scholarly journals A mouse carcinoembryonic antigen gene family member is a calcium-dependent cell adhesion molecule.

1991 ◽  
Vol 266 (1) ◽  
pp. 309-315 ◽  
Author(s):  
C Turbide ◽  
M Rojas ◽  
C P Stanners ◽  
N Beauchemin
1991 ◽  
Vol 113 (2) ◽  
pp. 429-436 ◽  
Author(s):  
J Balsamo ◽  
R Thiboldeaux ◽  
N Swaminathan ◽  
J Lilien

Embryonic chick neural retina cells have at their surface an N-Acetylgalactosaminylphosphotransferase (GalNAcPTase) which is associated with, and glycosylates, the calcium-dependent cell-cell adhesion molecule, N-cadherin (Balsamo, J., and J. Lilien. 1990. J. Biol. Chem. 265:2923-2928). In this manuscript, we demonstrate that antibodies directed against the GalNAcPTase, as well as anti-N-cadherin antibodies, are able to inhibit adhesion of chick neural retina cells to a cell monolayer, to immobilized N-cadherin, or to immobilized anti-N-cadherin antibody. These results indicate that anti-GalNAcPTase antibodies modulate the function of N-cadherin, interfering with the formation of N-cadherin-mediated adhesions. We also demonstrate that actin is associated with the N-cadherin/GalNAcPTase complex and that binding of anti-GalNAcPTase antibodies to intact cells results in dissociation of actin from the complex. We suggest that the GalNAcPTase modulates N-cadherin function by altering its interaction with the cytoskeleton.


1988 ◽  
Vol 106 (3) ◽  
pp. 873-881 ◽  
Author(s):  
K Hatta ◽  
A Nose ◽  
A Nagafuchi ◽  
M Takeichi

The neural cadherin (N-cadherin) is a Ca2+-dependent cell-cell adhesion molecule detected in neural tissues as well as in non-neural tissues. We report here the nucleotide sequence of the chicken N-cadherin cDNA and the deduced amino acid sequence. The sequence data suggest that N-cadherin has one transmembrane domain which divides the molecule into an extracellular and a cytoplasmic domain; the extracellular domain contains internal repeats of characteristic sequences. When the N-cadherin cDNA connected with virus promoters was transfected into L cells which have no endogenous N-cadherin, the transformants acquired the N-cadherin-mediated aggregating property, indicating that the cloned cDNA contained all information necessary for the cell-cell binding action of this molecule. We then compared the primary structure of N-cadherin with that of other molecules defined as cadherin subclasses. The results showed that these molecules contain common amino acid sequences throughout their entire length, which confirms our hypothesis that cadherins make a gene family.


1998 ◽  
Vol 273 (2) ◽  
pp. 763-770 ◽  
Author(s):  
Martin W. Nicholson ◽  
A. Neil Barclay ◽  
Mark S. Singer ◽  
Steven D. Rosen ◽  
P. Anton van der Merwe

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