PROTEIN ADSORPTION AND BACTERIAL ADHESION TO BILIARY STENT MATERIALS

Citation
Jl. Yu et al., PROTEIN ADSORPTION AND BACTERIAL ADHESION TO BILIARY STENT MATERIALS, The Journal of surgical research, 62(1), 1996, pp. 69-73
Citations number
29
Categorie Soggetti
Surgery
ISSN journal
00224804
Volume
62
Issue
1
Year of publication
1996
Pages
69 - 73
Database
ISI
SICI code
0022-4804(1996)62:1<69:PAABAT>2.0.ZU;2-T
Abstract
Four biliary stents inserted for relief of jaundice in patients with b iliary obstruction due to carcinoma of pancreatic head were examined f or the adsorption of biliary proteins and bacterial colonization, Fibr onectin and vitronectin (S-protein) were found to be the two main prot eins adsorbed on the inner surface of the stents, Biliary isolates inc luded Escherichia coli, Enterococcus faecalis, and Candida albicans. I n vitro studies were performed to clarify the kinetics of biliary prot ein and bacterial adhesion, Biliary drains of polytetrafluorethylene, polyethylene, polyurethane, and rubber were placed in a flow cell and perfused with human bile at 37 degrees C for 24 hr, The materials were subjected to either detection of adsorbed biliary proteins or perfusi on with H-3-labeled E. coli cells (1 x 10(6) cfu/ml). The results show that the adsorbed biliary proteins were detectable on the surface of biliary stents and able to enhance bacterial adhesion to the surface i n the first 24 hrs after the exposure of stent materials to bile, and that both the adsorption of biliary proteins and the adhesion of bacte rial cells were material- and strain-dependent. Furthermore, there was a clear correlation between the amount of adsorbed fibronectin and th e number of adherent bacteria. The results indicate that, in the clini cal situation, biliary proteins may be adsorbed on the surface of inse rted stents within a short time after insertion, and some of them may be used by bacterial cells as receptors for adhesion to the surface, a nd thus involved in the process of bacterial adhesion. (C) 1996 Academ ic Press, Inc.