scholarly journals Homologous liver parenchymal cell-cell adhesion mediated by an endogenous lectin and its receptor

2010 ◽  
Vol 15 (2) ◽  
Author(s):  
Saswati Banerjee ◽  
Gopal Majumder
Keyword(s):  
Cell Adhesion ◽  
Cell Surface ◽  
Liver Cell ◽  
Cell Model ◽  
Direct Role ◽  
Lectin Receptor ◽  
A Cell ◽  
Parenchymal Cells ◽  
Cell Cell

AbstractMany studies have implicated cell-surface lectins in heterologous cell-cell adhesion, but little is known about the participation of lectins in cellular adhesion in homologous cells. Here, we show the development of a cell model for investigating the direct role of a cell-surface lectin in homologous cell-cell adhesion. Parenchymal cells were isolated from caprine liver using a perfusion buffer, and dispersed in a chemically defined modified Ringer’s solution. These cells undergo autoagglutination in the presence of Ca2+. The autoagglutinated cells can be dissociated specifically with D-galactose (50 mM), which also inhibits the liver cell autoagglutination event. The blood serum protein fetuin has no effect on liver cell autoagglutination, whereas desialylated fetuin (100 μM), with its terminal D-galactose residue, showed a high affinity for blocking the autoagglutination event. The data demonstrates the occurrence of a Ca2+-dependent D-galactose-specific lectin and a lectin receptor on the parenchymal cells. Furthermore, it shows that the observed autoagglutination event is caused by the interaction of the cell-surface lectin with its receptor on the neighbouring homologous cells. The data supports the view that homologous cell-cell contact in mammalian tissues is triggered by such lectin-receptor interaction and that the previously reported cell-surface adhesive proteins serve as a secondary force to strengthen cell adhesion. This cell model could be extremely useful for investigating the direct role of cell-surface lectin and its receptor in homologous cell adhesion in a variety of tissues under normal and pathological conditions.

scholarly journals The role of spectrin in cell adhesion and cell–cell contact

2019 ◽  
Vol 244 (15) ◽  
pp. 1303-1312 ◽  
Author(s):  
Beata Machnicka ◽  
Renata Grochowalska ◽  
Dżamila M Bogusławska ◽  
Aleksander F Sikorski
Keyword(s):  
Extracellular Matrix ◽  
Cell Adhesion ◽  
Cell Surface ◽  
Cell Biology ◽  
Membrane Integrity ◽  
Cell Contact ◽  
Surface Activities ◽  
New Findings ◽  
Cell Cell

Spectrins are proteins that are responsible for many aspects of cell function and adaptation to changing environments. Primarily the spectrin-based membrane skeleton maintains cell membrane integrity and its mechanical properties, together with the cytoskeletal network a support cell shape. The occurrence of a variety of spectrin isoforms in diverse cellular environments indicates that it is a multifunctional protein involved in numerous physiological pathways. Participation of spectrin in cell–cell and cell–extracellular matrix adhesion and formation of dynamic plasma membrane protrusions and associated signaling events is a subject of interest for researchers in the fields of cell biology and molecular medicine. In this mini-review, we focus on data concerning the role of spectrins in cell surface activities such as adhesion, cell–cell contact, and invadosome formation. We discuss data on different adhesion proteins that directly or indirectly interact with spectrin repeats. New findings support the involvement of spectrin in cell adhesion and spreading, formation of lamellipodia, and also the participation in morphogenetic processes, such as eye development, oogenesis, and angiogenesis. Here, we review the role of spectrin in cell adhesion and cell–cell contact.Impact statementThis article reviews properties of spectrins as a group of proteins involved in cell surface activities such as, adhesion and cell–cell contact, and their contribution to morphogenesis. We show a new area of research and discuss the involvement of spectrin in regulation of cell–cell contact leading to immunological synapse formation and in shaping synapse architecture during myoblast fusion. Data indicate involvement of spectrins in adhesion and cell–cell or cell–extracellular matrix interactions and therefore in signaling pathways. There is evidence of spectrin’s contribution to the processes of morphogenesis which are connected to its interactions with adhesion molecules, membrane proteins (and perhaps lipids), and actin. Our aim was to highlight the essential role of spectrin in cell–cell contact and cell adhesion.

scholarly journals Dual Role of Cell-Cell Adhesion In Tumor Suppression and Proliferation Due to Collective Mechanosensing

2019 ◽  
Author(s):  
Abdul N Malmi-Kakkada ◽  
Xin Li ◽  
Sumit Sinha ◽  
D. Thirumalai
Keyword(s):  
Cell Adhesion ◽  
Adhesion Strength ◽  
Feedback Loop ◽  
Local Stress ◽  
Feedback Mechanism ◽  
Tissue Growth ◽  
Inhibition Of Proliferation ◽  
A Cell ◽  
Cell Cell

