Transcriptional regulation of intestinal hydrolase biosynthesis during postnatal development in rats

Lactase-phlorizin hydrolase (LPH) and sucrase-isomaltase (SI) are intestine-specific microvillus membrane hydrolases whose specific activities demonstrate reciprocal regulation during development but whose mechanisms of regulation have not been fully defined. To investigate transcriptional control of these two proteins, the rat LPH and SI genes were cloned, and antisense probes for preprocessed mRNAs (pre-mRNAs) were developed from intron sequence. LPH mRNA, as measured by quantitative ribonuclease (RNase) protection assays, was abundant before weaning and decreased two- to fourfold during weaning, whereas SI mRNA was first detected 14 days after birth and increased rapidly to abundant levels by age 28 days. LPH and SI pre-mRNA levels paralleled those of their respective mRNAs. LPH transcriptional rate declined during weaning, whereas that of SI increased during this time as determined by RNase protection assays of pre-mRNAs and nuclear run-on assays. In the adult rat, LPH mRNA was restricted to the jejunum and proximal ileum, whereas SI mRNA was detected throughout the small intestine, a pattern regulated by transcriptional rate as confirmed by nuclear run-on assays. Lactase and sucrase specific activities correlated well with their respective protein and mRNA concentrations in all experiments. We conclude that gene transcription plays a major role in the developmental and horizontal regulation of LPH and SI biosynthesis and that these two genes are regulated differently in rat small intestine.

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The nitric oxide donor molsidomine prevents ischemia/reperfusion injury of the adult rat small intestine

Pediatric Surgery International ◽

10.1007/s00383-002-0746-y ◽

2003 ◽

Vol 19 (4) ◽

pp. 305-308 ◽

Cited By ~ 4

Author(s):

Hayrettin Öztürk ◽

Mustafa Aldemir ◽

Ali İhsan Dokucu ◽

Yusuf Yağmur ◽

Nihal Kilinç ◽

...

Keyword(s):

Nitric Oxide ◽

Small Intestine ◽

Reperfusion Injury ◽

Ischemia Reperfusion Injury ◽

Ischemia Reperfusion ◽

Nitric Oxide Donor ◽

Rat Small Intestine ◽

Adult Rat

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Uptake and transport of poly(N-vinylpyrrolidone-co-maleic acid) by the adult rat small intestine cultured in vitro: Effect of chemical structure

International Journal of Pharmaceutics ◽

10.1016/0378-5173(94)90163-5 ◽

1994 ◽

Vol 104 (3) ◽

pp. 227-237 ◽

Cited By ~ 7

Author(s):

János Pató ◽

Melinda Móra ◽

Barbara Naisbett ◽

John F. Woodley ◽

Ruth Duncan

Keyword(s):

Small Intestine ◽

Maleic Acid ◽

Chemical Structure ◽

Rat Small Intestine ◽

Adult Rat ◽

Vitro Effect ◽

Uptake And Transport

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Studies of dihydroxyacetone phosphate acyltransferase in rat small intestine. Subcellular localization and effect of partially hydrogenated fish oil and clofibrate

Biochemical Journal ◽

10.1042/bj2820565 ◽

1992 ◽

Vol 282 (2) ◽

pp. 565-570 ◽

Cited By ~ 6

Author(s):

B Ruyter ◽

J S Lund ◽

M S Thomassen ◽

E N Christiansen

Keyword(s):

Small Intestine ◽

Subcellular Localization ◽

Fish Oil ◽

Gradient Centrifugation ◽

Dihydroxyacetone Phosphate ◽

Rat Small Intestine ◽

Specific Activities ◽

Fold Stimulation ◽

Effect Of Feeding ◽

Stimulation Of

The subcellular localization of dihydroxyacetone phosphate acyltransferase (DHAPAT) activity in rat small intestine was investigated by Nycodenz-gradient centrifugation. We found that DHAPAT had a predominant peroxisomal distribution, with a separate enzyme activity located in the microsomal fraction, the same distribution as found in rat liver. The effect of feeding rats on a diet with 20% (w/w) partially hydrogenated fish oil (PHFO) or 0.3% clofibrate on the activity of DHAPAT in rat small intestine and liver was studied. Both 20% PHFO and 0.3% clofibrate gave a 1.8-fold stimulation of the specific activities of DHAPAT in peroxisomes of the small intestine, whereas in the liver 20% PHFO gave a 1.4-fold stimulation and 0.3% clofibrate a 1.6-fold stimulation of the total DHAPAT activities in the postnuclear supernatant. The specific activities of DHAPAT in liver were not affected.

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Orange Juice and Its Component, Hesperidin, Decrease the Expression of Multidrug Resistance-Associated Protein 2 in Rat Small Intestine and Liver

Journal of Biomedicine and Biotechnology ◽

10.1155/2011/502057 ◽

2011 ◽

Vol 2011 ◽

pp. 1-8 ◽

Cited By ~ 8

Author(s):

Minoru Watanabe ◽

Naoki Matsumoto ◽

Yuko Takeba ◽

Toshio Kumai ◽

Masami Tanaka ◽

...

