scholarly journals Extension of neurites on axons is impaired by antibodies against specific neural cell surface glycoproteins.

1987 ◽  
Vol 104 (2) ◽  
pp. 355-362 ◽  
Author(s):  
S Chang ◽  
F G Rathjen ◽  
J A Raper
Keyword(s):  
Cell Surface ◽  
Polyclonal Antibodies ◽  
Growth Cones ◽  
Neural Cell ◽  
Cell Surface Antigens ◽  
Vitro Assay ◽  
Fab Fragments ◽  
Cell Surface Glycoproteins ◽  
Surface Glycoproteins

We have developed an in vitro assay which measures the ability of growth cones to extend on an axonal substrate. Neurite lengths were compared in the presence or absence of monovalent antibodies against specific neural cell surface glycoproteins. Fab fragments of antibodies against the neural cell adhesion molecule, NCAM, have an insignificant effect on the lengths of neurites elongating on either an axonal substrate or a laminin substrate. Fab fragments of polyclonal antibodies against two new neural cell surface antigens, defined by mAb G4 and mAb F11, decrease the lengths of neurites elongating on an axonal substrate, but have no effect on the lengths of neurites elongating on a laminin substrate. G4 antigen is related to mouse L1, while F11 antigen appears to be distinct from all known neural cell surface glycoproteins. Our results suggest that the G4 and F11 antigens help to promote the extension of growth cones on axons.

scholarly journals Functionalized Magnetic Nanoparticles for the Detection and Quantitative Analysis of Cell Surface Antigen

2013 ◽  
Vol 2013 ◽  
pp. 1-9 ◽  
Author(s):  
Daryoush Shahbazi-Gahrouei ◽  
Mohammad Abdolahi ◽  
Sayyed Hamid Zarkesh-Esfahani ◽  
Sophie Laurent ◽  
Corine Sermeus ◽  
...  
Keyword(s):  
Magnetic Nanoparticles ◽  
Cell Surface ◽  
Surface Antigen ◽  
Cell Separation ◽  
Cell Surface Antigen ◽  
Cell Surface Antigens ◽  
Vitro Assay ◽  
Gold Standard Method ◽  
Magnetic Cell Separation

Cell surface antigens as biomarkers offer tremendous potential for early diagnosis, prognosis, and therapeutic response in a variety of diseases such as cancers. In this research, a simple, rapid, accurate, inexpensive, and easily available in vitro assay based on magnetic nanoparticles and magnetic cell separation principle was applied to identify and quantitatively analyze the cell surface antigen expression in the case of prostate cancer cells. Comparing the capability of the assay with flow cytometry as a gold standard method showed similar results. The results showed that the antigen-specific magnetic cell separation with antibody-coated magnetic nanoparticles has high potential for quantitative cell surface antigen detection and analysis.

Structural and functional studies on neural cell surface glycoproteins

1983 ◽  
Vol 1 (3) ◽  
pp. 199-199
Author(s):  
C. Goridis ◽  
M. Hirn ◽  
A. Liabeuf ◽  
G. Rougon ◽  
R. Sadoul
Keyword(s):  
Cell Surface ◽  
Neural Cell ◽  
Functional Studies ◽  
Cell Surface Glycoproteins ◽  
Surface Glycoproteins

Structural and functional studies on neural cell surface glycoproteins

1983 ◽  
Vol 1 (3) ◽  
pp. 222-222
Author(s):  
C. Goridis ◽  
M. Hirn ◽  
A. Liabeuf ◽  
G. Rougon ◽  
R. Sadoul
Keyword(s):  
Cell Surface ◽  
Neural Cell ◽  
Functional Studies ◽  
Cell Surface Glycoproteins ◽  
Surface Glycoproteins

scholarly journals Myelin-associated glycoprotein, a member of the L2/HNK-1 family of neural cell adhesion molecules, is involved in neuron-oligodendrocyte and oligodendrocyte-oligodendrocyte interaction.

1987 ◽  
Vol 105 (4) ◽  
pp. 1893-1899 ◽  
Author(s):  
M Poltorak ◽  
R Sadoul ◽  
G Keilhauer ◽  
C Landa ◽  
T Fahrig ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Cell Surface ◽  
Brain Regions ◽  
Neural Cell ◽  
Target Cells ◽  
Neural Cells ◽  
Fab Fragments ◽  
Neural Cell Adhesion ◽  
Myelin Associated Glycoprotein

A monoclonal antibody to the myelin-associated glycoprotein (MAG) was prepared and characterized to probe for the involvement of MAG in cell surface interactions among neural cells in vitro. The antibody reacts specifically with oligodendrocyte cell surface and myelin-rich brain regions as expected from previous investigations. Not all O4 antigen-positive oligodendrocytes express MAG in vitro. Fab fragments of the antibody interfere with neuron to oligodendrocyte and oligodendrocyte to oligodendrocyte adhesion, but not with oligodendrocyte to astrocyte adhesion. MAG-containing liposomes bind to the cell surfaces of the appropriate target cells by a mechanism that is specifically inhibitable by Fab fragments of monoclonal MAG antibodies, demonstrating that MAG is a neural cell adhesion molecule.