AbstractIt is known that mechanical interactions couple a cell to its neighbors, enabling a feedback loop to regulate tissue growth. However, the interplay between cell-cell adhesion strength, local cell density and force fluctuations in regulating cell proliferation is poorly understood. Here, we show that spatial variations in the tumor growth rates, which depend on the location of cells within tissue spheroids, are strongly influenced by cell-cell adhesion. As the strength of the cell-cell adhesion increases, intercellular pressure initially decreases, enabling dormant cells to more readily enter into a proliferative state. We identify an optimal cell-cell adhesion regime where pressure on a cell is a minimum, allowing for maximum proliferation. We use a theoretical model to validate this novel collective feedback mechanism coupling adhesion strength, local stress fluctuations and proliferation. Our results predict the existence of a non-monotonic proliferation behavior as a function of adhesion strength, consistent with experimental results. Several experimental implications of the proposed role of cell-cell adhesion in proliferation are quantified, making our model predictions amenable to further experimental scrutiny. We show that the mechanism of contact inhibition of proliferation, based on a pressure-adhesion feedback loop, serves as a unifying mechanism to understand the role of cell-cell adhesion in proliferation.

scholarly journals Teratocarcinoma stem cell adhesion: the role of divalent cations and a cell surface lectin.

1983 ◽  
Vol 96 (6) ◽  
pp. 1532-1537 ◽  
Author(s):  
L B Grabel ◽  
M S Singer ◽  
G R Martin ◽  
S D Rosen
Keyword(s):  
Stem Cells ◽  
Stem Cell ◽  
Cell Adhesion ◽  
Cell Surface ◽  
Divalent Cations ◽  
Intercellular Adhesion ◽  
The Other ◽  
Calcium Dependent ◽  
A Cell

We describe two additive systems of intercellular adhesion in teratocarcinoma stem cells (Nulli cell line). One component is divalent cation-dependent (Ca++ or Mg++) and the other involves a cell surface fucan/mannan-specific lectin, previously identified on stem cells by an erythrocyte rosetting assay. The existence of these two systems is inferred from the observation that reaggregation of stem cells was partially inhibited by the removal of divalent cations or by the presence of lectin inhibitors such as fucoidan, but reaggregation was completely blocked when the two conditions were combined. Our results are related to recent work describing a calcium-dependent system of intercellular adhesion in teratocarcinoma stem cells.

scholarly journals Transmembrane 4 superfamily protein CD151 (PETA-3) associates with β1 and αIIbβ3 integrins in haemopoietic cell lines and modulates cell–cell adhesion

1999 ◽  
Vol 338 (1) ◽  
pp. 61-70 ◽  
Author(s):  
Stephen FITTER ◽  
Paul M. SINCOCK ◽  
Corina N. JOLLIFFE ◽  
Leonie K. ASHMAN
Keyword(s):  
Cell Adhesion ◽  
Cell Surface ◽  
Cell Lines ◽  
K562 Cells ◽  
Surface Proteins ◽  
A Cell ◽  
Cell Type Specific ◽  
Co Precipitation ◽  
Transmembrane 4 Superfamily ◽  
Cell Cell

CD151 (PETA-3/SFA-1) is a member of the transmembrane 4 superfamily (TM4SF) of cell-surface proteins and is expressed abundantly both on the cell surface and in intracellular membranes by the haemopoietic cell lines M07e, HEL and K562. In the presence of mild detergent (CHAPS), CD151 co-immunoprecipitated with integrin α4β1, α5β1, α6β1 and αIIbβ3. The association of CD151 with α4β1 and α5β1 seemed to be constitutive, as it was not modified by treatment of M07e cells with cytokines that regulate integrin function by ‘inside-out ’ signalling. CD151 also associated with other tetraspans in an apparently cell-type-specific fashion, as defined by its co-precipitation with CD9, CD63 and CD81 from M07e cells, but not from K562 cells, which express similar levels of these proteins. F(ab´)2 fragments of monoclonal antibodies (mAbs) against CD151 caused homotypic adhesion of HEL and K562 cells that was dependent on energy and cytoskeletal integrity and was augmented in the presence of RGDS peptides. The adhesion was not blocked by function-inhibiting mAbs against β1 or β3 integrins, suggesting that cell–cell adhesion was not mediated by the binding of integrin to a cell-associated ligand. Furthermore, mAb CD151 did not affect adhesion of the cells to fibronectin, laminin, collagen or fibrinogen, which are ligands for α4β1, α5β1, α6β1 and αIIbβ3 integrins. Taken together, these results indicate that the ligation of CD151 does not induce the up-regulation of integrin avidity, but might act as a component of integrin signalling complexes.

