Colonic Absorption of Sulfated and Nonsulfated Bile Acids in Rat

Walker, S.; Stiehl, A.; Raedsch, R.; Klöters, P.; Kommerell, B.

doi:10.1159/000199268

Cited by 16 publications

(6 citation statements)

References 8 publications

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“…It has been shown that SLA is present in substantial quantities in human faeces and that the LA\SLA ratio was 2.1 [15]. It has further been suggested that lowered uptake of sulphated bile acids in the ileum, and lack of uptake in the colon, may contribute to their excretion [16]. Finally, studies with mice have shown that sulphated bile acids may inhibit colon carcinogenesis [17].…”

Section: Discussionmentioning

confidence: 99%

Lithocholic acid and sulphated lithocholic acid differ in the ability to promote matrix metalloproteinase secretion in the human colon cancer cell line CaCo-2

Halvorsen

Staff

LIGAARDEN

et al. 2000

Biochemical Journal

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The human colon carcinoma cell line CaCo-2 has the ability to sulphate the secondary bile acid lithocholic acid (LA), whereas other primary or secondary bile acids were not sulphated [Halvorsen, Kase, Prydz, Gharagozlian, Andresen and Kolset (1999) Biochem. J. 343, 533-539]. To study the biological implications of this modification, CaCo-2 cells were incubated with either LA or sulphated lithocholic acid (3-sulpholithocholic acid, SLA), and in some experiments with taurine-conjugated lithocholic acid. Increased secretion of matrix metalloproteinases (MMPs) correlates with transformation of colon epithelial cells. When CaCo-2 cells were incubated with LA, the secretion of MMP-2 was found to increase approx. 60 % when analysed by gelatin zymography, and 80 % when analysed by Western blotting. SLA, in contrast, did not affect the level of MMP-2 secretion, and after zymography the level of enzyme activity was

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Section: Discussionmentioning

confidence: 99%

Lithocholic acid and sulphated lithocholic acid differ in the ability to promote matrix metalloproteinase secretion in the human colon cancer cell line CaCo-2

Halvorsen

Staff

LIGAARDEN

et al. 2000

Biochemical Journal

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“…This is a general principle explained by the hydrophylic nature of glucurono-and sulfoconjugates which precludes their intestinal absorption [50]. Moreover, it was found recently that sulfated bile salts are poorly absorbed in the ileum and not at all in the colon [51], in contrast to unsulfated bile salts. Furthermore, Robben et al [15] reported that the 13 contamination of germ-free rats with sulfataseproducing anaerobic bacteria resulted in a 5-fold increase of the time required for the fecal excretion of the injected cholate sulfate, indicating a strong enhancement of the enterohepatic circulation of conjugates by hydrolytic bacteria.…”

Section: Discussionmentioning

confidence: 99%

Hydrolysis of iodothyronine conjugates by intestinal bacteria

Hazenberg¹,

Herder

Visser

1988

FEMS Microbiology Letters

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Glucuronide and sulfate conjugation are important pathways in the peripheral metabolism of thyroid hormone. These reactions occur predominantly in the liver, and especially the glucuronides are excreted in the bile. Although an enterohepatic circulation after intestinal hydrolysis of iodothyronine conjugates is suggested by several authors, substantial proof has not been presented so far. In the present paper experimental work from our group is reviewed. The studies showed that fecal suspensions of human or rat origin hydrolysed iodothyronine conjugates, whereas oral administration of antibiotics to rats strongly reduced this capacity. Obligately anaerobic intestinal bacteria were found to be responsible for the hydrolysis and several species belonging to the major residents of the intestinal flora of man and rat could be isolated and identified. Recent studies with conventional and decontaminated rats produced strong support for the existence of an enterohepatic circulation of thyroid hormone. Our findings are discussed in connection with other relevant studies on this subject.

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“…[3][4][5][6][7] Sulfated bile acids, similar to the precursor bile acids, are able to induce bile flow and may play a protective role in cholestasis. 8,9 Sulfated bile acid amidates, in contrast to their nonsulfated, amidated bile acid precursors, do not undergo extensive enterohepatic circulation [10][11][12] because they are poor substrates of the intestinal sodium-dependent bile acid transporter that is present abundantly in ileal enterocytes. 12,13 It is therefore imperative to fully understand the uptake mechanisms of sulfated bile acid amidates in the liver.…”

mentioning

confidence: 99%

Transport of the sulfated, amidated bile acid, sulfolithocholyltaurine, into rat hepatocytes is mediated by Oatp1 and Oatp2

et al. 2002

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The uptake of the sulfated bile acid sulfolithocholyltaurine (SLCT) was investigated in isolated rat hepatocytes and in HeLa cells transfected with complementary DNAs (cDNAs) of organic anion transporting polypeptides (Oatps) 1 and 2 cloned from rat liver. In hepatocytes, transport of SLCT was greatly reduced by bromosulfophthalein (BSP), estrone sulfate, the precursor bile acids cholyltaurine and lithocholyltaurine, and 4,4 -diisothiocyanostilbene-2-2 -disulfonic acid (DIDS). However, SLCT transport was insensitive to 4-methylumbelliferyl sulfate, harmol sulfate, digoxin, fexofenadine, and lack of sodium ion. Because the estimation of kinetic constants was enhanced with use of inhibitors, BSP (1-50 mol/L) was added to isolated rat hepatocytes to assess the various transport components for SLCT uptake. The resulting data showed a nonsaturable pathway and at least 2 pathways of different Michaelis-Menten constants (K m ) (70 and 6 mol/L) and similar maximum velocities (V max ) (1.73 and 1.2 nmol/min/mg protein) and inhibition constants of 0.63 and 10.3 mol/L for BSP. In expression systems, SLCT was taken up by Oatp1 and Oatp2 expressed in HeLa cells with similar K m values (12.6 ؎ 6.2 and 14.6 ؎ 1.9 mol/L). These K m values were comparable to that observed for the high-affinity pathway in rat hepatocytes. In conclusion, the results suggest that transport of SLCT into rat liver is mediated in part by Oatp1 and Oatp2, high-affinity pathways, a lower-affinity pathway of unknown origin, and a nonsaturable pathway that is compatible with a transport system of high K m and/or passive diffusion. (HEPATOLOGY 2002;35:1031-1040

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Colonic Absorption of Sulfated and Nonsulfated Bile Acids in Rat

Cited by 16 publications

References 8 publications

Lithocholic acid and sulphated lithocholic acid differ in the ability to promote matrix metalloproteinase secretion in the human colon cancer cell line CaCo-2

Lithocholic acid and sulphated lithocholic acid differ in the ability to promote matrix metalloproteinase secretion in the human colon cancer cell line CaCo-2

Hydrolysis of iodothyronine conjugates by intestinal bacteria

Transport of the sulfated, amidated bile acid, sulfolithocholyltaurine, into rat hepatocytes is mediated by Oatp1 and Oatp2

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