scholarly journals Extracellular pressure stimulates tumor cell adhesion in vitro by paxillin activation

2006 ◽  
Vol 5 (9) ◽  
pp. 1169-1178 ◽  
Author(s):  
J. van der Voort van Zyp ◽  
W.C. Conway ◽  
D.H. Craig ◽  
N. van der Voort van Zyp ◽  
V. Thamilselvan ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Tumor Cell ◽  
Tumor Cell Adhesion

scholarly journals Identification and characterization of a tumor cell receptor for CSVTCG, a thrombospondin adhesive domain.

1993 ◽  
Vol 120 (2) ◽  
pp. 513-521 ◽  
Author(s):  
G P Tuszynski ◽  
V L Rothman ◽  
M Papale ◽  
B K Hamilton ◽  
J Eyal
Keyword(s):  
Cell Adhesion ◽  
Tumor Cell ◽  
Fluid Phase ◽  
Cell Receptor ◽  
Anion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Dependent Manner ◽  
Tumor Cell Adhesion ◽  
Reducing Conditions

We have previously shown that peptides derived from the thrombospondin sequence, CSVTCG, promoted tumor cell adhesion. To further investigate this observation, the CSVTCG-tumor cell adhesion receptor from A549 human lung adenocarcinoma cells was isolated and characterized. A single protein peak was isolated by CSVTCG affinity chromatography which also analyzed as a single peak by anion exchange chromatography. The purified protein had a pI of 4.7 and analyzed on SDS-gels as a single band of M(r) = 50,000 under nonreducing conditions and as two protein bands of M(r) = 50,000, and 60,000 under reducing conditions. Purified CSVTCG binding protein (CBP) bound either CSVTCG- or TSP-Sepharose but showed little interaction with either VCTGSC- or BSA-Sepharose. CBP was cell surface exposed. CSVTCG derivatized with [125I] Bolton-Hunter reagent was taken up by cells in a dose-dependent manner and the cell association was inhibited with a monospecific polyclonal anti-CBP antibody. Examination of the cell proteins crosslinked to labeled CSVTCG by SDS-gel electrophoresis revealed one band that comigrated with purified CPB. Using an in vitro binding assay, purified CBP bound mannose, galactose, and glucosamine-specific lectins. CBP bound TSP saturably and reversibly. The binding was Ca+2/Mg+2 ion dependent and inhibited with fluid phase TSP and anti-CBP. Little or no binding was observed on BSA, fibronectin, GRGES, and GRGDS. Heparin, but not lactose, inhibited binding. Anti-CBP IgG and anti-CSVTCG peptide IgG inhibited A549 cell spreading and adhesion on TSP but not on fibronectin and laminin. These results indicate that CBP and the CSVTCG peptide domain of TSP can mediate TSP-promoted tumor cell adhesion.

The inhibition of tumor cell adhesion on human mesothelial cells (HOMC) by phospholipids in vitro

2006 ◽  
Vol 391 (2) ◽  
pp. 96-101 ◽  
Author(s):  
M. Jansen ◽  
P. Lynen Jansen ◽  
J. Otto ◽  
T. Kirtil ◽  
S. Neuss ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Tumor Cell ◽  
Mesothelial Cells ◽  
Tumor Cell Adhesion

scholarly journals Candida albicans Increases Tumor Cell Adhesion to Endothelial Cells In Vitro: Intraspecific Differences and Importance of the Mannose Receptor

PLoS ONE ◽  
2013 ◽  
Vol 8 (1) ◽  
pp. e53584 ◽  
Author(s):  
Andoni Ramirez-Garcia ◽  
Beatriz Arteta ◽  
Ana Abad-Diaz-de-Cerio ◽  
Aize Pellon ◽  
Aitziber Antoran ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Candida Albicans ◽  
Cell Adhesion ◽  
Tumor Cell ◽  
Mannose Receptor ◽  
Tumor Cell Adhesion

Interleukin-1 increases tumor cell adhesion to endothelial cells through an RGD dependent mechanism: in vitro and in vivo studies

