scholarly journals Molecular organization of the uvomorulin-catenin complex.

1992 ◽  
Vol 116 (4) ◽  
pp. 989-996 ◽  
Author(s):  
M Ozawa ◽  
R Kemler
Keyword(s):  
Gene Family ◽  
Cell Adhesion Molecule ◽  
Molecular Organization ◽  
Beta Catenin ◽  
Crucial Importance ◽  
Precursor Molecule ◽  
Dependent Cell ◽  
Single Complex ◽  
Alpha Beta ◽  
Biochemical Analyses

The Ca(2+)-dependent cell adhesion molecule uvomorulin is a member of the cadherin gene family. Its cytoplasmic region complexes with structurally defined proteins termed alpha-, beta-, and gamma-catenins. Here we show that A-CAM (N-cadherin), another member of this gene family, also associates with catenins suggesting that this complex formation may be a general property of the cadherins. For uvomorulin it has been found that this association with catenins is of crucial importance for the adhesive function, but little is known about the molecular organization of the uvomorulin-catenin complex. Using a combination of biochemical analyses we show that a single complex is composed of one molecule of uvomorulin, one or two molecules of beta-catenin, and one molecule of alpha-catenin. Furthermore, beta-catenin seems to interact more directly with uvomorulin. In pulse-chase experiments beta-catenin is already associated with the 135-kD uvomorulin precursor molecule but the assembly of the newly synthesized alpha-catenin into the complex is only detected around the time of endoproteolytic processing.

scholarly journals Cloning and expression of cDNA encoding a neural calcium-dependent cell adhesion molecule: its identity in the cadherin gene family.

1988 ◽  
Vol 106 (3) ◽  
pp. 873-881 ◽  
Author(s):  
K Hatta ◽  
A Nose ◽  
A Nagafuchi ◽  
M Takeichi
Keyword(s):  
Cell Adhesion ◽  
Amino Acid ◽  
Gene Family ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Cloning And Expression ◽  
Common Amino Acid ◽  
Neural Tissues ◽  
Dependent Cell ◽  
Cell Cell

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.

scholarly journals Affinity and Kinetic Analysis of L-selectin (CD62L) Binding to Glycosylation-dependent Cell-adhesion Molecule-1

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
Keyword(s):  
Cell Adhesion ◽  
Kinetic Analysis ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Dependent Cell ◽  
Cell Adhesion Molecule 1

Cell confluence regulates tyrosine phosphorylation of adherens junction components in endothelial cells

1997 ◽  
Vol 110 (17) ◽  
pp. 2065-2077 ◽  
Author(s):  
M.G. Lampugnani ◽  
M. Corada ◽  
P. Andriopoulou ◽  
S. Esser ◽  
W. Risau ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Tyrosine Phosphorylation ◽  
Adherens Junction ◽  
Cell Junctions ◽  
Molecular Organization ◽  
Beta Catenin ◽  
Cell Contacts ◽  
Cell Type Specific ◽  
Dynamic Structures ◽  
Cell Cell

In src- and ras-transformed cells, tyrosine phosphorylation of adherens junction (AJ) components is related to impairment of cell-cell adhesion. In this paper we report that in human endothelial cells (EC), tyrosine phosphorylation of AJ can be a physiological process regulated by cell density. Immunofluorescence analysis revealed that a phosphotyrosine (P-tyr) antibody could stain cell-cell junctions only in sparse or loosely confluent EC, while the staining was markedly reduced in tightly confluent cultures. This process was reversible, since on artificial wounding of EC monolayers, the cells at the migrating front reacquired P-tyr labelling at cell contacts. In EC, the major cadherin at intercellular AJ is the cell-type-specific VE-cadherin. We therefore analyzed whether this molecule was at least in part responsible for the changes in P-tyr content at cell junctions. Tyrosine phosphorylation of VE-cadherin, beta-catenin and p120, occurred in looser AJ, i.e. in recently confluent cells, and was notably reduced in tightly confluent cultures. Changes in P-tyr content paralleled changes in the molecular organization of AJ. VE-cadherin was mostly associated with beta-catenin and p120 in loose EC monolayers, while in long-confluent cells, these two catenins were largely replaced by plakoglobin. Inhibition of P-tyr phosphatases (PTPases) by PV markedly augmented the P-tyr content of VE-cadherin, which bound p120 and beta-catenin more efficiently, but not plakoglobin. Transfection experiments in CHO cells showed that p120 could bind to a VE-cadherin cytoplasmic region different from that responsible for beta-catenin binding, and PV stabilized this association. Overall these data indicate that endothelial AJ are dynamic structures that can be affected by the state of confluence of the cells. Tyrosine phosphorylation of VE-cadherin and its association to p120 and beta-catenin characterizes early cell contacts, while the formation of mature and cytoskeleton-connected junctions is accompanied by dephosphorylation and plakoglobin association.

scholarly journals Wnt-1 modulates cell-cell adhesion in mammalian cells by stabilizing beta-catenin binding to the cell adhesion protein cadherin

1994 ◽  
Vol 124 (5) ◽  
pp. 729-741 ◽  
Author(s):  
L Hinck ◽  
WJ Nelson ◽  
J Papkoff
Keyword(s):  
Cell Adhesion ◽  
Mammalian Cells ◽  
Signal Transduction Pathway ◽  
Beta Catenin ◽  
Adhesion Protein ◽  
Calcium Dependent ◽  
Cell Adhesion Protein ◽  
Segment Polarity ◽  
Dependent Cell ◽  
Cell Cell

Wnt-1 homologs have been identified in invertebrates and vertebrates and play important roles in cellular differentiation and organization. In Drosophila, the products of the segment polarity genes wingless (the Wnt-1 homolog) and armadillo participate in a signal transduction pathway important for cellular boundary formation in embryonic development, but functional interactions between the proteins are unknown. We have examined Wnt-1 function in mammalian cells in which armadillo (beta-catenin and plakoglobin) is known to bind to and regulate cadherin cell adhesion proteins. We show that Wnt-1 expression results in the accumulation of beta-catenin and plakoglobin. In addition, binding of beta-catenin to the cell adhesion protein, cadherin, is stabilized, resulting in a concomitant increase in the strength of calcium-dependent cell-cell adhesion. Thus, a consequence of the functional interaction between Wnt-1 and armadillo family members is the strengthening of cell-cell adhesion, which may lead to the specification of cellular boundaries.

Ultrastructural localization of E-cadherin and alpha-/beta-catenin in adenoid cystic carcinoma

1999 ◽  
Vol 35 (5) ◽  
pp. 423-431 ◽  
Author(s):  
Shibuya ◽  
Ri ◽  
Umeda ◽  
Yoshikawa ◽  
Masago ◽  
...  
Keyword(s):  
Adenoid Cystic Carcinoma ◽  
Ultrastructural Localization ◽  
Beta Catenin ◽  
Adenoid Cystic ◽  
Alpha Beta ◽  
E Cadherin
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