Cadherin-mediated adhesion in pancreatic islet cells is modulated by a cell surface N-acetylgalactosaminylphosphotransferase

1992 ◽  
Vol 103 (4) ◽  
pp. 1235-1241 ◽  
Author(s):  
G.E. Bauer ◽  
J. Balsamo ◽  
J. Lilien
Keyword(s):  
Cell Adhesion ◽  
Cell Surface ◽  
Pancreatic Islet ◽  
Islet Cells ◽  
Pancreatic Islet Cells ◽  
Rinm5f Cells ◽  
Pancreatic Islet Cell ◽  
A Cell ◽  
Rat Pancreatic Islet ◽  
Cell Cell

Rat pancreatic islet cells and RINm5F cells, an islet derived cell line, have at their cell surface an N-acetylgalactosaminylphosphotransferase (GalNAcPTase) similar to that found at the surface of chick neural retina cells and at the rat neuromuscular junction. On islet cells and RINm5F cells the GalNAcPTase is stably associated with cadherin cell-cell adhesion molecules. The effect of antibodies directed against the GalNAcPTase on homophilic, cadherin mediated adhesion was analyzed by measuring their effect on adhesion of islet and RINm5F cells to an immobilized anti-cadherin antibody. In this experimental paradigm anti-GalNAcPtase antibodies completely inhibit cadherin mediated adhesion. Furthermore, cadherin and GalNAcPTase co-distribute in islet and non-islet tissue. We conclude that pancreatic islet cell-cell adhesion is cadherin mediated and under the control of a tightly associated, cell surface GalNAcPTase.

scholarly journals Replacement of the phospholipid-anchor in the contact site A glycoprotein of D. discoideum by a transmembrane region does not impede cell adhesion but reduces residence time on the cell surface

1994 ◽  
Vol 124 (1) ◽  
pp. 205-215 ◽  
Author(s):  
A Barth ◽  
A Müller-Taubenberger ◽  
P Taranto ◽  
G Gerisch
Keyword(s):  
Plasma Membrane ◽  
Cell Adhesion ◽  
Cell Surface ◽  
Transmembrane Region ◽  
Contact Site ◽  
A Cell ◽  
Internalization Rate ◽  
Actin Promoter ◽  
Wild Type Form

The contact site A (csA) glycoprotein of Dictyostelium discoideum, a cell adhesion molecule expressed in aggregating cells, is inserted into the plasma membrane by a ceramide-based phospholipid (PL) anchor. A carboxyterminal sequence of 25 amino acids of the primary csA translation product proved to contain the signal required for PL modification. CsA is known to be responsible for rapid, EDTA-resistant cohesion of cells in agitated suspensions. To investigate the role of the PL modification of this protein, the anchor was replaced by the transmembrane region and short cytoplasmic tail of another plasma membrane protein of D. discoideum. In cells transformed with appropriate vectors, PL-anchored or transmembrane csA was expressed under the control of an actin promoter during growth and development. The transmembrane form enabled the cells to agglutinate in the presence of shear forces, similar to the PL-anchored wild-type form. However, the transmembrane form was much more rapidly internalized and degraded. In comparison to other cell-surface glycoproteins of D. discoideum the internalization rate of the PL-anchored csA was extremely slow, most likely because of its exclusion from the clathrin-mediated pathway of pinocytosis. Thus, our results indicate that the phospholipid modification is not essential for the csA-mediated fast type of cell adhesion but guarantees long persistence of the protein on the cell surface.

scholarly journals p120 catenin associates with kinesin and facilitates the transport of cadherin–catenin complexes to intercellular junctions

2003 ◽  
Vol 163 (3) ◽  
pp. 547-557 ◽  
Author(s):  
Xinyu Chen ◽  
Shin-ichiro Kojima ◽  
Gary G. Borisy ◽  
Kathleen J. Green
Keyword(s):  
Cell Adhesion ◽  
Cell Surface ◽  
Deletion Mutant ◽  
Intercellular Junctions ◽  
Time Lapse ◽  
Small Gtpases ◽  
P120 Catenin ◽  
Time Lapse Imaging ◽  
Cell Cell

p120 catenin (p120) is a component of adherens junctions and has been implicated in regulating cadherin-based cell adhesion as well as the activity of Rho small GTPases, but its exact roles in cell–cell adhesion are unclear. Using time-lapse imaging, we show that p120-GFP associates with vesicles and exhibits unidirectional movements along microtubules. Furthermore, p120 forms a complex with kinesin heavy chain through the p120 NH2-terminal head domain. Overexpression of p120, but not an NH2-terminal deletion mutant deficient in kinesin binding, recruits endogenous kinesin to N-cadherin. Disruption of the interaction between N-cadherin and p120, or the interaction between p120 and kinesin, leads to a delayed accumulation of N-cadherin at cell–cell contacts during calcium-initiated junction reassembly. Our analyses identify a novel role of p120 in promoting cell surface trafficking of cadherins via association and recruitment of kinesin.

scholarly journals Keratin 19 maintains E-cadherin localization at the cell surface and stabilizes cell-cell adhesion of MCF7 cells

2021 ◽  
Vol 15 (1) ◽  
pp. 1-17
Author(s):  
Sarah Alsharif ◽  
Pooja Sharma ◽  
Karina Bursch ◽  
Rachel Milliken ◽  
Van Lam ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Cell Surface ◽  
Mcf7 Cells ◽  
Keratin 19 ◽  
E Cadherin ◽  
Cell Cell
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