Cytoskeletal involvement in the sequential capping of rat thymocyte surface glycoproteins

1988 ◽  
Vol 89 (3) ◽  
pp. 309-319
Author(s):  
C.E. Turner ◽  
M.R. Newton ◽  
D.M. Shotton
Keyword(s):  
Monoclonal Antibodies ◽  
Cell Surface ◽  
Cytoskeletal Proteins ◽  
The Other ◽  
A Cell ◽  
Major Surface ◽  
Surface Glycoproteins

The independent capping of the three major rat thymocyte glycoproteins, the leucocyte-common (L-C) antigen, the leucocyte sialoglycoprotein (LSGP) and Thy-1, was investigated using specific monoclonal antibodies. The capping of each antigen did not require redistribution of the other major surface glycoproteins, and was accompanied by a partial co-capping of the cytoskeletal proteins fodrin and actin, but not of tubulin. A study of the ability of a cell that already possesses one glycoprotein cap to cap a second different glycoprotein showed that this was possible in all cases to varying degrees, the second cap always forming at the same position on the cell surface as the first. Colchicine failed to perturb this observed sequential capping polarity, indicating that microtubules did not direct this second capping event.

MONOCLONAL ANTIBODIES RECOGNISING PROTEINS OF THE OUTER AND INNER SURFACE OF THE PLATELET PLASMA MEMBRANE

1987 ◽  
Author(s):  
J M Wilkinson ◽  
N Hack ◽  
L I Thorsen ◽  
J A Thomas
Keyword(s):  
Monoclonal Antibodies ◽  
Plasma Membrane ◽  
Binding Protein ◽  
Cytoskeletal Proteins ◽  
Membrane Preparation ◽  
Actin Binding ◽  
Actin Binding Protein ◽  
Crossed Immunoelectrophoresis ◽  
Major Surface ◽  
Surface Glycoproteins

Platelet membrane preparations can be fractionated into two major subpopulations by free flow electrophoresis and these have been shown to correspond to the plasma membrane and the endoplasmic reticulum of the platelet. The plasma membrane fraction can be shown, by two-dimensional electrophoresis, to contain the major surface glycoproteins together with considerable amounts of actin and actin-associated proteins such as the 250 kDa actin-binding protein (filamin), P235 (talin), myosin, α-actinin and tropomyosin (Hack, N. … Crawford, N., Biochem. J. 222, 235 (1984). These cytoskeletal proteins are associated with the cytoplasmic face of the plasma membrane and probably interact with transmembrane glycoproteins. We have raised monoclonal antibodies to the purified plasma membrane preparation in order to investigate the nature of these glycoprotein-cytoskeletal interactions. In two fusion experiments, out of 804 tested, 104 hybrids secreted antibody to the membrane preparation and of these 24 were selected for further study. Initial assays were by ELISA using either the membrane preparation or whole fixed platelets as the target antigen. The specificity of the antibodies was investigated further by immunoblotting of SDS gels of total platelet proteins prepared under reducing and nonreducing conditions, by immunofluorescence, by immunohisto-chemistry and by crossed immunoelectrophoresis. The majority of the antibodies recognise major surface glycoproteins; of these, four bind to glycoprotein Ib under all conditions examined while another seven recognise the glycoprotein IIb/IIIa complex as detected by crossed immunoelectrophoresis. Three antibodies recognise the actin binding protein and these cross-react with the smooth muscle protein filamin in a number of different species. Further characterisation of these antibodies in both structural and functional terms will be presented.We are grateful to the Smith and Nephew Foundation for financial support for these studies

Cell surface glycoproteins of rabbit lymphocytes: Characterization with monoclonal antibodies

1984 ◽  
Vol 21 (1) ◽  
pp. 95-103 ◽  
Author(s):  
John M. Wilkinson ◽  
Debra L. Wetterskog ◽  
John A. Sogn ◽  
Thomas J. Kindt
Keyword(s):  
Monoclonal Antibodies ◽  
Cell Surface ◽  
Rabbit Lymphocytes ◽  
Cell Surface Glycoproteins ◽  
Surface Glycoproteins

scholarly journals Production of Monoclonal Antibodies Directed against Carbohydrate Moieties of Cell Surface Glycoproteins