Keyword(s):

Small Intestine ◽

Multidrug Resistance ◽

Orange Juice ◽

Tap Water ◽

Pharmacokinetic Parameters ◽

Mrna Levels ◽

Rat Small Intestine ◽

Sprague Dawley ◽

Water Ingestion ◽

Sprague Dawley Rats

We investigated the effects of orange juice (OJ) or hesperidin, a component of OJ, on the pharmacokinetics of pravastatin (PRV) and the expression of both protein and mRNA of multidrug resistance-associated protein 2 (Mrp2) in the rat small intestine and liver. Eight-week-old male Sprague-Dawley rats were used in this study. OJ or a 0.079% hesperidin suspension was administered orally for 2 days. Tap water was given as a control. A single dose of PRV at 100 mg/kg p.o. was administered after 2 days of OJ, hesperidin, or tap water ingestion. The AUC, , andt1/2values of PRV were significantly increased in OJ group. Mrp2 protein and mRNA levels in the small intestine and liver, respectively, were significantly decreased after the ingestion of OJ. The same results were obtained with hesperidin. These results suggest that the changes in PRV pharmacokinetic parameters and the decrease in Mrp2 expression caused by OJ are due to hesperidin in the juice.

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Interactions between the promoter and first intron are involved in transcriptional control of alpha 1(I) collagen gene expression.

Molecular and Cellular Biology ◽

10.1128/mcb.8.11.4851 ◽

1988 ◽

Vol 8 (11) ◽

pp. 4851-4857 ◽

Cited By ~ 68

Author(s):

P Bornstein ◽

J McKay ◽

D J Liska ◽

S Apone ◽

S Devarayalu

Keyword(s):

Growth Hormone ◽

Human Growth Hormone ◽

Transcriptional Control ◽

Rnase Protection Assay ◽

Human Growth ◽

Collagen Gene ◽

Mrna Levels ◽

3T3 Cells ◽

Rnase Protection ◽

First Intron

The first intron of the human collagen alpha 1(I) gene contains several positively and negatively acting elements. We have studied the transcription of collagen-human growth hormone fusion genes, containing deletions and rearrangements of collagen intronic sequences, by transient transfection of chick tendon fibroblasts and NIH 3T3 cells. In chick tendon fibroblasts, but not in 3T3 cells, inversion of intronic sequences containing a previously studied 274-base-pair segment, A274, resulted in markedly reduced human growth hormone mRNA levels as determined by an RNase protection assay. This inhibitory effect was largely alleviated when deletions were introduced in the collagen promoter of plasmids containing negatively oriented intronic sequences. Evidence for interaction of the promoter with the intronic segment, A274, was obtained by gel mobility shift assays. We suggest that promoter-intron interactions, mediated by DNA-binding proteins, regulate collagen gene transcription. Inversion of intronic segments containing critical interactive elements might then lead to an altered geometry and reduced activity of a transcriptional complex in those cells with sufficiently high levels of appropriate transcription factors. We further suggest that the deleted promoter segment plays a key role in directing DNA interactions involved in transcriptional control.

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Na,K-ATPase in diabetic rat small intestine. Changes at protein and mRNA levels and role of glucagon.

Journal of Clinical Investigation ◽

10.1172/jci117287 ◽

1994 ◽

Vol 93 (6) ◽

pp. 2725-2731 ◽

Cited By ~ 14

Author(s):

K Barada ◽

C Okolo ◽

M Field ◽

N Cortas

Keyword(s):

Small Intestine ◽

Diabetic Rat ◽

Mrna Levels ◽

Rat Small Intestine

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Apolipoprotein A-IV synthesis in rat intestine: regulation by dietary triglyceride

AJP Gastrointestinal and Liver Physiology ◽

10.1152/ajpgi.1987.252.5.g662 ◽

1987 ◽

Vol 252 (5) ◽

pp. G662-G666 ◽

Cited By ~ 21

Author(s):

T. F. Apfelbaum ◽

N. O. Davidson ◽

R. M. Glickman

Keyword(s):

