Identification of mammalian and invertebrate analogues of the avian calcium-dependent cell adhesion protein N-cadherin with syntheticpeptide directed antibodies against a conserved cytoplasmic domain

1990 ◽  
Vol 172 (1) ◽  
pp. 313-320 ◽  
Author(s):  
Laura A. Lagunowich ◽  
Larry A. Donoso ◽  
Gerald B. Grunwald
Keyword(s):  
Cell Adhesion ◽  
Cytoplasmic Domain ◽  
Adhesion Protein ◽  
Calcium Dependent ◽  
Cell Adhesion Protein ◽  
Dependent Cell

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.

scholarly journals Desmosomal glycoproteins 2 and 3 (desmocollins) show N-terminal similarity to calcium-dependent cell-cell adhesion molecules

1990 ◽  
Vol 97 (2) ◽  
pp. 239-246
Author(s):  
J.L. Holton ◽  
T.P. Kenny ◽  
P.K. Legan ◽  
J.E. Collins ◽  
J.N. Keen ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Cell Adhesion ◽  
Intercellular Space ◽  
Solid Phase ◽  
Rabbit Antiserum ◽  
High Titre ◽  
Polyclonal Antiserum ◽  
Keyhole Limpet Haemocyanin ◽  
Calcium Dependent ◽  
Dependent Cell

The N-terminal sequence of a mixture of desmosomal glycoproteins 2 and 3 (dg2/3, desmocollins) from bovine nasal epidermis, prepared by electro-elution from polyacrylamide gels, was determined by solid-phase Edman degradation. A sequence of 23 amino acids was obtained. This showed 43% identity with that of the N terminus of the calcium-dependent cell adhesion molecule, N-cadherin. A lesser degree of identity with other members of the cadherin-uvomorulin-L-CAM family was also found. In order to confirm that the sequence was derived from the dg2/3 molecules a rabbit antiserum was raised against a synthetic peptide corresponding to the sequence, conjugated to keyhole limpet haemocyanin (KLH). The antiserum obtained showed high (titre) activity against both the peptide and KLH in ELISA. Each activity could be specifically adsorbed with the appropriate ligand. The antiserum reacted specifically with both dg2 and dg3 of bovine nasal epidermis on immunoblots, this binding was blocked by the N-terminal peptide but was unaffected by KLH. The identity of dg2 and -3 in these preparations was confirmed by immunoblotting with two monoclonal antibodies and one polyclonal antiserum raised against the whole molecules. The N-terminal peptide antiserum was shown to bind to the intercellular space of desmosome profiles by immunoelectron microscopy on ultra-thin frozen sections. One of the two monoclonal antibodies (07–4D) also reacted with the desmosomal intercellular space. dg2 and -3 were shown by Staphylococcus aureus V8 protease digestion to have identical one-dimensional peptide maps. Both the N-terminal antiserum and 07–4D reacted with a V8 fragment of 19,000 Mr derived from dg2 and dg3.(ABSTRACT TRUNCATED AT 250 WORDS)

Antisense RNA inactivation of gene expression of a cell-cell adhesion protein (gp64) in the cellular slime mold Polysphondylium pallidum

1996 ◽  
Vol 109 (5) ◽  
pp. 1009-1016
Author(s):  
S. Funamoto ◽  
H. Ochiai
Keyword(s):  
Gene Expression ◽  
Cell Adhesion ◽  
Antisense Rna ◽  
Resistant Cell ◽  
Cell Contact ◽  
Cellular Slime Mold ◽  
Adhesion Protein ◽  
Cell Adhesion Protein ◽  
Polysphondylium Pallidum ◽  
Cell Cell

The gp64 protein of Polysphondylium pallidum has been shown to mediate EDTA-stable cell-cell adhesion. To explore the functional role of gp64, we made an antisense RNA expression construct designed to prevent the gene expression of gp64; the construct was introduced into P. pallidum cells and the transformants were characterised. The antisense RNA-expressing clone L3mc2 which had just been harvested at the growth phase tended to re-form in aggregates smaller in size than did the parental cells in either the presence or absence of 10 mM EDTA. In contrast, 6.5-hour starved L3mc2 cells remained considerably dissociated from each other after 5 minutes gyrating, although aggregation gradually increased by 50% during a further 55 minutes gyrating in the presence of 10 mM EDTA. Correspondingly, L3mc2 lacked specifically the cell-cell adhesion protein, gp64. We therefore conclude that the gp64 protein is involved in forming the EDTA-resistant cell-cell contact. In spite of the absence of gp64, L3mc2 exhibited normal developmental processes, a fact which demonstrates that another cell-cell adhesion system exists in the development of Polysphondylium. This is the first report in which an antisense RNA technique was successfully applied to Polysphondylium.

scholarly journals Developmental expression patterns of Beta-ig (βIG-H3) and its function as a cell adhesion protein

2003 ◽  
Vol 120 (8) ◽  
pp. 851-864 ◽  
Author(s):  
Jill W. Ferguson ◽  
Michelle F. Mikesh ◽  
Esther F. Wheeler ◽  
Richard G. LeBaron
Keyword(s):  
Cell Adhesion ◽  
Expression Patterns ◽  
Developmental Expression ◽  
Adhesion Protein ◽  
Cell Adhesion Protein ◽  
A Cell

scholarly journals Human tumour-associated cell adhesion protein MN/CA IX: identification of M75 epitope and of the region mediating cell adhesion

2000 ◽  
Vol 82 (11) ◽  
pp. 1808-1813 ◽  
Author(s):  
J Závada ◽  
Z Závadová ◽  
J Pastorek ◽  
Z Biesová ◽  
J Jez˘ek ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Human Tumour ◽  
Adhesion Protein ◽  
Cell Adhesion Protein ◽  
Ca Ix
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