Sex-independent expression of chloride/formate exchanger Cfex (Slc26a6) in rat pancreas, small intestine, and liver, and male-dominant expression in kidneys
Dean KaraicaDavorka BreljakJovica LončarMila LovrićVedran MicekIvana VrhovacHrvoje BrzicaCarol M. Herak–KrambergerJana DuporMarija LjubojevićTvrtko SmitalŽeljka VogrincGerhard BurckhardtBirgitta C. BurckhardtIvan Sabolić
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Abstract Chloride/formate exchanger (CFEX; SLC26A6) mediates oxalate transport in various mammalian organs. Studies in Cfex knockout mice indicated its possible role in development of male-dominant hyperoxaluria and oxalate urolithiasis. Rats provide an important model for studying this pathophysiological condition, but data on Cfex (rCfex) localisation and regulation in their organs are limited. Here we applied the RT-PCR and immunochemical methods to investigate rCfex mRNA and protein expression and regulation by sex hormones in the pancreas, small intestine, liver, and kidneys from intact prepubertal and adult as well as gonadectomised adult rats treated with sex hormones. rCfex cDNA-transfected HEK293 cells were used to confirm the specificity of the commercial anti-CFEX antibody. Various biochemical parameters were measured in 24-h urine collected in metabolic cages. rCfex mRNA and related protein expression varied in all tested organs. Sex-independent expression of the rCfex protein was detected in pancreatic intercalated ducts (apical domain), small intestinal enterocytes (brush-border membrane; duodenum > jejunum > ileum), and hepatocytes (canalicular membrane). In kidneys, the rCfex protein was immunolocalised to the proximal tubule brush-border with segment-specific pattern (S1=S2<S3), and both rCfex mRNA and protein expression exhibited male-dominant sex differences driven by stimulatory effects of androgens after puberty. However, urinary oxalate excretion was unrelated to renal rCfex protein expression. While the effect of male-dominant expression of rCfex in renal proximal tubules on urine oxalate excretion remains unknown, its expression in the hepatocyte canalicular membrane may be a pathway of oxalate elimination via bile.Keywords:
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Brush border
Yersinia enterocolitica
Jejunum
Disaccharidase
Villous atrophy
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The effect of diets containing various amounts of casein and starch on enzymes bound to the brush border of the small intestine and kidney of rats were investigated with the following results. 1) Diets with low starch and high casein contents resulted in higher specific activity of leucineaminopeptidase in the small intestine than diets with high starch and low casein contents. Diets with high starch and low casein contents increased the specific activity of maltase. 2) Rat small intestine contains at least two isoenzymes of leucineaminopeptidase: one bound to the brush border and the other not bound to it but recoverable in the soluble fraction. Only the former was influenced by the diet. 3) The maximum velocity (Vmax) of leucineaminopeptidase bound to the brush border was twice as much in rats on a high casein diet as in those on a low casein diet, but the Michaelis constant (Km) was approximately the same in both groups of rats. 4) Leucineaminopeptidase and maltase activities in the kidney were not influenced by diet.
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Alpha-glucosidase
Disaccharidase
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P-glycoprotein
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To determine the functional specificity of intestinal brush-border pteroylpolyglutamate hydrolase (PPH), we compared the regional location of in vivo hydrolysis of pteroyltriglutamate (PteGlu3) with the location of activity and immunoreactivity of the enzyme in the pig. After in vivo incubations, PteGlu3 hydrolytic products were recovered from intestinal segments in the jejunum but not from the ileum. Brush-border PPH activity in fractionated mucosa was 10-fold greater in the jejunum than in the ileum, whereas the activity of intracellular PPH was increased in the distal ileum. Antibodies to purified brush-border PPH identified a major protein band at 120 kDa and a minor protein band at 195 kDa in solubilized jejunal brush border. Immunohistochemistry identified the enzyme only on the brush-border surface of the jejunum, whereas an immunoblot of solubilized brush-border membranes identified brush-border PPH in the jejunum but not in the ileum. The parallel of the regional location of in vivo hydrolysis of PteGlu3 with the location of brush-border PPH activity and immunoreactivity demonstrates the functional specificity of this enzyme in folate digestion.
