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.

scholarly journals Large remodeling of the Myc-induced cell surface proteome in B cells and prostate cells creates new opportunities for immunotherapy

2021 ◽  
Vol 118 (4) ◽  
pp. e2018861118
Author(s):  
Wentao Chen ◽  
Kurt Yun Mou ◽  
Paige Solomon ◽  
Rahul Aggarwal ◽  
Kevin K. Leung ◽  
...  
Keyword(s):  
Cell Surface ◽  
B Cell ◽  
Cell Lines ◽  
Surface Proteins ◽  
Cell Type ◽  
Hematological Cancers ◽  
A Cell ◽  
Surface Proteome ◽  
The Impact ◽  
Cell Surface Proteome

MYC is a powerful transcription factor overexpressed in many human cancers including B cell and prostate cancers. Antibody therapeutics are exciting opportunities to attack cancers but require knowledge of surface proteins that change due to oncogene expression. To identify how MYC overexpression remodels the cell surface proteome in a cell autologous fashion and in different cell types, we investigated the impact of MYC overexpression on 800 surface proteins in three isogenic model cell lines either of B cell or prostate cell origin engineered to have high or low MYC levels. We found that MYC overexpression resulted in dramatic remodeling (both up- and down-regulation) of the cell surfaceome in a cell type-dependent fashion. We found systematic and large increases in distinct sets of >80 transporters including nucleoside transporters and nutrient transporters making cells more sensitive to toxic nucleoside analogs like cytarabine, commonly used for treating hematological cancers. Paradoxically, MYC overexpression also increased expression of surface proteins driving cell turnover such as TNFRSF10B, also known as death receptor 5, and immune cell attacking signals such as the natural killer cell activating ligand NCR3LG1, also known as B7-H6. We generated recombinant antibodies to these two targets and verified their up-regulation in MYC overexpression cell lines and showed they were sensitive to bispecific T cell engagers (BiTEs). Our studies demonstrate how MYC overexpression leads to dramatic bidirectional remodeling of the surfaceome in a cell type-dependent but functionally convergent fashion and identify surface targets or combinations thereof as possible candidates for cytotoxic metabolite or immunotherapy.

scholarly journals Folliculin regulates cell-cell adhesion, AMPK, and mTORC1 in a cell-type-specific manner in lung-derived cells

2014 ◽  
Vol 2 (8) ◽  
pp. e12107 ◽  
Author(s):  
Damir Khabibullin ◽  
Douglas A. Medvetz ◽  
Miguel Pinilla ◽  
Venkatesh Hariharan ◽  
Chenggang Li ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Cell Type ◽  
Specific Manner ◽  
A Cell ◽  
Cell Type Specific ◽  
Cell Cell

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 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 Identification of a Drosophila homologue of alpha-catenin and its association with the armadillo protein.

1993 ◽  
Vol 121 (5) ◽  
pp. 1133-1140 ◽  
Author(s):  
H Oda ◽  
T Uemura ◽  
K Shiomi ◽  
A Nagafuchi ◽  
S Tsukita ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Cell Lines ◽  
Chromosome Band ◽  
Cell Contact ◽  
Beta Catenin ◽  
Contact Sites ◽  
Adhesion System ◽  
A Cell ◽  
Drosophila Embryos ◽  
Cell Cell

The cadherin cell adhesion system plays a central role in cell-cell adhesion in vertebrates, but its homologues are not identified in the invertebrate. alpha-Catenins are a group of proteins associated with cadherins, and this association is crucial for the cadherins' function. Here, we report the cloning of a Drosophila alpha-catenin gene by low stringent hybridization with a mouse alpha E-catenin probe. Isolated cDNAs encoded a 110-kD protein with 60% identity to mouse alpha E-catenin, and this protein was termed D alpha-catenin. The gene of this protein was located at the chromosome band 80B. Immunostaining analysis using a mAb to D alpha-catenin revealed that it was localized to cell-cell contact sites, expressed throughout development and present in a wide variety of tissues. When this protein was immunoprecipitated from detergent extracts of Drosophila embryos or cell lines, several proteins co-precipitated. These included the armadillo product which was known to be a Drosophila homologue of beta-catenin, another cadherin-associated protein in vertebrates, and a 150-kD glycoprotein. These results strongly suggest that Drosophila has a cell adhesion machinery homologous to the vertebrate cadherin-catenin system.

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

scholarly journals SurfaceGenie: a web-based application for prioritizing cell-type-specific marker candidates

2020 ◽  
Vol 36 (11) ◽  
pp. 3447-3456 ◽  
Author(s):  
Matthew Waas ◽  
Shana T Snarrenberg ◽  
Jack Littrell ◽  
Rachel A Jones Lipinski ◽  
Polly A Hansen ◽  
...  
Keyword(s):  
Cell Surface ◽  
Specific Surface ◽  
Web Application ◽  
Rank Order ◽  
Surface Proteins ◽  
Supplementary Information ◽  
Live Cells ◽  
Specific Marker ◽  
Cell Type ◽  
Cell Type Specific

Abstract Motivation Cell-type-specific surface proteins can be exploited as valuable markers for a range of applications including immunophenotyping live cells, targeted drug delivery and in vivo imaging. Despite their utility and relevance, the unique combination of molecules present at the cell surface are not yet described for most cell types. A significant challenge in analyzing ‘omic’ discovery datasets is the selection of candidate markers that are most applicable for downstream applications. Results Here, we developed GenieScore, a prioritization metric that integrates a consensus-based prediction of cell surface localization with user-input data to rank-order candidate cell-type-specific surface markers. In this report, we demonstrate the utility of GenieScore for analyzing human and rodent data from proteomic and transcriptomic experiments in the areas of cancer, stem cell and islet biology. We also demonstrate that permutations of GenieScore, termed IsoGenieScore and OmniGenieScore, can efficiently prioritize co-expressed and intracellular cell-type-specific markers, respectively. Availability and implementation Calculation of GenieScores and lookup of SPC scores is made freely accessible via the SurfaceGenie web application: www.cellsurfer.net/surfacegenie. Contact [email protected] Supplementary information Supplementary data are available at Bioinformatics online.

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