Cell adhesion on chiral surface: The role of protein adsorption

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.

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Faculty Opinions recommendation of Addressing the role of cell adhesion in tumor cell dormancy.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1057729.509642 ◽

2006 ◽

Author(s):

Anthony D Ho

Keyword(s):

Cell Adhesion ◽

Tumor Cell ◽

Cell Dormancy

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Role of association on protein adsorption isotherms

Journal of Chromatography A ◽

10.1016/s0021-9673(01)93202-9 ◽

1989 ◽

Vol 482 (1) ◽

pp. 1-12 ◽

Cited By ~ 29

Author(s):

R. Blanco ◽

A. Arai ◽

N. Grinberg ◽

M. Yarmush ◽

B.L. Karger

Keyword(s):

Protein Adsorption ◽

Adsorption Isotherms

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The role of dermatopontin in cell adhesion in bovine placenta during early-mid pregnancy and parturition – pilot study

Theriogenology ◽

10.1016/j.theriogenology.2021.05.014 ◽

2021 ◽

Author(s):

Jacek Wawrzykowski ◽

Monika Jamioł ◽

Marta Kankofer

Keyword(s):

Cell Adhesion ◽

Pilot Study ◽

Bovine Placenta

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The oncogenic role of the cerebral endothelial cell adhesion molecule (CERCAM) in bladder cancer cells in vitro and in vivo

Cancer Medicine ◽

10.1002/cam4.3955 ◽

2021 ◽

Author(s):

Yali Zuo ◽

Xiaoliang Xu ◽

Minfeng Chen ◽

Lin Qi

Keyword(s):

Bladder Cancer ◽

Cell Adhesion ◽

Endothelial Cell ◽

Adhesion Molecule ◽

Cell Adhesion Molecule ◽

Bladder Cancer Cells ◽

Endothelial Cell Adhesion

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The role of adsorbed fibrinogen in platelet adhesion to polyurethane surfaces: A comparison of surface hydrophobicity, protein adsorption, monoclonal antibody binding, and platelet adhesion

Journal of Biomedical Materials Research Part A ◽

10.1002/jbm.a.30381 ◽

2005 ◽

Vol 74A (4) ◽

pp. 722-738 ◽

Cited By ~ 144

Author(s):

Yuguang Wu ◽

Felix I. Simonovsky ◽

Buddy D. Ratner ◽

Thomas A. Horbett

Keyword(s):

Monoclonal Antibody ◽

Protein Adsorption ◽

Platelet Adhesion ◽

Surface Hydrophobicity ◽

Antibody Binding ◽

Monoclonal Antibody Binding

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Serine and Threonine Phosphorylation of the Paxillin LIM Domains Regulates Paxillin Focal Adhesion Localization and Cell Adhesion to Fibronectin

Molecular Biology of the Cell ◽

10.1091/mbc.9.7.1803 ◽

1998 ◽

Vol 9 (7) ◽

pp. 1803-1816 ◽

Cited By ~ 91

Author(s):

Michael C. Brown ◽

Joseph A. Perrotta ◽

Christopher E. Turner

Keyword(s):

Cell Adhesion ◽

Focal Adhesion ◽

Binding Sites ◽

Protein Localization ◽

Model System ◽

Lim Domain ◽

Amino Terminal ◽

Lim Domains ◽

Inside Out

We have previously shown that the LIM domains of paxillin operate as the focal adhesion (FA)-targeting motif of this protein. In the current study, we have identified the capacity of paxillin LIM2 and LIM3 to serve as binding sites for, and substrates of serine/threonine kinases. The activities of the LIM2- and LIM3-associated kinases were stimulated after adhesion of CHO.K1 cells to fibronectin; consequently, a role for LIM domain phosphorylation in regulating the subcellular localization of paxillin after adhesion to fibronectin was investigated. An avian paxillin-CHO.K1 model system was used to explore the role of paxillin phosphorylation in paxillin localization to FAs. We found that mutations of paxillin that mimicked LIM domain phosphorylation accelerated fibronectin-induced localization of paxillin to focal contacts. Further, blocking phosphorylation of the LIM domains reduced cell adhesion to fibronectin, whereas constitutive LIM domain phosphorylation significantly increased the capacity of cells to adhere to fibronectin. The potentiation of FA targeting and cell adhesion to fibronectin was specific to LIM domain phosphorylation as mutation of the amino-terminal tyrosine and serine residues of paxillin that are phosphorylated in response to fibronectin adhesion had no effect on the rate of FA localization or cell adhesion. This represents the first demonstration of the regulation of protein localization through LIM domain phosphorylation and suggests a novel mechanism of regulating LIM domain function. Additionally, these results provide the first evidence that paxillin contributes to “inside-out” integrin-mediated signal transduction.

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