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Jejunum
Hydrolase
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Jejunum
Northern blot
Large intestine
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The objective of this study was to investigate the development of the weight and the morphological development of the small intestine in Yangzhou geese. The weight, length and perimeter of the small intestine, height and width of the villi, depth of the crypts were measured when geese were 1, 14, 28, 42, 56 and 70 days of age. The results revealed that the weight of the duodenum, jejunum, and ileum (relative to the BW) increased, peaked on day 14 and tended to decline thereafter with age. The weight of the duodenum, jejunum, and ileum (relative to the BW) kept steady-going on 56, 42, 42 days, respectively. A 3-fold increase in length and 2-fold increase in perimeter for the three segments during the period were obtained. The duodenum increased little in length, whereas both jejunum and ileum increased 2 and 3-folds from 1 to 70 days examined. The increase in perimeter of the duodenum, jejunum and ileum was greater from day 1 to 14 than from day 14 to 28. The length and perimeter of the intestinal segments of the gastro-intestinal of Yangzhou geese (relative to the BW) peaked on day 1, then decreased with age and kept steady-going on 42 days, except the relative perimeter of the duodenum. The villus height, surface area and crypt depth in the small intestine were positively correlated with the age of the geese. The ratio of the villus height to the crypt depth (V/C) differed among the segments of the small intestine and at the different time points. The V/C in the ileum increased from day 1 to 70, whereas in the duodenum the ratio first decreased, then rose and descended. However, in the jejunum the ratio increased first, then dropped and rose again, and descended eventually. Key words : Geese, small intestine, morphology.
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ABSTRACT Three segments of cattle small intestine (duodenum, upper jejuno‐ileum and lower jejuno‐ileum) were examined in an in vitro system for activity of ornithine carbamoyltransferase (OCT; EC 2.1.3.3) which is involved in the synthesis of citrulline (Cit) from ornithine (Orn). The mucosa of the three segments of small intestine was collected from Japanese black cattle, homogenized and then centrifuged. The supernatant fraction was used as the crude OCT enzyme solution. The OCT activity was assayed by the production of Cit from Orn determined directly by HPLC. The optimal pH and temperature for OCT activities in the duodenum, upper jejuno‐ileum and lower jejuno‐ileum of cattle small intestine were 7.47 and 39°C. Little difference was observed between the three segments. The OCT activity in cattle kidney was also examined for comparison, and almost no activity was found. The OCT activities in crude enzyme solutions of the three segments of small intestine were stable for up to one month of storage at −20°C in Tris HCl buffer solution. Finally, the role of the small intestine in supplying Cit as a precursor for arginine synthesis in cattle kidney was discussed.
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The distribution of the 10,000 molecular weight calcium binding protein along the human small and large intestine was studied using an enzyme linked immunoadsorbent assay. Small intestinal mucosal samples were obtained from the duodenal bulb, the second and third part of the duodenum and at about 50 cm intervals from jejunum and ileum of five whole small intestines of necro-kidney donors. Mucosal samples of caecum, colon ascendens, and transversum were also investigated. The amount of calcium binding protein per milligram of cytosolic protein increased throughout duodenum to reach the maximum in the proximal segment of jejunum and then declined steadily to nearly undetectable levels in ileum. In the colon no 10,000 molecular weight CaBP was detectable. The distribution of CaBP along the small and large intestine of man is thus parallel to the efficiency of the active calcium absorption of human intestine.
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To study the effect of circulation small peptides concentration on mRNA expression in small intestine, graded amount of soybean small peptides (SSP) were infused into lactating goats through duodenal fistulas. Peptide-bound amino acid (PBAA) concentration in arterial plasma and the mRNA expression of PepT1 was detected in the current study. The results showed that concentrations of all peptidebound amino acids (PBAA) increased and the activity of PepT1 in duodenum tissue was enhanced by SSP infusion. The PepT1expression in duodenum tissue was significantly increased with the increment of amounts of SSP infusion (P<0.05). That in ileum tissue was increased with the increment of the amounts of SSP infusion; the increment of Pep T1 expression was significant only in the 180 g/d treatment (P<0.05). mRNA abundance of PepT1 in jejunum tissue was 1.1 to 1.8 to 2.4 times in SSP infusion group as compared with the control group. In the 120 and 180 g/d treatment, the difference of PepT1 expression in jejunum was significant (P<0.05). The data suggested Pep T1 expression in duodenum, ileum and jejunum tissue was enhanced by an increase in circulation small peptide concentration, and the duodenum might be a main position of small peptides absorption in intestine.
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The size, morphology, and mucosal enzyme activity of small intestines in poults were determined from hatch to 12 d of age. Mass and length of the small intestines increased at different rates in the duodenum, jejunum, and ileum and mass increased more than length. Intestinal weight increased more rapidly then other body organs, reaching a peak at about Day 6, and then decreased. Examination of the morphology of the small intestine showed that villus height and area increased several fold in the jejunum and duodenum and less in the ileum over the period examined. Enterocyte size increased slightly in the initial posthatch period. Activities of mucosal enzymes also increased at different rates in the different intestinal segments and sucrase, maltase, and gamma-glutamyltransferase activities per gram of intestine peaked at 2 to 5 d posthatch before decreasing. Regional mucosal intestine activities exhibited a steady increase, which was highly correlated with BW and thus mucosal hydrolysis may be a determining step in digestion. Poult villus size and area were smaller and mucosal enzyme activity was lower than that found in broilers and this may explain the initial slower growth rate in poults.
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Enterocyte
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Digestion
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