-wt protein, which suggests that cell-adheron binding is mediated in part by interactions between cell surface heparan sulfate proteoglycan and 170,000-mol-wt protein contained in the adheron particles. Previous studies have indicated that this type of cell-substratum adhesion is tissue-specific since retina cells do not attach to muscle adherons. Schubert D., M. LaCorbiere, F. G. Klier, and C. Birdwell, 1983, J. Cell Biol. 96:990-998.

scholarly journals Codistribution of heparan sulfate proteoglycan, laminin, and fibronectin in the extracellular matrix of normal rat kidney cells and their coordinate absence in transformed cells.

1982 ◽  
Vol 94 (1) ◽  
pp. 28-35 ◽  
Author(s):  
E G Hayman ◽  
A Oldberg ◽  
G R Martin ◽  
E Ruoslahti
Keyword(s):  
Cell Surface ◽  
Heparan Sulfate ◽  
Chondroitin Sulfate ◽  
Rat Kidney ◽  
Heparan Sulfate Proteoglycan ◽  
Chondroitin Sulfate Proteoglycan ◽  
Transformed Cells ◽  
Kidney Cells ◽  
Sulfate Proteoglycan ◽  
Normal Rat

We used antibodies raised against both a heparan sulfate proteoglycan purified from a mouse sarcoma and a chondroitin sulfate proteoglycan purified from a rat yolk sac carcinoma to study the appearance and distribution of proteoglycans in cultured cells. Normal rat kidney cells displayed a fibrillar network of immunoreactive material at the cell surface when stained with antibodies to heparan sulfate proteoglycan, while virally transformed rat kidney cells lacked such a surface network. Antibodies to chondroitin sulfate proteoglycan revealed a punctate pattern on the surface of both cell types. The distribution of these two proteoglycans was compared to that of fibronectin by double-labeling immunofluorescent staining. The heparan sulfate proteoglycan was found to codistribute with fibronectin, and fibronectin and laminin gave coincidental stainings. The distribution of chondroitin sulfate proteoglycan was not coincidental with that of fibronectin. Distinct fibers containing fibronectin but lacking chondroitin sulfate proteoglycan were observed. When the transformed cells were cultured in the presence of sodium butyrate, their morphology changed, and fibronectin, laminin, and heparan sulfate proteoglycan appeared at the cell surface in a pattern resembling that of normal cells. These results suggest that fibronectin, laminin, and heparan sulfate proteoglycan may be complexed at the cell surface. The proteoglycan may play a central role in assembly of such complexes since heparan sulfate has been shown to interact with both fibronectin and laminin.

Sign in / Sign up

Export Citation Format

Share Document