Kinetics of cell adhesion to polymer surfaces

1988 ◽  
Vol 22 (3) ◽  
pp. 215-229 ◽  
Author(s):  
D. R. Absolom ◽  
C. Thomson ◽  
L. A. Hawthorn ◽  
W. Zingg ◽  
A. W. Neumann
Keyword(s):  
Cell Adhesion ◽  
Polymer Surfaces ◽  
Kinetics Of

Effect of Preadsorbed Proteins on Cell Adhesion to Polymer Surfaces

1993 ◽  
Vol 155 (2) ◽  
pp. 334-339 ◽  
Author(s):  
Yasushi Tamada ◽  
Yoshito Ikada
Keyword(s):  
Cell Adhesion ◽  
Polymer Surfaces

scholarly journals Human leukocyte elastase is an endogenous ligand for the integrin CR3 (CD11b/CD18, Mac-1, alpha M beta 2) and modulates polymorphonuclear leukocyte adhesion.

1996 ◽  
Vol 184 (4) ◽  
pp. 1213-1223 ◽  
Author(s):  
T Q Cai ◽  
S D Wright
Keyword(s):  
Cell Adhesion ◽  
Polymorphonuclear Leukocytes ◽  
Leukocyte Adhesion ◽  
Human Leukocyte ◽  
Endogenous Ligand ◽  
Leukocyte Elastase ◽  
Human Leukocyte Elastase ◽  
Beta 2 ◽  
Coated Surfaces ◽  
Kinetics Of

Integrin CR3 (CD11b/CD18, Mac-1, alpha M beta 2) mediates the transient adhesion of polymorphonuclear leukocytes (PMN) to surfaces coated with fibrinogen, C3bi, ICAM-1, and other ligands. Recent studies (Cai, T.-Q., and S.D. Wright 1995. J. Biol. Chem. 270:14358) suggest that adhesion may be favored by stimulus-dependent changes in the kinetics of ligand binding by CR3. Cell detachment, on the other hand, must occur by a different mechanism because binding kinetics cannot affect cell adhesion after binding of ligand has occurred. We have sought a mechanism that would reverse binding of ligand to CR3 and report here that lysates of PMN contain an endogenous ligand that binds CR3 and competes the binding of C3bi. Purification and sequence analysis identified the structurally homologous azurophilic granule proteins, elastase, protease 3, and azurocidin as candidates. Studies with purified elastase and azurocidin showed that each bound specifically to purified, immobilized CR3. Elastase may play a role in modulating integrin-mediated cell adhesion because it is expressed at the cell surface, and the expression level is inversely proportional to cell adhesivity. Furthermore, a monoclonal antibody against elastase prevented detachment of PMN from fibrinogen-coated surfaces and blocked chemotaxis, confirming a role for this protein in regulating integrin-mediated adhesion. These studies suggest a model for release of integrin-mediated cell adhesion in which endogenous ligands such as elastase may release adhesion by "'eluting" substrate-bound ligand. A role for the proteolytic activity of elastase appears likely but is not demonstrated in this study.

scholarly journals Studies on cell adhesion and recognition. II. The kinetics of cell adhesion and cell spreading on surfaces coated with carbohydrate-reactive proteins (glycosidases and lectins) and fibronectin.

1981 ◽  
Vol 88 (1) ◽  
pp. 138-148 ◽  
Author(s):  
W G Carter ◽  
H Rauvala ◽  
S I Hakomori
Keyword(s):  
Cell Adhesion ◽  
Cell Surface ◽  
Cell Attachment ◽  
Cell Spreading ◽  
Galactose Oxidase ◽  
Cross Linking ◽  
Con A ◽  
Coated Surfaces ◽  
Plastic Surfaces ◽  
Kinetics Of

The kinetics of cell attachment and cell spreading on the coated surfaces of two classes of carbohydrate-reactive proteins, enzymes and lectins, have been compared with those on fibronectin-coated surfaces with the following results: (a) A remarkable similarity between the kinetics of cell attachment to fibronectin-coated and glycosidase-coated surfaces was found. In contrast, cell attachment kinetics induced by lectin- and galactose oxidase-coated surfaces, in general, were strikingly different from those on fibronectin and glycosidase surfaces. The distinction between fibronectin- or glycosidase- and lectin- or galactose oxidase (an enzyme with lectin-type characteristics)-coated surfaces was further supported by the finding that cytochalasin B and EDTA inhibited cell attachment to fibronectin- and glycosidase-coated surfaces but not lectin-coated surfaces. (b) Fibronectin, if labeled and added to a cell suspension, showed only low or negligible interaction with the cell surface. However, fibronectin absorbed on plastic surfaces showed a high cell-attaching activity. It is assumed that fibronectin coated on plastic surfaces may form polyvalent attachment sites in contrast to its lower valency in aqueous solution. (c) Various inhibitors of cell attachment to both fibronectin-, galactose oxidase-, and lectin-coated surfaces were effective only during the first few minutes of the adhesion assay, after which time the attached cells became insensitive to the inhibitors. It is suggested that the initial specific recognition on either lectin-type or fibronectin-type surfaces is followed by an active cell-dependent attachment process. The primary role of the adhesion surface is to stimulate the cell-dependent attachment response. (d) Cells attached on tetravalent concanavalin A (Con A) spread very rapidly and quantitatively, whereas divalent succinyl Con A and monovalent Con A were effective stimulators of cell attachment but not cell spreading. Cross-linking of succinyl Con A restored the cell spreading activity. Tetravalent Con A surfaces specifically bind soluble glycoproteins, whereas succinyl Con A has a greatly reduced ability to bind the same glycoproteins. These results suggest that cross-linking of cell surface glycoproteins by the multivalent adhesive surface may trigger the cellular reaction leading to cell spreading.

scholarly journals Single-cell adhesion force kinetics of cell populations from combined label-free optical biosensor and robotic fluidic force microscopy

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Milan Sztilkovics ◽  
Tamas Gerecsei ◽  
Beatrix Peter ◽  
Andras Saftics ◽  
Sandor Kurunczi ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Single Cell ◽  
Temporal Resolution ◽  
Adhesion Force ◽  
Optical Biosensor ◽  
Cell Populations ◽  
Label Free ◽  
Kinetic Evaluation ◽  
Force Microscopy ◽  
Kinetics Of

AbstractSingle-cell adhesion force plays a crucial role in biological sciences, however its in-depth investigation is hindered by the extremely low throughput and the lack of temporal resolution of present techniques. While atomic force microcopy (AFM) based methods are capable of directly measuring the detachment force values between individual cells and a substrate, their throughput is limited to few cells per day, and cannot provide the kinetic evaluation of the adhesion force over the timescale of several hours. In this study a high spatial and temporal resolution resonant waveguide grating based label-free optical biosensor was combined with robotic fluidic force microscopy to monitor the adhesion of living cancer cells. In contrast to traditional fluidic force microscopy methods with a manipulation range in the order of 300–400 micrometers, the robotic device employed here can address single cells over mm-cm scale areas. This feature significantly increased measurement throughput, and opened the way to combine the technology with the employed microplate-based, large area biosensor. After calibrating the biosensor signals with the direct force measuring technology on 30 individual cells, the kinetic evaluation of the adhesion force and energy of large cell populations was performed for the first time. We concluded that the distribution of the single-cell adhesion force and energy can be fitted by log-normal functions as cells are spreading on the surface and revealed the dynamic changes in these distributions. The present methodology opens the way for the quantitative assessment of the kinetics of single-cell adhesion force and energy with an unprecedented throughput and time resolution, in a completely non-invasive manner.

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