S5.7 Identification of a cell surface heparan-sulfate proteoglycan involved in HB-GAM (heparin-binding growth-associated molecule)-induced axon outgrowth

1993 ◽  
Vol 10 (4) ◽  
pp. 257-257
Author(s):  
E. Raulo ◽  
R. Nolo ◽  
H. Rauvala
Keyword(s):  
Cell Surface ◽  
Heparan Sulfate ◽  
Heparan Sulfate Proteoglycan ◽  
Axon Outgrowth ◽  
Sulfate Proteoglycan ◽  
Heparin Binding ◽  
A Cell

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

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.

Syndecan-3: a cell-surface heparan sulfate proteoglycan important for chondrocyte proliferation and function during limb skeletogenesis

2005 ◽  
Vol 23 (3) ◽  
pp. 191-199 ◽  
Author(s):  
Maurizio Pacifici ◽  
Tsuyoshi Shimo ◽  
Chiara Gentili ◽  
Thorsten Kirsch ◽  
Theresa A. Freeman ◽  
...  
Keyword(s):  
Cell Surface ◽  
Heparan Sulfate ◽  
Heparan Sulfate Proteoglycan ◽  
Sulfate Proteoglycan ◽  
Chondrocyte Proliferation ◽  
A Cell ◽  
And Function

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 Isolation of a cell-surface receptor for chick neural retina adherons.

1985 ◽  
Vol 100 (1) ◽  
pp. 56-63 ◽  
Author(s):  
D Schubert ◽  
M LaCorbiere
Keyword(s):  
Cell Surface ◽  
Heparan Sulfate ◽  
Cell Aggregation ◽  
Neural Retina ◽  
Heparan Sulfate Proteoglycan ◽  
Cell Surface Receptor ◽  
Sulfate Proteoglycan ◽  
Surface Receptor ◽  
A Cell ◽  
Cell Cell

Embryonic chick neural retina cells release glycoprotein complexes, termed adherons, into their culture medium. When absorbed onto the surface of petri dishes, neural retina adherons increase the initial rate of neural retina cell adhesion. In solution they increase the rate of cell-cell aggregation. Cell-cell and adheron-cell adhesions of cultured retina cells are selectively inhibited by heparan-sulfate glycosaminoglycan, but not by chondroitin sulfate or hyaluronic acid, suggesting that a heparan-sulfate proteoglycan may be involved in the adhesion process. We isolated a heparan-sulfate proteoglycan from the growth-conditioned medium of neural retina cells, and prepared an antiserum against it. Monovalent Fab' fragments of these antibodies completely inhibited cell-adheron adhesion, and partially blocked spontaneous cell-cell aggregation. An antigenically and structurally similar heparan-sulfate proteoglycan was isolated from the cell surface. This proteoglycan bound directly to adherons, and when absorbed to plastic, stimulated cell-substratum adhesion. These data suggest that a heparan-sulfate proteoglycan on the surface of chick neural retina cells acted as a receptor for adhesion-mediating glycoprotein complexes (adherons).

scholarly journals Direct Interaction of CASK/LIN-2 and Syndecan Heparan Sulfate Proteoglycan and Their Overlapping Distribution in Neuronal Synapses

1998 ◽  
Vol 142 (1) ◽  
pp. 139-151 ◽  
Author(s):  
Yi-Ping Hsueh ◽  
Fu-Chia Yang ◽  
Viktor Kharazia ◽  
Scott Naisbitt ◽  
Alexandra R. Cohen ◽  
...  
Keyword(s):  
Cell Surface ◽  
Heparan Sulfate ◽  
Pdz Domain ◽  
Specific Interaction ◽  
Direct Interaction ◽  
Heparan Sulfate Proteoglycan ◽  
Mammalian Brain ◽  
Sulfate Proteoglycan ◽  
Heparin Binding ◽  
Neuronal Synapses

CASK, the rat homolog of a gene (LIN-2) required for vulval differentiation in Caenorhabditis elegans, is expressed in mammalian brain, but its function in neurons is unknown. CASK is distributed in a punctate somatodendritic pattern in neurons. By immunogold EM, CASK protein is concentrated in synapses, but is also present at nonsynaptic membranes and in intracellular compartments. This immunolocalization is consistent with biochemical studies showing the presence of CASK in soluble and synaptosomal membrane fractions and its enrichment in postsynaptic density fractions of rat brain. By yeast two-hybrid screening, a specific interaction was identified between the PDZ domain of CASK and the COOH terminal tail of syndecan-2, a cell surface heparan sulfate proteoglycan (HSPG). The interaction was confirmed by coimmunoprecipitation from heterologous cells. In brain, syndecan-2 localizes specifically at synaptic junctions where it shows overlapping distribution with CASK, consistent with an interaction between these proteins in synapses. Cell surface HSPGs can bind to extracellular matrix proteins, and are required for the action of various heparin-binding polypeptide growth/differentiation factors. The synaptic localization of CASK and syndecan suggests a potential role for these proteins in adhesion and signaling at neuronal synapses.

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