1990 ◽  
Vol 8 (1) ◽  
pp. 27-32 ◽  
Author(s):  
Davide Lauri ◽  
Maria-Cruz Bertomeu ◽  
F. William Orr ◽  
Eva Bastida ◽  
D. Sauder ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Cell Adhesion ◽  
Tumor Cell ◽  
Interleukin 1 ◽  
In Vivo Studies ◽  
Tumor Cell Adhesion ◽  
Dependent Mechanism

Platelet and Shear Rate Promote Tumor Cell Adhesion to Human Endothelial Extracellular Matrix - Absence of a Role for Platelet Cyclooxygenase

1989 ◽  
Vol 61 (03) ◽  
pp. 485-489 ◽  
Author(s):  
Eva Bastida ◽  
Lourdes Almirall ◽  
Antonio Ordinas
Keyword(s):  
Cell Adhesion ◽  
Shear Rate ◽  
Tumor Cell ◽  
Umbilical Vein ◽  
Blood Platelets ◽  
Flow Conditions ◽  
Tumor Cell Adhesion ◽  
Rate Dependent ◽  
Static Conditions

SummaryBlood platelets are thought to be involved in certain aspects of malignant dissemination. To study the role of platelets in tumor cell adherence to vascular endothelium we performed studies under static and flow conditions, measuring tumor cell adhesion in the absence or presence of platelets. We used highly metastatic human adenocarcinoma cells of the lung, cultured human umbilical vein endothelial cells (ECs) and extracellular matrices (ECM) prepared from confluent EC monolayers. Our results indicated that under static conditions platelets do not significantly increase tumor cell adhesion to either intact ECs or to exposed ECM. Conversely, the studies performed under flow conditions using the flat chamber perfusion system indicated that the presence of 2 × 105 pl/μl in the perfusate significantly increased the number of tumor cells adhered to ECM, and that this effect was shear rate dependent. The maximal values of tumor cell adhesion were obtained, in presence of platelets, at a shear rate of 1,300 sec-1. Furthermore, our results with ASA-treated platelets suggest that the role of platelets in enhancing tumor cell adhesion to ECM is independent of the activation of the platelet cyclooxygenase pathway.

scholarly journals Glycan-to-Glycan Binding: Molecular Recognition through Polyvalent Interactions Mediates Specific Cell Adhesion

Molecules ◽  
2021 ◽  
Vol 26 (2) ◽  
pp. 397
Author(s):  
Gradimir Misevic ◽  
Emanuela Garbarino
Keyword(s):  
Cell Adhesion ◽  
Plasma Membranes ◽  
Specific Cell ◽  
Cellular Interactions ◽  
New Paradigm ◽  
Tumor Cell Adhesion ◽  
Self Recognition ◽  
Structural And Functional Properties ◽  
Low Valent

Glycan-to-glycan binding was shown by biochemical and biophysical measurements to mediate xenogeneic self-recognition and adhesion in sponges, stage-specific cell compaction in mice embryos, and in vitro tumor cell adhesion in mammals. This intermolecular recognition process is accepted as the new paradigm accompanying high-affinity and low valent protein-to-protein and protein-to-glycan binding in cellular interactions. Glycan structures in sponges have novel species-specific sequences. Their common features are the large size >100 kD, polyvalency >100 repeats of the specific self-binding oligosaccharide, the presence of fucose, and sulfated and/or pyruvylated hexoses. These structural and functional properties, different from glycosaminoglycans, inspired their classification under the glyconectin name. The molecular mechanism underlying homophilic glyconectin-to-glyconectin binding relies on highly polyvalent, strong, and structure-specific interactions of small oligosaccharide motifs, possessing ultra-weak self-binding strength and affinity. Glyconectin localization at the glycocalyx outermost cell surface layer suggests their role in the initial recognition and adhesion event during the complex and multistep process. In mammals, Lex-to-Lex homophilic binding is structure-specific and has ultra-weak affinity. Cell adhesion is achieved through highly polyvalent interactions, enabled by clustering of small low valent structure in plasma membranes.

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