scholarly journals EMA: A developmentally regulated cell-surface glycoprotein of CNS neurons that is concentrated at the leading edge of growth cones

1992 ◽  
Vol 194 (4) ◽  
pp. 311-325 ◽  
Author(s):  
Nikki L. Baumrind ◽  
David Parkinson ◽  
Denise B. Wayne ◽  
John E. Heuser ◽  
Alan L. Pearlman
Keyword(s):  
Cell Surface ◽  
Leading Edge ◽  
Growth Cones ◽  
Surface Glycoprotein ◽  
Developmentally Regulated ◽  
Cell Surface Glycoprotein ◽  
Cns Neurons

scholarly journals A polymorphic, prespore-specific cell surface glycoprotein is present in the extracellular matrix of Dictyostelium discoideum.

1985 ◽  
Vol 5 (10) ◽  
pp. 2559-2566 ◽  
Author(s):  
W N Grant ◽  
D L Welker ◽  
K L Williams
Keyword(s):  
Extracellular Matrix ◽  
Cell Surface ◽  
Dictyostelium Discoideum ◽  
Genetic Relationships ◽  
Specific Protein ◽  
Surface Glycoprotein ◽  
Specific Cell ◽  
Developmentally Regulated ◽  
Cell Surface Glycoprotein ◽  
Specific Cell Surface

Polymorphisms of a major developmentally regulated prespore-specific protein (PsA) in Dictyostelium discoideum slugs are described. These polymorphisms allowed discrimination between PsA (found on the cell surface and in the extracellular matrix) and a similar extracellular but nonpolymorphic protein, ShA. The two proteins were also distinguished by their differing reactivities with a range of monoclonal antibodies and by their sensitivity to release from the sheath with cellulase. The results are discussed in terms of the molecular and genetic relationships between the cell surface and the extracellular matrix during development.

scholarly journals Redistribution of a major cell surface glycoprotein during cell movement.

1984 ◽  
Vol 99 (5) ◽  
pp. 1613-1623 ◽  
Author(s):  
K Jacobson ◽  
D O'Dell ◽  
B Holifield ◽  
T L Murphy ◽  
J T August
Keyword(s):  
Monoclonal Antibodies ◽  
Cell Surface ◽  
Cell Movement ◽  
Leading Edge ◽  
Surface Glycoprotein ◽  
Direct Immunofluorescence ◽  
Surface Distribution ◽  
Cell Surface Glycoprotein ◽  
Cell Functions ◽  
Motile Cells

The distribution in living cells of an 80,000-dalton major cell surface glycoprotein of murine fibroblasts has been studied by use of monoclonal antibodies. The presence of the molecule throughout the plasma membrane and on the substrate attached surface of the cell was demonstrated by immunofluorescence. Cell growth kinetics were not altered and the cells remained motile in the presence of the antibody. The uniform distribution of the direct immunofluorescence stain persisted for long periods (greater than 100 h), which indicates that the fluorescent monoclonal antibodies may be used to trace antigen surface distribution during cell functions. In motile cells, but not G0 or confluent cells, the degree of fluorescent staining decreased toward the leading edge; this gradient increased markedly during the time that the antibody was bound to the cells. However, the gradation was not seen with the lipid probe, dihexadecylindocarbocyanine. The antigen was "patched" only by the application of a second antibody directed to the rat monoclonal antibody and the relationships of these patches to the underlying cytoskeleton were characterized.

A polymorphic, prespore-specific cell surface glycoprotein is present in the extracellular matrix of Dictyostelium discoideum

1985 ◽  
Vol 5 (10) ◽  
pp. 2559-2566
Author(s):  
W N Grant ◽  
D L Welker ◽  
K L Williams
Keyword(s):  
Extracellular Matrix ◽  
Cell Surface ◽  
Dictyostelium Discoideum ◽  
Genetic Relationships ◽  
Specific Protein ◽  
Surface Glycoprotein ◽  
Specific Cell ◽  
Developmentally Regulated ◽  
Cell Surface Glycoprotein ◽  
Specific Cell Surface

Polymorphisms of a major developmentally regulated prespore-specific protein (PsA) in Dictyostelium discoideum slugs are described. These polymorphisms allowed discrimination between PsA (found on the cell surface and in the extracellular matrix) and a similar extracellular but nonpolymorphic protein, ShA. The two proteins were also distinguished by their differing reactivities with a range of monoclonal antibodies and by their sensitivity to release from the sheath with cellulase. The results are discussed in terms of the molecular and genetic relationships between the cell surface and the extracellular matrix during development.

Cloning of the gene encoding TROP-2, a cell-surface glycoprotein expressed by human carcinomas

1995 ◽  
Vol 62 (5) ◽  
pp. 610-618 ◽  
Author(s):  
Mara Fornaro ◽  
Roberta Dell' Arciprete ◽  
Manuela Stella ◽  
Cecilia Bucci ◽  
Michele Nutini ◽  
...  
Keyword(s):  
Cell Surface ◽  
Surface Glycoprotein ◽  
Gene Encoding ◽  
Cell Surface Glycoprotein ◽  
Human Carcinomas ◽  
A Cell
Sign in / Sign up

Export Citation Format

Share Document