scholarly journals Genes for two calcium-dependent cell adhesion molecules have similar structures and are arranged in tandem in the chicken genome.

1991 ◽  
Vol 88 (24) ◽  
pp. 11545-11549 ◽  
Author(s):  
B. C. Sorkin ◽  
W. J. Gallin ◽  
G. M. Edelman ◽  
B. A. Cunningham
Keyword(s):  
Cell Adhesion ◽  
Adhesion Molecules ◽  
Cell Adhesion Molecules ◽  
Chicken Genome ◽  
Calcium Dependent ◽  
Dependent Cell

Calcium-dependent cell adhesion molecules

1989 ◽  
Vol 1 (5) ◽  
pp. 892-897 ◽  
Author(s):  
R. Kemler ◽  
M. Ozawa ◽  
M. Ringwald
Keyword(s):  
Cell Adhesion ◽  
Adhesion Molecules ◽  
Cell Adhesion Molecules ◽  
Calcium Dependent ◽  
Dependent Cell

scholarly journals Calcium-dependent cell-cell adhesion molecules (cadherins): subclass specificities and possible involvement of actin bundles.

1987 ◽  
Vol 105 (6) ◽  
pp. 2501-2510 ◽  
Author(s):  
S Hirano ◽  
A Nose ◽  
K Hatta ◽  
A Kawakami ◽  
M Takeichi
Keyword(s):  
Cell Adhesion ◽  
Adhesion Molecules ◽  
Cell Adhesion Molecules ◽  
Cell Types ◽  
Apical Region ◽  
Cell Sheets ◽  
Actin Bundles ◽  
Calcium Dependent ◽  
Dependent Cell ◽  
Cell Cell

Cadherins are a family of cell-cell adhesion molecules and are divided into subclasses with distinct adhesive specificities and tissue distribution. Here we examined the distribution of cadherins at contact sites between cells expressing the same or different cadherin subclasses. Each cadherin was concentrated at the boundary between cells expressing an identical cadherin subclass, irrespective of the cell types connected. However, such localization decreased or disappeared at the boundary between cells containing different cadherin subclasses. We also found that the localization of cadherins precisely coincided with that of actin bundles; both were detected at the apical region of cell sheets. This co-localization was retained even after cells were either treated with cytochalasin D or extracted with the detergent NP40. These results suggest that each cadherin subclass preferentially interacts with its own molecular type at intercellular boundaries, and that cadherin molecules may be associated with actin-based cytoskeletal elements.

scholarly journals Retinal patterning by Pax6-dependent cell adhesion molecules

2010 ◽  
Vol 70 (11) ◽  
pp. 764-780 ◽  
Author(s):  
Elisabeth Rungger-Brändle ◽  
Jürgen A. Ripperger ◽  
Kurt Steiner ◽  
Alain Conti ◽  
Ariane Stieger ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Adhesion Molecules ◽  
Cell Adhesion Molecules ◽  
Dependent Cell

scholarly journals A complex of Protocadherin-19 and N-cadherin mediates a novel mechanism of cell adhesion

2011 ◽  
Vol 195 (7) ◽  
pp. 1115-1121 ◽  
Author(s):  
Michelle R. Emond ◽  
Sayantanee Biswas ◽  
Cheasequah J. Blevins ◽  
James D. Jontes
Keyword(s):  
Cell Adhesion ◽  
Adhesion Molecules ◽  
Dominant Role ◽  
Cell Interactions ◽  
Homophilic Binding ◽  
Calcium Dependent ◽  
Classical Cadherins ◽  
Dependent Cell ◽  
Embryonic Morphogenesis ◽  
Cadherin Superfamily

During embryonic morphogenesis, adhesion molecules are required for selective cell–cell interactions. The classical cadherins mediate homophilic calcium-dependent cell adhesion and are founding members of the large and diverse cadherin superfamily. The protocadherins are the largest subgroup within this superfamily, yet their participation in calcium-dependent cell adhesion is uncertain. In this paper, we demonstrate a novel mechanism of adhesion, mediated by a complex of Protocadherin-19 (Pcdh19) and N-cadherin (Ncad). Although Pcdh19 alone is only weakly adhesive, the Pcdh19–Ncad complex exhibited robust adhesion in bead aggregation assays, and Pcdh19 appeared to play the dominant role. Adhesion by the Pcdh19–Ncad complex was unaffected by mutations that disrupt Ncad homophilic binding but was inhibited by a mutation in Pcdh19. In addition, the complex exhibited homophilic specificity, as beads coated with Pcdh19–Ncad did not intermix with Ncad- or Pcdh17–Ncad-coated beads. We propose a model in which association of a protocadherin with Ncad acts as a switch, converting between distinct binding specificities.

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