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Human erythrocyte adhesion and spreading on protein-coated polymer surfaces

✍ Scribed by Steinberg, J. ;Neumann, A. W. ;Absolom, D. R. ;Zingg, W.

Publisher
John Wiley and Sons
Year
1989
Tongue
English
Weight
1012 KB
Volume
23
Category
Article
ISSN
0021-9304

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✦ Synopsis

Protein adsorption is t h e first event which occurs when polymer surfaces are exposed to blood. The adsorption of proteins modifies the surface properties of the substrates and therefore influences subsequent cell-surface interactions. In an attempt to elucidate the fundamental mechanisms governing cell-proteinatedsurface interactions, the extent of fresh human erythrocyte adhesion and spreading on protein-coated surfaces was examined. Five human serum proteins (albumin, fibrinogen, immunoglobulin G, fibronectin, and transferrin) were used at bulk con-centrations ranging from 0.01 mg/mL to 50 mg/mL. Polymer substrates covering a wide range of wettability were employed. Protein adsorption significantly reduces erythrocyte adhesion and spreading on all test surfaces with minimum adhesion observed on fibrinogen: IgG > albumin > fibronectin > transferrin > fibrinogen.

The extent of these effects is dependent on the nature of the adsorbed protein, the protein bulk concentration, and the surface properties of the underlying polymer substrates.

*This work represents, in part, the M.A.Sc thesis of J. Steinberg.

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