scholarly journals New insights in glycosphingolipid function: "glycosignaling domain," a cell surface assembly of glycosphingolipids with signal transducer molecules, involved in cell adhesion coupled with signaling

Glycobiology ◽  
1998 ◽  
Vol 8 (10) ◽  
pp. xi-xviii ◽  
Author(s):  
S.-i. Hakomori ◽  
K. Handa ◽  
K. Iwabuchi ◽  
S. Yamamura ◽  
A. Prinetti
Keyword(s):  
Cell Adhesion ◽  
Cell Surface ◽  
Signal Transducer ◽  
Surface Assembly ◽  
A Cell

scholarly journals Retention of a cell adhesion complex at the paranodal junction requires the cytoplasmic region of Caspr

2002 ◽  
Vol 157 (7) ◽  
pp. 1247-1256 ◽  
Author(s):  
Leora Gollan ◽  
Helena Sabanay ◽  
Sebastian Poliak ◽  
Erik O. Berglund ◽  
Barbara Ranscht ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Cell Adhesion ◽  
Cell Surface ◽  
Cell Adhesion Molecules ◽  
Cytoplasmic Domain ◽  
Short Sequence ◽  
Extracellular Region ◽  
A Cell ◽  
Adhesion Complex ◽  
Protein 4.1B

An axonal complex of cell adhesion molecules consisting of Caspr and contactin has been found to be essential for the generation of the paranodal axo-glial junctions flanking the nodes of Ranvier. Here we report that although the extracellular region of Caspr was sufficient for directing it to the paranodes in transgenic mice, retention of the Caspr–contactin complex at the junction depended on the presence of an intact cytoplasmic domain of Caspr. Using immunoelectron microscopy, we found that a Caspr mutant lacking its intracellular domain was often found within the axon instead of the junctional axolemma. We further show that a short sequence in the cytoplasmic domain of Caspr mediated its binding to the cytoskeleton-associated protein 4.1B. Clustering of contactin on the cell surface induced coclustering of Caspr and immobilized protein 4.1B at the plasma membrane. Furthermore, deletion of the protein 4.1B binding site accelerated the internalization of a Caspr–contactin chimera from the cell surface. These results suggest that Caspr serves as a “transmembrane scaffold” that stabilizes the Caspr/contactin adhesion complex at the paranodal junction by connecting it to cytoskeletal components within the axon.

Identification of a cell-surface glycoprotein mediating cell adhesion in EBV-immortalized normal B cells

1986 ◽  
Vol 38 (4) ◽  
pp. 539-547 ◽  
Author(s):  
Manuel Patarroyo ◽  
Patrick G. Beatty ◽  
Kenneth Nilsson ◽  
Carl G. Gahmberg
Keyword(s):  
Cell Adhesion ◽  
B Cells ◽  
Cell Surface ◽  
Surface Glycoprotein ◽  
Cell Surface Glycoprotein ◽  
A Cell

scholarly journals Teratocarcinoma stem cell adhesion: the role of divalent cations and a cell surface lectin.

1983 ◽  
Vol 96 (6) ◽  
pp. 1532-1537 ◽  
Author(s):  
L B Grabel ◽  
M S Singer ◽  
G R Martin ◽  
S D Rosen
Keyword(s):  
Stem Cells ◽  
Stem Cell ◽  
Cell Adhesion ◽  
Cell Surface ◽  
Divalent Cations ◽  
Intercellular Adhesion ◽  
The Other ◽  
Calcium Dependent ◽  
A Cell

We describe two additive systems of intercellular adhesion in teratocarcinoma stem cells (Nulli cell line). One component is divalent cation-dependent (Ca++ or Mg++) and the other involves a cell surface fucan/mannan-specific lectin, previously identified on stem cells by an erythrocyte rosetting assay. The existence of these two systems is inferred from the observation that reaggregation of stem cells was partially inhibited by the removal of divalent cations or by the presence of lectin inhibitors such as fucoidan, but reaggregation was completely blocked when the two conditions were combined. Our results are related to recent work describing a calcium-dependent system of intercellular adhesion in teratocarcinoma stem cells.

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