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)

Effects of polystyrene surface chemistry on the biological activity of solid phase fibronectin and vitronectin, analysed with monoclonal antibodies

1993 ◽  
Vol 104 (3) ◽  
pp. 793-803 ◽  
Author(s):  
P.A. Underwood ◽  
J.G. Steele ◽  
B.A. Dalton
Keyword(s):  
Monoclonal Antibodies ◽  
Cell Adhesion ◽  
Solid Phase ◽  
Divalent Cations ◽  
Biological Activities ◽  
Optimal Growth ◽  
Cell Types ◽  
Cell Binding ◽  
Urea Treatment ◽  
Bhk Cells

The conformation and biological activities of fibronectin (FN) and vitronectin (VN) coated on different plastic surfaces were investigated using cell adhesion and a panel of domain-specific monoclonal antibodies (mAbs). The adhesion of BHK fibroblasts was markedly better on FN coated on hydrophilic tissue culture polystyrene (TCPS) than on hydrophobic, untreated polystyrene (PS). mAbs A17 and 3E3, which inhibit the binding of BHK cells to the RGD-containing sequence within the cell binding region of FN, also bound preferentially to FN on TCPS. In contrast, two anti-FN mAbs, which have no effect on cell adhesion (A35 and A3), bound preferentially to the conformation of FN on the more hydrophobic PS. Mouse melanoma cells utilise an additional cell-binding site in the Hep II domain of FN and their preference for FN coated on TCPS was less marked than that of BHK cells. This reduced preference was again mimicked by the binding of a mAb, A32, which inhibits the binding of B16 cells to the Hep II domain of FN. In contrast, BHK cell adhesion to VN did not display a preference for TCPS over PS. The cell-binding activity of adsorbed VN was matched by the binding of a cell adhesion-inhibitory mAb, A18, which, unlike mAbs A17 and A32, displayed slightly increased binding to VN coated on PS, rather than TCPS. When the denaturating effect of coating FN and VN to PS in the presence of urea was investigated, similar correlations between BHK cell adhesion and the binding of inhibitory mAbs were observed. Urea treatment of FN significantly reduced both BHK cell adhesion and the binding of both cell adhesion-inhibitory mAbs, whereas the binding of A35 and A3 was unaffected. There was no significant effect of urea treatment of VN upon either BHK cell adhesion or mAb binding. A larger panel of anti-FN mAbs was used, together with the anti-VN mAbs, to determine whether there were differences in mAb recognition of FN and VN adsorbed on three different brands of TCPS. The mAbs segregated into four reactivity patterns, of which A17, A32, A35 and A18 respectively were representative. Significant differences were observed in mAb recognition of FN and VN adsorbed to different brands of TCPS. These may reflect differences in the ability of these surfaces to support optimal growth of different cell types. The effect of divalent cations upon adsorbed FN and VN was also investigated.(ABSTRACT TRUNCATED AT 400 WORDS)

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 Calcium-dependent cell-cell adhesion molecules common to hepatocytes and teratocarcinoma stem cells.

1983 ◽  
Vol 97 (3) ◽  
pp. 944-948 ◽  
Author(s):  
S I Ogou ◽  
C Yoshida-Noro ◽  
M Takeichi
Keyword(s):  
Stem Cells ◽  
Cell Adhesion ◽  
Cell Types ◽  
Surface Proteins ◽  
Calcium Dependent ◽  
Molecular Weights ◽  
Teratocarcinoma Cells ◽  
Dependent Cell ◽  
Molecular Constitution ◽  
Cell Cell

The molecules involved in Ca2+-dependent cell-cell adhesion systems (CDS) in mouse hepatocytes were characterized and compared with those in teratocarcinoma cells. Fab fragments of antibody raised against liver tissues (anti-liver) inhibited Ca2+-dependent aggregation of both liver and teratocarcinoma cells. A monoclonal antibody raised against teratocarcinoma CDS (ECCD-1) also inhibited the Ca2+-dependent aggregation of these two cell types equally. These antibodies induced disruption of cell-cell adhesion in monolayers of hepatocytes. Thus, CDS in these two cell types are not immunologically distinctive. Immunochemical analyses with these antibodies showed that CDS in both hepatocytes and teratocarcinoma cells involved at least two classes of cell surface proteins with molecular weights of 124,000 and 104,000. ECCD-1 selectively bound to hepatocytes but not to fibroblastic cells in liver cell cultures. Thus, the molecular constitution of CDS in hepatocytes and teratocarcinoma stem cells is identical. As ECCD-1 reacts with other classes of embryonic and fetal cells, the molecules identified here could have a major role in cell-cell adhesion in various tissues at any developmental stage of animals.

