Lipopolysaccharides and Beta-Glucuronidase Activity in Choledochal Bile in Relation to Choledocholithiasis

Common duct gallstones are mainly of the brown pigment type, which are usually attributed to bacterial factors. Bacterial β-glucuronidase most probably plays a role in the pathogenesis in many but not all patients. The role of other bacterial factors is more undecided. The aims of this study were to...

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Published inDigestion Vol. 58; no. 5; pp. 437 - 443
Main Authors Osnes, T., Sandstad, O., Skar, V., Osnes, M.
Format Journal Article
LanguageEnglish
Published Basel, Switzerland Karger 01.01.1997
S. Karger AG
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Summary:Common duct gallstones are mainly of the brown pigment type, which are usually attributed to bacterial factors. Bacterial β-glucuronidase most probably plays a role in the pathogenesis in many but not all patients. The role of other bacterial factors is more undecided. The aims of this study were to investigate a possible association between lipopolysaccharides (LPS) and choledocholithiasis, and to examine the interrelationship to β-glucuronidase. Common duct bile obtained at endoscopic retrograde cholangiography in 86 patients was assayed for LPS by a limulus amebocyte lysate test, and β-glucuronidase activity at pH 7.0 was measured. We found that both elevated concentration of LPS and the presence of juxtapapillary duodenal diverticula were associated with common duct stones (p < 0.01, both). Patients who had their common duct stones removed recently had a lower LPS concentration and a lower activity of β-glucuronidase than those who had a stone in situ (p < 0.01 both), but still higher LPS concentration than those without choledocholithiasis at all (p < 0.01). In multiple logistic regression analysis, elevated LPS was the significant predictor of common duct stones (p < 0.01), and not confounding with neither β-glucuronidase nor juxtapapillary diverticula. We conclude that gram-negative bacteria convey bacterial factors associated with choledocholithiasis, by mechanisms independent of, and additional to β-glucuronidase.
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ISSN:0012-2823
1421-9867
DOI:10.1159/000201480