PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 6825535

Endogenous bile acid tolerance test for liver function.

M van Blankenstein·M Frenkel·J W van den Berg·F J ten Kate·E P Bosman-Jacobs·A C Touw-Blommesteyn
View original source ↗Export metadata ↓

Abstract

Fasting and postprandial (stimulated) serum conjugated bile acids (CBA) were measured by a solid-phase radioimmunoassay in 329 patients undergoing liver biopsy, and the results were analyzed for 231 who fitted into 10 diagnostic categories. In healthy volunteers the mean fasting CBA of 1.8 +/- 0.7 mumol/liter rose to 3.0 +/- 0.8 mumol/liter postprandially. In patients mean fasting and stimulated CBA were only significantly raised in moderate to severe chronic and acute liver disease. Diagnostic sensitivity was poor in mild liver disease. Individuals with normal results were found in 8 of 11 disease categories. The ratio of stimulated to fasting CBA expressed in a stimulation quotient did not rise in more advanced liver disease. These findings are best explained by a constant fractional clearance of bile acids by the liver. We conclude that the serum conjugated bile acid determination as a test of liver cell function is not sensitive enough to identify all cases of biopsy-proven liver disease.

Explore related subjects

Bile Acids and SaltsFastingHumansLiver DiseasesLiver Function TestsRadioimmunoassayTime FactorsJournal Article

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

M van Blankenstein, M Frenkel, J W van den Berg, F J ten Kate, E P Bosman-Jacobs, A C Touw-Blommesteyn. 1983. Endogenous bile acid tolerance test for liver function.. https://doi.org/10.1007/bf01315143

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2025

Clostridium scindens: history and current outlook for a keystone species in the mammalian gut involved in bile acid and steroid metabolism.

Clostridium scindens is a keystone bacterial species in the mammalian gut that, while low in abundance, has a significant impact on bile acid and steroid metabolism. Numerous studies indicate that the two most studied strains of C. scindens (i.e. ATCC 35704 and VPI 12708) are important for a myriad of physiological processes in the host. We focus on both historical and current microbiological and molecular biology work on the Hylemon-Björkhem pathway and the steroid-17,20-desmolase pathway that were first discovered in C. scindens. Our most recent analysis now calls into question whether strains currently defined as C. scindens represent two separate taxonomic groups. Future directions include developing genetic tools to further explore the physiological role of bile acid and steroid metabolism by strains of C. scindens and the causal role of these pathways in host physiology and disease.

Bile Acids and Salts↗
PubMed1995

Structural features of the hydroxy- and keto-disubstituted bile salts: human serum albumin binding.

The binding of keto- and hydroxy bile salts to human serum albumin, the identity of the bile salts binding sites and the identification of the amino acids present in these sites were studied. The keto bile salts cholanate-3-one (C3), cholanate-3,6-dione (C3-6) and cholanate-3-hydroxy-6-one (KHC) were found to quench the native fluorescence emission of albumin. This suggested that the tryptophan residue of human albumin (residue 214) is accessible to the keto bile salts and not to the hydroxy parent compounds. The binding of the keto bile salts was characterized by a simple population of binding sites with Ka ranging from 22 x 10(4) M-1 for the mono keto bile salt (C3) down to 4 x 10(4) M-1 for the hydroxy-keto bile salt (KHC). The substitution of an oxo group at carbon C3 in C3-6 molecule for a hydroxy group (KHC) produce a significant decreasing of the interaction, suggesting that the hybridization state of the carbon at C3 in the steroid ring of the bile salt molecule is also an essential requirement for bile salts binding. It was found that bile salts are bound to the benzodiazepine binding site on human albumin (site II), producing a perturbation on site I, fatty acids and bilirubin binding site. The presence of only one substituent at C3 (oxo or OH) produce an important perturbation on the fatty acid binding sites, decreasing the polarity of the its microenvironment, while a little effect was observed for the dihydroxy and di-oxo-substituted BS, suggesting that the hydroxy substituents at C6, C7 and C12 do not interact in a significant manner with the fatty acid binding sites on HSA. The participation of specific amino acids in albumin-bile salt binding sites depends on the polar groups on the bile salt molecules as exemplified by the quantitatively different role of lysyl residues like those interacting with KHC, C3 and C3-6, and tyrosyl residue interacting with KHC. The following amino acids in human albumin were found to play a role in the bile salts-albumin interaction: lysyl 195 and 225, several arginyls, histidyl 146 and tyrosyl 411.

Bile Acids and Salts↗
PubMed1995

Bile acid/phosphatidylcholine interactions in mixed monomolecular layers: differences in condensation effects but not interfacial orientation between hydrophobic and hydrophilic bile acid species.

Monomolecular layers of undissociated bile acids and membrane lipids at the air/water interface serve as useful models for the interactions between fully ionized bile salts and physiological membranes. Employing an automated Langmuir-Pockels surface balance, surface pressures and dipole moments were measured as functions of molecular area for six dihydroxy bile acids: ursodeoxycholic acid (UDCA), deoxycholic acid (DCA), chenodeoxycholic acid (CDCA), hyodeoxycholic acid (HDCA), allodeoxycholic acid (alloDCA), and 7 alpha,12 alpha-dihydroxycholanoic acid (7,12-OH-DCA), individually and in mixed mono-molecular layers with 1-palmitoyl-2-oleoyl-sn-3-glycerophosphatidylcholine (POPC) with and without cholesterol on a 5 M NaCl subphase at pH 2. In general, monolayers of hydrophilic bile acids (UDCA, HDCA) had lower collapse pressures and surface dipole moments than hydrophobic bile acids (CDCA approximately DCA approximately alloDCA < 7,12-OH-DCA). In binary mixtures with POPC, all bile acids including the synthetic 7,12-OH-DCA and the uncommon alloDCA condensed mixed monomolecular layers, with the degree of condensation correlating positively with bile acid hydrophobicity. In contrast, none of the bile acids caused further condensation of condensed POPC/cholesterol monomolecular layers. Surface dipole moments of binary bile acid/POPC +/- cholesterol mixtures demonstrated strict additivity, implying that no change in molecular orientation of the interface occurred over film compositions that varied from 0 to 100% bile acid. We conclude that the long axes of the steroid nuclei of dihydroxy bile acids remain parallel to the interface in mixed bile acid/POPC +/- cholesterol monomolecular layers under all conditions. We infer that fully dissociated hydrophobic and, to a lesser extent, hydrophilic bile salts condense phospholipid monomolecular layers and membranes in a similar fashion.

Bile Acids and Salts↗