scholarly journals Measurement Systems for Cell Adhesive Forces

2015 ◽  
Vol 137 (2) ◽  
Author(s):  
Dennis W. Zhou ◽  
Andrés J. García
Keyword(s):  
Cell Adhesion ◽  
Temporal Dynamics ◽  
Cell Phenotype ◽  
Measurement Systems ◽  
Cell Matrix ◽  
Cell Adhesive ◽  
Cell Traction ◽  
A Cell ◽  
Adhesive Interactions ◽  
Adhesive Forces

Abstract Cell adhesion to the extracellular matrix (ECM) involves integrin receptor–ligand binding and clustering to form focal adhesion (FA) complexes, which mechanically link the cell’s cytoskeleton to the ECM and regulate fundamental cell signaling pathways. Although elucidation of the biochemical events in cell-matrix adhesive interactions is rapidly advancing, recent studies show that the forces underlying cell-matrix adhesive interactions are also critical to cell responses. Therefore, multiple measurement systems have been developed to quantify the spatial and temporal dynamics of cell adhesive forces, and these systems have identified how mechanical events influence cell phenotype and FA structure–function relationships under physiological and pathological settings. This review focuses on the development, methodology, and applications of measurement systems for probing (a) cell adhesion strength and (b) 2D and 3D cell traction forces.

scholarly journals Hyaluronate can function as a cell adhesion molecule and CD44 participates in hyaluronate recognition.

1990 ◽  
Vol 172 (1) ◽  
pp. 69-75 ◽  
Author(s):  
K Miyake ◽  
C B Underhill ◽  
J Lesley ◽  
P W Kincade
Keyword(s):  
Cell Adhesion ◽  
Stromal Cells ◽  
Divalent Cations ◽  
Cell Types ◽  
Lymphoid Cells ◽  
Hybridoma Cells ◽  
Antibody Treatment ◽  
A Cell ◽  
Adhesive Interactions ◽  
Potential Ligand

A cell adhesion model was previously used to select a series of monoclonal antibodies (mAbs), which were subsequently found to recognize CD44/Pgp-1. Interest in these reagents increased with the finding that they totally inhibited production of lymphoid or myeloid cells in long-term bone marrow cultures. Further investigation has now revealed that hyaluronate is a potential ligand for CD44 and that hyaluronate recognition accounts for the adhesion between B lineage hybridoma and stromal cells. The hybridoma cells adhered to hyaluronate-coated plastic wells as well as to monolayers of stromal cells. The adhesion in both cases was inhibited by treatment with hyaluronidases, and did not require divalent cations. Addition of exogenous hyaluronate also diminished binding of lymphoid cells to stromal cells. One of several mAbs to Pgp-1/CD44 was particularly effective at blocking these interactions. Since hyaluronate and Pgp-1/CD44 were present on both cell types, experiments were done to determine the cellular location of interacting molecules required for the adhesion process. Treatment of lymphoid cells with an anti-Pgp-1/CD44 antibody was more inhibitory than antibody treatment of the stromal cells. Conversely, hyaluronidase treatment of stromal cells reduced subsequent binding more than treatment of the lymphoid cells. Adhesive interactions that involve hyaluronate and CD44 could contribute to a number of cell recognition processes, including ones required for normal lympho-hemopoiesis.

scholarly journals Characterisation and assessment of electrospun Poly/hydroxyapatite nanofibres together with a cell adhesive for bone repair applications

2014 ◽  
Vol 59 (No. 10) ◽  
pp. 498-501 ◽  
Author(s):  
SY Heo ◽  
JW Seol ◽  
NS Kim
Keyword(s):  
Extracellular Matrix ◽  
Cell Adhesion ◽  
Bone Repair ◽  
Adhesion Test ◽  
Cell Adhesive ◽  
A Cell ◽  
Electrospun Nanofibres ◽  
Potential Use

In this study, we fabricated Poly(lactide-co-glycolide)/hydroxyapatite (PLGA/HAp) nanofibres using electrospinning and evaluated their potential use for bone repair applications. Analysis confirmed that the PLGA nanofibres were similar to the natural extracellular matrix and included HAp particles. Further, gelatin augmented the adhesion of electrospun nanofibres in the cell adhesion test. Therefore, electrospun PLGA/HAp nanofibres together with gelatin can be utilised for bone repair applications.  

scholarly journals Biological activities of peptides and peptide analogues derived from common sequences present in thrombospondin, properdin, and malarial proteins.

1992 ◽  
Vol 116 (1) ◽  
pp. 209-217 ◽  
Author(s):  
G P Tuszynski ◽  
V L Rothman ◽  
A H Deutch ◽  
B K Hamilton ◽  
J Eyal
Keyword(s):  
Cell Adhesion ◽  
Platelet Aggregation ◽  
Tumor Cell ◽  
Biological Activities ◽  
Type I ◽  
Cell Metastasis ◽  
Cell Adhesive ◽  
Tumor Cell Metastasis ◽  
Dependent Cell ◽  
Adhesive Interactions