Protein Synthesis ◽

Small Intestine ◽

Total Protein ◽

Mrna Levels ◽

Rat Small Intestine ◽

Rat Intestine ◽

Apolipoprotein A ◽

Rat Enterocytes

Apolipoprotein A-IV (apoA-IV) synthesis rates were measured in vivo in rat enterocytes by immunoprecipitation after administration of [3H]leucine into in situ loops of jejunum and ileum. Basal apoA-IV synthesis rates (percent total protein synthesis) were significantly higher in jejunal enterocytes (2.05 +/- 0.54%) compared with ileal enterocytes (0.48 +/- 0.32%) from the same fasted animals. After an acute triglyceride bolus, significant and sustained elevations of apoA-IV synthesis rates were seen in both jejunal and ileal enterocytes with maximal effects noted at 4-6 h. Animals fed diets containing 30% wt/wt triglyceride as saturated (SF) or polyunsaturated (UF) fats for 6 wk had similarly increased rates of apoA-IV synthesis in jejunal enterocytes with both SF (3.73 +/- 0.83%) and UF (3.33 +/- 0.64%) but no change in ileal enterocytes. By contrast, animals consuming a fat-free diet for 3 wk had jejunal apoA-IV synthesis rates indistinguishable from basal values (2.40 +/- 0.45%). Translatable intestinal mRNA levels for pre-apoA-IV after triglyceride increased in parallel to synthesis rates with a 50% increase in jejunum and a 350% increase in ileum observed at 4-6 h. These results suggest that apoA-IV synthesis by rat small intestine increases in response to acute and chronic dietary triglyceride, is maintained in the absence of dietary triglyceride, and may be under pretranslational control.

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Exercise modulates antioxidant enzyme gene expression in rat myocardium and liver

Journal of Applied Physiology ◽

10.1152/jappl.2000.88.5.1791 ◽

2000 ◽

Vol 88 (5) ◽

pp. 1791-1796 ◽

Cited By ~ 45

Author(s):

D. O. Wilson ◽

P. Johnson

Keyword(s):

Glutathione Peroxidase ◽

Antioxidant Enzyme ◽

Enzyme Activities ◽

Transcriptional Control ◽

Rnase Protection Assay ◽

Antioxidant Enzyme Activities ◽

Mrna Levels ◽

Rnase Protection ◽

Spontaneously Hypertensive ◽

Wistar Kyoto

Our previous studies have shown that exercise caused changes in the tissue activities of the antioxidant enzymes glutathione peroxidase, superoxide dismutase, and catalase in spontaneously hypertensive (SH) and Wistar-Kyoto (WKY) rats. To determine whether the changes observed were due to changes in mRNA levels of the enzymes, levels of tissue mRNA were determined by quantitative RNase protection assay. Comparisons of tissue enzyme activities and mRNA levels in sedentary and exercised animals showed that, in some cases (e.g., glutathione peroxidase in SH and WKY myocardium), parallel changes in enzyme activity and mRNA levels occurred, whereas in other cases (e.g., catalase in SH and WKY liver), nonparallel changes were found. Exercise of hypertensive rats altered antioxidant enzyme mRNA levels to those seen in normotensive animals in some, but not all, cases. The results suggest that transcriptional control over changes in exercise-related antioxidant enzyme activities is operative in some cases, although in other cases posttranscriptional regulatory mechanisms may exist.

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Age-related changes in chemical composition and physical properties of mucus glycoproteins from rat small intestine

Biochemical Journal ◽

10.1042/bj2150405 ◽

1983 ◽

Vol 215 (2) ◽

pp. 405-411 ◽

Cited By ~ 66

Author(s):

M D Shub ◽

K Y Pang ◽

D A Swann ◽

W A Walker

Keyword(s):

Small Intestine ◽

Amino Acid ◽

Reciprocal Relationship ◽

Molar Ratio ◽

Chemical Compositions ◽

Rat Small Intestine ◽

Newborn Rats ◽

Adult Rat ◽

Age Related ◽

Mucus Glycoproteins

Mucus glycoproteins from newborn and adult rat small intestine were radiolabelled in vivo with Na2 35SO4 and isolated from mucosal homogenates by using Sepharose 4B column chromatography followed by CsCl-density-gradient centrifugation. Non-covalently bound proteins, lipids and nucleic acids were not detected in the purified glycoproteins. Amino acid, carbohydrate and sulphate compositions were similar to chemical compositions reported for other intestinal mucus glycoproteins, as were sedimentation properties. There were, however, important differences in the chemical and physical characteristics of the mucus glycoproteins from newborn and adult animals. The buoyant density in CsCl was higher for the glycoproteins from newborn rats (1.55 g/ml versus 1.47 g/ml). On sodium dodecyl sulphate/polyacrylamide/agarose-gel electrophoresis, the glycoprotein from newborn rats had a greater mobility than the adult-rat sample. Although both preparations had similar general amino acid compositions, variations were observed for individual amino acids. The total protein content was greater in the glycoprotein from newborn animals (27%, w/w, versus 18%, w/w). The molar ratio of carbohydrate to protein was less in the newborn, primarily owing to a decreased fucose and N-acetylgalactosamine content. Comparison of the molar ratio of fucose and sialic acid to galactose for both glycoproteins demonstrated a reciprocal relationship similar to that described by Dische [(1963) Ann. N.Y. Acad. Sci. 106, 259-270]. The sulphate content was greater in the glycoprotein from newborn rats (5.5%, w/w, versus 0.9%, w/w). Both had similar sedimentation coefficients in a dissociative solvent. These results suggest an age-related difference in the types of mucus glycoproteins synthesized by small intestine.

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