1988 ◽  
Vol 79 (10) ◽  
pp. 1119-1129 ◽  
Author(s):  
Shigeyuki Fukui ◽  
Yoshito Numata ◽  
Akira Kurosaka ◽  
Hiroshi Kitagawa ◽  
Hiroshi Nakada ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Cell Surface ◽  
Cell Surface Glycoproteins ◽  
Surface Glycoproteins

scholarly journals The membrane change in En(a-) human erythrocytes. Absence of the major erythrocyte sialoglycoprotein

1976 ◽  
Vol 153 (2) ◽  
pp. 271-277 ◽  
Author(s):  
M J A Tanner ◽  
D J Anstee
Keyword(s):  
Cell Surface ◽  
Electrophoretic Mobility ◽  
Mammalian Cell ◽  
Band 3 ◽  
Human Erythrocytes ◽  
The Other ◽  
A Cells ◽  
Biochemical Function ◽  
Major Surface ◽  
Membrane Change

We investigated the membrane of En(a-) human erythrocytes as part of a study of the structure and biochemical function of the surface glycoproteins of the mammalian cell. 2. En(a-) erythrocytes were selected because they have more extensive changes at the cell surface than any other known erythrocyte variant. 3. Our results show that in En(a-) erythrocytes: (a) the major membrane sialoglycoprotein is lacking; (b) the other major membrane-penetrating glycoprotein (band 3) has an altered electrophoretic mobility. 4. The apparent clinical normality of En(a-) cells suggests that the change in band 3 may compensate for the loss of the membrane sialoglycoproteins. It is clear that a viable erythrocyte can exist despite the absence of one of its major surface components.

Monoclonal antibodies identify a cell-surface antigen associated with an activated cellular oncogene

Nature ◽  
1984 ◽  
Vol 312 (5994) ◽  
pp. 545-548 ◽  
Author(s):  
Jeffrey A. Drebin ◽  
David F. Stern ◽  
Victoria C. Link ◽  
Robert A. Weinberg ◽  
Mark I. Greene
Keyword(s):  
Monoclonal Antibodies ◽  
Cell Surface ◽  
Surface Antigen ◽  
Cell Surface Antigen ◽  
Cellular Oncogene ◽  
A Cell

A cell surface ELISA for the screening of monoclonal antibodies to antigens on viable cells in suspension

1994 ◽  
Vol 171 (1) ◽  
pp. 93-102 ◽  
Author(s):  
Roland Grunow ◽  
Massimo D'Apuzzo ◽  
Tony Wyss-Coray ◽  
Karin Frutig ◽  
Werner J. Pichler
Keyword(s):  
Monoclonal Antibodies ◽  
Cell Surface ◽  
Viable Cells ◽  
A Cell

scholarly journals Expression of a cell surface immobilization antigen during serotype transformation in Tetrahymena thermophila.

1985 ◽  
Vol 5 (8) ◽  
pp. 1925-1932 ◽  
Author(s):  
N E Williams ◽  
F P Doerder ◽  
A Ron
Keyword(s):  
Cell Surface ◽  
Microsomal Fraction ◽  
Cytochalasin B ◽  
Actinomycin D ◽  
Tetrahymena Thermophila ◽  
Temperature Shift ◽  
Surface Immobilization ◽  
Immobilization Antigen ◽  
A Cell ◽  
Major Surface

A temperature shift from 40 to 28 degrees C rapidly induced expression of a specific immobilization antigen at the cell surface in Tetrahymena thermophila. This transformation was inhibited by actinomycin D and cycloheximide but not by colchicine or cytochalasin B. The major surface antigen expressed at 28 degrees C in cells homozygous for the SerH3 allele was partially purified, and an antiserum against this preparation was raised in rabbits. Electrophoresis, immunoblot, and [35S]methionine incorporation studies are reported which support the conclusion that the H3 antigen is an acidic protein with an Mr of approximately 52,000 daltons. An induced synthesis of the H3 immobilization antigen was detected within 30 min after a shift from 40 to 28 degrees C. This protein appeared to be synthesized in the microsomal fraction and transferred without cleavage to the cell surface, where it was inserted first into nonciliated regions.

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