Thrombospondin (TSP), a major platelet-secreted protein, has recently been shown to have activity in tumor cell metastasis, cell adhesion, and platelet aggregation. The type 1 repeats of TSP contain two copies of CSVTCG and one copy of CSTSCG, per each of the three polypeptide chains of TSP and show homology with peptide sequences found in a number of other proteins including properdin, malarial circumsporozoite, and a blood-stage antigen of Plasmodium falciparum. To investigate whether these common sequences functioned as a cell adhesive domain in TSP, we assessed the effect of peptides corresponding to these sequences and an antibody raised against one of these sequences, CSTSCG, in three biological assays which depend, in part, on the cell adhesive activity of TSP. These assays were TSP-dependent cell adhesion, platelet aggregation, and tumor cell metastasis. We found that a number of peptides homologous to CSVTCG promoted the adhesion of a variety of cells including mouse B16-F10 melanoma cells, inhibited platelet aggregation and tumor cell metastasis, whereas control peptides had no effect. Anti-CSTSCG, which specifically recognized TSP, inhibited TSP-dependent cell adhesion, platelet aggregation, and tumor cell metastasis, whereas control IgG had no effect. These results suggest that CSVTCG and CSTSCG present in the type I repeats function in the adhesive interactions of TSP that mediate cell adhesion, platelet aggregation, and tumor cell metastasis. Peptides, based on the structure of these repeats, may find wide application in the treatment of thrombosis and in the prevention of cancer spread.

scholarly journals Integrin-linked kinase tunes cell-cell and cell-matrix adhesions to regulate the switch between apoptosis and EMT downstream of TGFβ1

2021 ◽  
pp. mbc.E20-02-0092
Author(s):  
Ayse Nihan Kilinc ◽  
Siyang Han ◽  
Lena Barrett ◽  
Niroshan Anandasivam ◽  
Celeste M. Nelson
Keyword(s):  
Cell Adhesion ◽  
Epithelial Cells ◽  
Focal Adhesions ◽  
Cell Phenotype ◽  
High Cell ◽  
Potent Inducer ◽  
Mesenchymal Transition ◽  
Cell Matrix ◽  
Integrin Linked Kinase ◽  
Cell Cell

Epithelial-mesenchymal transition (EMT) is a morphogenetic process that endows epithelial cells with migratory and invasive potential. Mechanical and chemical signals from the tumor microenvironment can activate the EMT program, thereby permitting cancer cells to invade the surrounding stroma and disseminate to distant organs. Transforming growth factor β1 (TGFβ1) is a potent inducer of EMT that can also induce apoptosis depending on the microenvironmental context. In particular, stiff microenvironments promote EMT while softer ones promote apoptosis. Here, we investigated the molecular signaling downstream of matrix stiffness that regulates the phenotypic switch in response to TGFβ1, and uncovered a critical role for integrin-linked kinase (ILK). Specifically, depleting ILK from mammary epithelial cells precludes their ability to sense the stiffness of their microenvironment. In response to treatment with TGFβ1, ILK-depleted cells undergo apoptosis on both soft and stiff substrata. We found that knockdown of ILK decreases focal adhesions and increases cell-cell adhesions, thus shifting the balance from cell-matrix to cell-cell adhesion. High cell-matrix adhesion promotes EMT whereas high cell-cell adhesion promotes apoptosis downstream of TGFβ1. These results highlight an important role for ILK in controlling cell phenotype by regulating adhesive connections to the local microenvironment.

Functionalizing micro-3D-printed protein hydrogels for cell adhesion and patterning

2016 ◽  
Vol 4 (10) ◽  
pp. 1818-1826 ◽  
Author(s):  
D. S. Hernandez ◽  
E. T. Ritschdorff ◽  
S. K. Seidlits ◽  
C. E. Schmidt ◽  
J. B. Shear
Keyword(s):  
Cell Culture ◽  
Cell Adhesion ◽  
Schwann Cells ◽  
Spatial Resolution ◽  
Cell Adhesive ◽  
A Cell ◽  
3D Printed ◽  
Protein Hydrogels

A versatile and dynamic photoconjugation platform is introduced that provides high, 3D spatial resolution for functionalizing micro-3D-printed (μ-3DP) hydrogels. Schwann cells are patterned on μ-3DP hydrogels precisely labeled with RGD, a cell adhesive peptide, demonstrating utility of this platform for cell culture applications.

Simple and Biocompatible Ion Beam Micropatterning of a Cell-Repellent Polymer on Cell-Adhesive Surfaces to Manipulate Cell Adhesion

2016 ◽  
Vol 12 (2) ◽  
pp. 387-393 ◽  
Author(s):  
In-Tae Hwang ◽  
Chan-Hee Jung ◽  
Chang-Hee Jung ◽  
Jae-Hak Choi ◽  
Kwanwoo Shin ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Ion Beam ◽  
Cell Adhesive ◽  
A Cell

Amelogenin is a Cell Adhesion Protein

2002 ◽  
Vol 81 (7) ◽  
pp. 497-500 ◽  
Author(s):  
A.M. Hoang ◽  
R.J. Klebe ◽  
B. Steffensen ◽  
O.H. Ryu ◽  
J.P. Simmer ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Tooth Enamel ◽  
Periodontal Regeneration ◽  
Major Protein ◽  
Therapeutic Effects ◽  
Partial Explanation ◽  
Adhesion Protein ◽  
Cell Adhesion Protein ◽  
Cell Adhesive ◽  
A Cell

Amelogenin, the major protein component of tooth enamel, is shown to be a cell adhesion protein. Since it had been shown that an amelogenin-containing preparation, Emdogain®, possessed cell-adhesive activity, we tested the hypothesis that amelogenin was responsible for cell-adhesive activity. Recombinant amelogenin was found to promote adhesion at less than 15 μg/60-mm plate and requires divalent cations for activity. While we found that amelogenin does not bind to collagen or heparin under physiological conditions, it was demonstrated previously that amelogenin does bind to hydroxyapatite. The cell-adhesive activity of amelogenin may play a role in development and may provide a partial explanation for the therapeutic effects of Emdogain® in periodontal regeneration.

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