Activities of Intestinal Enzymes in Experimental Chronic Renal Insufficiency

Grimmel, K.; Bongartz, S; Kasper, Heinrich

doi:10.1159/000180869

Cited by 14 publications

(14 citation statements)

References 22 publications

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“…Several enzymatic reactions carried out by the intestinal mucosa have been shown to be decreased in rats with CRF. For instance, sucrase and maltase activities, as well as xanthine oxidase, were significantly reduced, whereas the activities of other dipeptidases were unchanged (Grimmel et al, 1977). More recently, we have also demonstrated that intestinal cytochrome P450 is reduced in CRF .…”

Section: Downloaded Frommentioning

confidence: 59%

Down-Regulation of Intestinal Drug Transporters in Chronic Renal Failure in Rats

Naud¹,

Jl²,

Boisvert³

et al. 2006

J Pharmacol Exp Ther

105

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Chronic renal failure (CRF) is associated with an increased bioavailability of drugs by a poorly understood mechanism. One hypothesis is a reduction in the elimination of drugs by the intestine, i.e., drug elimination mediated by protein membrane transporters such as P-glycoprotein (Pgp) and multidrug-resistance-related protein (MRP) 2. The present study aimed to investigate the repercussions of CRF on intestinal transporters involved in drug absorption [organic anion-transportingpolypeptide (Oatp)] and those implicated in drug extrusion (Pgp and MRP2). Pgp, MRP2, MRP3, Oatp2, and Oatp3 protein expression and Pgp, MRP2, and Oatp3 mRNA expression were assessed in the intestine of CRF (induced by five-sixth nephrectomy) and control rats. Pgp and MRP2 activities were measured using the everted gut technique. Rat enterocytes and Caco-2 cells were incubated with sera from control and CRF rats to characterize the mechanism of transporters' down-regulation. Protein expression of Pgp, MRP2, and MRP3 were reduced by more than 40% (p Ͻ 0.01) in CRF rats, whereas Oatp2 and Oatp3 expression remained unchanged. There was no difference in the mRNA levels assessed by real-time polymerase chain reaction. Pgp and MRP2 activities were decreased by 30 and 25%, respectively, in CRF rats compared with control (p Ͻ 0.05). Uremic sera induced a reduction in protein expression and in activity of drug transporters compared with control sera. Our results demonstrate that CRF in rats is associated with a decrease in intestinal Pgp and MRP2 protein expression and function secondarily to serum uremic factors. This reduction could explain the increased bioavailability of drugs in CRF.

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Section: Downloaded Frommentioning

confidence: 59%

Down-Regulation of Intestinal Drug Transporters in Chronic Renal Failure in Rats

Naud¹,

Jl²,

Boisvert³

et al. 2006

J Pharmacol Exp Ther

105

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“…Uraemic rats given a diet with normal protein content exhibit increased activities of some dipeptidases in homo genate of mucosa and in brush border preparations [1,[17][18][19]. We found that glycyl-L-leucine and L-methionyl-L-methionine dipeptidase activities were increased, but that the L-alanyl-L-proline dipeptidase activity was un changed in uraemic rats given a normal diet (24% protein) [1].…”

Section: Discussionmentioning

confidence: 92%

Small Intestinal Dipeptidases and Disaccharidases in Uraemic Rats on a Low Protein Diet

Sterner¹,

Lindberg²,

Asp

et al. 1983

Nephron

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Small intestinal dipeptidases (substrate: glycyl-L-leucine, L-methionyl-L-methionine, and L-alanyl-L-proline) were determined in uraemic and sham-operated rats given normal protein diet (24%), low protein diet (6%), and total parenteral nutrition for 10–14 days. Disaccharidases (substrate: maltose, sucrose, trehalose, and lactose) were measured after normal and low protein diet orally. Glycyl-L-leucine and L-methionyl-L-methionine splitting activities were increased on normal protein diet but decreased after low protein feeding in uraemic rats. Parenteral nutrition further lowered the enzyme activity. L-Alanyl-L-proline dipeptidase activity showed an inverse relation to protein intake with the highest values after parenteral nutrition. Lactase increased in uraemic rats after low protein feeding and was the only disaccharidase to be affected by the nutritional change. It is suggested that the changes of the intestinal dipeptidase activities in uraemia are adaptive to variation in the luminal content of di- and ohgopeptides because of the type of nutrition given.

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“…Grimmer et al [5,6] showed a drecrease of sucrase and maltase activities of the intestinal mucosa, whereas Wizemann et al [19] found an increase of maltase and no change in lactase and sucrase, and Sterner et al [18] observed a slight increase of sucrase and no change in maltase, trehalase and lactase.…”

Section: Discussionmentioning

confidence: 99%

“…Although morphological dis orders of the gastrointestinal tract in chronic renal failure are well documented [1,3,8,9], conflicting data have been reported concerning intestinal enzyme activities [3,5,6,9,18,19],…”

mentioning

confidence: 99%

Circadian Rhythms of Intestinal Disaccharidases in Experimental Uremia in Rats

Inagaki¹,

Mori²,

Shimomura³

et al. 1982

Nephron

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The activity of intestinal disaccharidases, maltase trehalase, sucrase and lactase, was measured in five-sixths-nephrectomized uremic rats fed ad libitum and kept under conventional lighting conditions, with a dark night. In normal rats (controls), these disaccharidase activities changed with time of day, being high at night and low during daytime. In five-sixths-nephrectomized uremic rats, these disaccharidase activities were not as high at night and not as low during daytime as in controls, so their circadian variations were smaller than those of controls.

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Activities of Intestinal Enzymes in Experimental Chronic Renal Insufficiency

Cited by 14 publications

References 22 publications

Down-Regulation of Intestinal Drug Transporters in Chronic Renal Failure in Rats

Down-Regulation of Intestinal Drug Transporters in Chronic Renal Failure in Rats

Small Intestinal Dipeptidases and Disaccharidases in Uraemic Rats on a Low Protein Diet

Circadian Rhythms of Intestinal Disaccharidases in Experimental Uremia in Rats

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