Literature DB >> 10737870

Leukocyte adhesion on model surfaces under flow: effects of surface chemistry, protein adsorption, and shear rate.

V A Tegoulia1, S L Cooper.   

Abstract

The effect of specific chemical functionalities on the adhesion of polymorphonuclear leukocytes (PMNs) under flow was investigated using a set of well-characterized, chemically functionalized surfaces prepared by self-assembly of alkanethiolate monolayers on gold surfaces. Terminal functionalities included CH(3), CH(2)OH, COOH, and (OCH(2)CH(2))(3)OH groups. A new surface modification was used to incorporate a phosphorylcholine moiety on the hydroxyl-terminated monolayer. Surface modification was verified using contact-angle measurements, ellipsometry, and X-ray photoelectron spectroscopy. Adhesion on the surfaces was studied in the presence and absence of pre-adsorbed fibrinogen. Fibrinogen adsorption on self-assembled monolayers (SAMs) was quantified using radioisotope detection. PMN adhesion was found to be dependent on the monolayer's terminal functionality. Adhesion was higher on the hydrophobic CH(3) surface and the polar COOH monolayer. Leukocyte adhesion was least on the phosphorylcholine-rich surface, followed by the ethylene-oxide-containing monolayer. Cell adhesion also was low on the hydrophilic OH monolayer. Attachment was decreased with increasing shear rate, exhibiting a three-fold decrease between 20 and 100 s(-1). Fibrinogen adsorption was higher on the CH(3) monolayer but comparable for the other four SAMs. Preincubation of the surfaces with fibrinogen decreased adhesion on all SAMs examined. Copyright 2000 John Wiley & Sons, Inc.

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Year:  2000        PMID: 10737870     DOI: 10.1002/(sici)1097-4636(20000605)50:3<291::aid-jbm2>3.0.co;2-1

Source DB:  PubMed          Journal:  J Biomed Mater Res        ISSN: 0021-9304


  11 in total

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5.  Immunoblot analysis of proteins associated with self-assembled monolayer surfaces of defined chemistries.

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8.  Modification of human polymorphonuclear neutrophilic cell (PMN)-adhesion on biomaterial surfaces by protein preadsorption under static and flow conditions.

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10.  Investigation of the effects of surface chemistry and solution concentration on the conformation of adsorbed proteins using an improved circular dichroism method.

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