scholarly journals Structure-Based Virtual Screening Allows the Identification of Efficient Modulators of E-Cadherin-Mediated Cell–Cell Adhesion

2019 ◽  
Vol 20 (14) ◽  
pp. 3404 ◽  
Author(s):  
Andrea Dalle Vedove ◽  
Federico Falchi ◽  
Stefano Donini ◽  
Aurelie Dobric ◽  
Sebastien Germain ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Virtual Screening ◽  
Adherens Junction ◽  
Large Family ◽  
Calcium Dependent ◽  
Molecule Inhibitor ◽  
Dependent Cell ◽  
Cell Adhesion Proteins ◽  
E Cadherin ◽  
Cell Cell

Cadherins are a large family of transmembrane calcium-dependent cell adhesion proteins that orchestrate adherens junction formation and are crucially involved in tissue morphogenesis. Due to their important role in cancer development and metastasis, cadherins can be considered attractive targets for drug discovery. A recent crystal structure of the complex of a cadherin extracellular portion and a small molecule inhibitor allowed the identification of a druggable interface, thus providing a viable strategy for the design of cadherin dimerization modulators. Here, we report on a structure-based virtual screening approach that led to the identification of efficient and selective modulators of E-cadherin-mediated cell–cell adhesion. Of all the putative inhibitors that were identified and experimentally tested by cell adhesion assays using human pancreatic tumor BxPC-3 cells expressing both E-cadherin and P-cadherin, two compounds turned out to be effective in inhibiting stable cell–cell adhesion at micromolar concentrations. Moreover, at the same concentrations, one of them also showed anti-invasive properties in cell invasion assays. These results will allow further development of novel and selective cadherin-mediated cell–cell adhesion modulators for the treatment of a variety of cadherin-expressing solid tumors and for improving the efficiency of drug delivery across biological barriers.

The Superfamily of Cadherins: Calcium-Dependent Cell Adhesion Receptors

2011 ◽  
Author(s):  
Thomas Ahrens ◽  
Jörg Stetefeld ◽  
Daniel Häussinger ◽  
Jürgen Engel
Keyword(s):  
Cell Adhesion ◽  
Adhesion Receptors ◽  
Calcium Dependent ◽  
Dependent Cell

Characterization of the interactions of alpha-catenin with alpha-actinin and beta-catenin/plakoglobin

1997 ◽  
Vol 110 (8) ◽  
pp. 1013-1022 ◽  
Author(s):  
J.E. Nieset ◽  
A.R. Redfield ◽  
F. Jin ◽  
K.A. Knudsen ◽  
K.R. Johnson ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Protein Interactions ◽  
Beta Catenin ◽  
Protein Protein Interactions ◽  
Yeast Two Hybrid ◽  
Calcium Dependent ◽  
Cytoplasmic Proteins ◽  
Dependent Cell ◽  
Two Hybrid ◽  
Cell Cell

Cadherins are calcium-dependent, cell surface glycoproteins involved in cell-cell adhesion. To function in cell-cell adhesion, the transmembrane cadherin molecule must be associated with the cytoskeleton via cytoplasmic proteins known as catenins. Three catenins, alpha-catenin, beta-catenin and gamma-catenin (also known as plakoglobin), have been identified. beta-catenin or plakoglobin is associated directly with the cadherin; alpha-catenin binds to beta-catenin/plakoglobin and serves to link the cadherin/catenin complex to the actin cytoskeleton. The domains on the cadherin and betacatenin/plakoglobin that are responsible for protein-protein interactions have been mapped. However, little is known about the molecular interactions between alpha-catenin and beta-catenin/plakoglobin or about the interactions between alpha-catenin and the cytoskeleton. In this study we have used the yeast two-hybrid system to map the domains on alpha-catenin that allow it to associate with beta-catenin/plakoglobin and with alpha-actinin. We also identify a region on alpha-actinin that is responsible for its interaction with alpha-catenin. The yeast two-hybrid data were confirmed with biochemical studies.

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