The 180-kD component of the neural cell adhesion molecule N-CAM is involved in cell-cell contacts and cytoskeleton-membrane interactions

1987 ◽  
Vol 250 (1) ◽  
pp. 227-236 ◽  
Author(s):  
G. Elisabeth Pollerberg ◽  
Keith Burridge ◽  
Keith E. Krebs ◽  
Steven R. Goodman ◽  
Melitta Schachner
Keyword(s):  
Cell Adhesion ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Neural Cell Adhesion Molecule ◽  
Neural Cell ◽  
Membrane Interactions ◽  
Cell Contacts ◽  
Neural Cell Adhesion ◽  
Cell Cell

The neural cell adhesion molecule (NCAM) as a regulator of cell-cell interactions

Science ◽  
1988 ◽  
Vol 240 (4848) ◽  
pp. 53-57 ◽  
Author(s):  
U Rutishauser ◽  
A Acheson ◽  
A. Hall ◽  
D. Mann ◽  
J Sunshine
Keyword(s):  
Cell Adhesion ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Neural Cell Adhesion Molecule ◽  
Neural Cell ◽  
Cell Interactions ◽  
Neural Cell Adhesion ◽  
Cell Cell

scholarly journals Clusters of neural cell adhesion molecule at sites of cell-cell contact.

1992 ◽  
Vol 116 (2) ◽  
pp. 449-463 ◽  
Author(s):  
R J Bloch
Keyword(s):  
Cell Adhesion ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Neural Cell Adhesion Molecule ◽  
Neural Cell ◽  
Extracellular Proteins ◽  
Cell Contact ◽  
L929 Cells ◽  
Neural Cell Adhesion ◽  
Cell Cell

I have examined the distribution of neural cell adhesion molecule (N-CAM) in cultured C2 myogenic cells and other cell lines to determine if N-CAM accumulates at sites of cell-cell contact. C2 cells growing in log phase display large clusters of neural cell adhesion molecule where they contact each other. These clusters are remarkably stable, do not form at cell-substrate contacts, and appear not to be enriched in a number of other cytoskeletal, membrane, or extracellular proteins. Thus, N-CAM clusters form preferentially in response to cell-cell contact and are specifically enriched in N-CAM. As C2 cultures mature and differentiate, clusters persist at contacts between aligning myoblasts and between myotubes, consistent with a role in myogenesis. N-CAM is also enriched at cell-cell contacts in cultures of PC12, NRK, and CHO cells. These cells have significant amounts of N-CAM as detected on immunoblots. Clusters are not seen in L929 cells, which do not have detectable amounts of N-CAM. Coculture of these cells with C2 cells results in the clustering of N-CAM at heterologous contacts between C2 cells and NRK, CHO, or PC12 cells, but not between C2 cells and L929 cells. These results suggest that N-CAM specifically accumulates where N-CAM-bearing cells contact one another. Clustering of N-CAM may be an important step in strengthening intercellular adhesion.

scholarly journals Identification of a peptide sequence involved in homophilic binding in the neural cell adhesion molecule NCAM.

1992 ◽  
Vol 118 (4) ◽  
pp. 937-949 ◽  
Author(s):  
Y Rao ◽  
X F Wu ◽  
J Gariepy ◽  
U Rutishauser ◽  
C H Siu
Keyword(s):  
Monoclonal Antibodies ◽  
Cell Adhesion ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Neural Cell Adhesion Molecule ◽  
Neural Cell ◽  
Peptide Sequence ◽  
Homophilic Binding ◽  
Neural Cell Adhesion ◽  
Cell Cell

The neural cell adhesion molecule NCAM is capable of mediating cell-cell adhesion via homophilic interactions. In this study, three strategies have been combined to identify regions of NCAM that participate directly in NCAM-NCAM binding: analysis of domain deletion mutations, mapping of epitopes of monoclonal antibodies, and use of synthetic peptides to inhibit NCAM activity. Studies on L cells transfected with NCAM mutant cDNAs using cell aggregation and NCAM-covasphere binding assays indicate that the third immunoglobulin-like domain is involved in homophilic binding. The epitopes of four monoclonal antibodies that have been previously shown to affect cell-cell adhesion mediated by NCAM were also mapped to domain 3. Overlapping hexapeptides were synthesized on plastic pins and assayed for binding with these monoclonal antibodies. One of them (PP) reacted specifically with the sequence KYSFNY. Synthetic oligopeptides containing the PP epitope were potent and specific inhibitors of NCAM binding activity. A substratum containing immobilized peptide conjugates also exhibited adhesiveness for neural retinal cells. Cell attachment was specifically inhibited by peptides that contained the PP-epitope and by anti-NCAM univalent antibodies. The shortest active peptide has the sequence KYSFNYDGSE, suggesting that this site is directly involved in NCAM homophilic interaction.

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