Protective antigens of bloodstage Plasmodium knowlesi parasites

1984 ◽  
Vol 307 (1131) ◽  
pp. 159-169 ◽  
Keyword(s):  
Monoclonal Antibodies ◽  
Cell Surface ◽  
Plasmodium Knowlesi ◽  
Surface Antigens ◽  
Red Cell ◽  
Cell Surface Antigens ◽  
Susceptible Host ◽  
Protective Antigens ◽  
Stage Of Development

The simian malaria Plasmodium knowlesi provides many favourable features as an experimental model; it can be grown in vivo or in vitro . Parasites of defined variant specificity and stage of development are readily obtained and both the natural host and a highly susceptible host are available for experimental infection and vaccination trials. Proteins synthesized by erythrocytic P. knowlesi parasites are characteristic of the developmental stage, as are the alterations that the parasite induces in the red cell surface. Erythrocytic merozoites are anatomically and biochemically complex, their surface alone is covered by at least eight distinct polypeptides. Immune serum from merozoite-immunized rhesus recognizes many parasite components, especially those synthesized by schizonts. All of the merozoite surface components and some of the schizont-infected red cell surface antigens are recognized by such immune sera. Rhesus monkeys rendered immune by repeated infection may by contrast recognize comparatively few antigens; a positive correlation was established for these ‘ naturally ’ immunized monkeys between protection and antibody directed against a 74000 molecular mass antigen. Im m unization with this purified antigen confers partial protection. O ther putative protective antigens have been identified by monoclonal antibodies that inhibit merozoite invasion of red cells in vitro . The antigens recognized by inhibitory monoclonal antibodies are synthesized exclusively by schizonts and are processed, at the time ofschizont rupture and merozoite release, to smaller molecules that are present on the merozoite surface. The multiplicity of protective antigens is clearly demonstrated by the fact that seven distinct merozoite surface antigens are recognized by three different inhibitory monoclonals. None of the protective antigens identified are variant or strain specific.

Recognition of collagen by fibroblasts through cell surface glycoproteins reactive with Phaseolus vulgaris agglutinin

1992 ◽  
Vol 101 (3) ◽  
pp. 625-633
Author(s):  
H. Asaga ◽  
K. Yoshizato
Keyword(s):  
Phaseolus Vulgaris ◽  
Cell Surface ◽  
Ricinus Communis ◽  
Specific Binding ◽  
Collagen Gel ◽  
Collagen Fibrils ◽  
Pokeweed Mitogen ◽  
Collagen Gel Contraction ◽  
Cell Surface Glycoproteins ◽  
Surface Glycoproteins

The role of glycochains of cell surface glycoproteins in the cell to collagen interaction was examined by studying the effect of lectins on the fibroblast-mediated collagen gel contraction. Lectins of Phaseolus vulgaris agglutinin (PHA), concanavalin A (ConA), lentil seed agglutinin (LCA), pea agglutinin (PSA), Ricinus communis agglutinin-60 (RCA), and wheat germ agglutinin (WGA) dose-dependently inhibited gel contraction, while lectins of mushroom agglutinin (ABA), peanut agglutinin (PNA), pokeweed mitogen (PWM), and soybean agglutinin (SBA) did not. Of these lectins, PHA seemed to be worthy of further analysis, because PHA, but not other lectins, inhibited spreading of fibroblasts on collagen fibrils but not on plastic or gelatin, suggesting that cell-surface glycoproteins responsive to the lectin are involved in the specific binding of fibroblasts to native collagen fibrils. The inhibitory effect of PHA-E4, an isolectin of PHA, was more intense than that of PHA-L4, another isolectin of PHA. The collagen gel contraction was also inhibited by tunicamycin and monensin in a concentration-dependent and reversible manner. These results strongly suggest that PHA-E4-reactive glycoproteins of the fibroblast surface play an important role in cell to collagen binding during the gel contraction. Five membrane proteins including beta 1 subunits of the integrin family were obtained by affinity chromatography with PHA-E4.

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