Correction to: Small Intestinal Length Associates with Serum Triglycerides Before and After LRYGB

Sodium butyrate (SB) provided orally favours body growth and maturation of the gastrointestinal tract (GIT) in milk-fed pigs. In weaned pigs, conflicting results have been obtained. Therefore, we hypothesised that the effects of SB (3 g/kg DM intake) depend on the period (before v. after weaning) of its oral administration. From the age of 5 d, thirty-two pigs, blocked in quadruplicates within litters, were assigned to one of four treatments: no SB (control), SB before (for 24 d), or after (for 11–12 d) weaning and SB before and after weaning (for 35–36 d). Growth performance, feed intake and various end-point indices of GIT anatomy and physiology were investigated at slaughter. The pigs supplemented with SB before weaning grew faster after weaning than the controls (P < 0·05). The feed intake was higher in pigs supplemented with SB before or after weaning (P < 0·05). SB provided before weaning improved post-weaning faecal digestibility (P < 0·05) while SB after weaning decreased ileal and faecal digestibilities (P < 0·05). Gastric digesta retention was higher when SB was provided before weaning (P < 0·05). Post-weaning administration of SB decreased the activity of three pancreatic enzymes and five intestinal enzymes (P < 0·05). IL-18 gene expression tended to be lower in the mid-jejunum in SB-supplemented pigs. The small-intestinal mucosa was thinner and jejunal villous height lower in all SB groups (P < 0·05). In conclusion, the pre-weaning SB supplementation was the most efficient to stimulate body growth and feed intake after weaning, by reducing gastric emptying and intestinal mucosa weight and by increasing feed digestibility.

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Three-dimensional CT enterography versus barium follow-through examination in measurement of remnant small intestinal length in short bowel syndrome patients

Abdominal Radiology ◽

10.1007/s00261-018-1597-x ◽

2018 ◽

Vol 43 (11) ◽

pp. 2955-2962 ◽

Cited By ~ 2

Author(s):

Wei Cheng ◽

Shaoyi Zhang ◽

Jian Wang ◽

Changsheng Zhou ◽

Yousheng Li ◽

...

Keyword(s):

Short Bowel Syndrome ◽

Three Dimensional ◽

Ct Enterography ◽

Short Bowel ◽

Intestinal Length ◽

Small Intestinal

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The putative ‘link’ glycopeptide associated with mucus glycoproteins. Composition and properties of preparations from the gastrointestinal tracts of several mammals

Biochemical Journal ◽

10.1042/bj2610637 ◽

1989 ◽

Vol 261 (2) ◽

pp. 637-647 ◽

Cited By ~ 40

Author(s):

A M Roberton ◽

M Mantle ◽

R E F Fahim ◽

R D Specian ◽

A Bennick ◽

...

Keyword(s):

Gel Electrophoresis ◽

Proteinase Inhibitors ◽

Polyacrylamide Gel Electrophoresis ◽

Collaborative Study ◽

Polyacrylamide Gel ◽

Disulphide Bond ◽

Before And After ◽

Amino Acid Profiles ◽

Small Intestinal ◽

Similar Amino Acid

The existence of a discrete ‘link’ peptide in epithelial mucins has been debated for many years. There is evidence that at least some mucins contain a specific ‘link’ peptide (or glycopeptide) that enhances mucin polymerization by forming disulphide bridges to large mucin glycoprotein subunits. A major difficulty has been to know whether the reported differences in putative ‘link’ components represent artifacts generated by inter-laboratory differences in technical procedures used in mucin purification. The present paper outlines the results of a collaborative study involving five laboratories and 53 samples of purified gastrointestinal mucins (including salivary, gastric, small-intestinal and colonic mucins) prepared by five techniques from four different animal species. An early step in mucin purification in all cases was the addition of proteinase inhibitors. Representative mucins were analysed for their composition, electrophoretic mobility in SDS/polyacrylamide-gel electrophoresis before and after disulphide-bond reduction, and for their reactivity with monospecific antibodies developed against the 118 kDa putative ‘link’ glycopeptide isolated from either rat or human small-intestinal mucins. Our results indicate that, despite differences in laboratory techniques, preparative procedures, organs and species, each of the purified mucins contained a ‘link’ component that was released by disulphide-bond reduction and produced a band on SDS/polyacrylamide-gel electrophoresis at a position of approx. 118 kDa. After electroelution and analyses, the 118 kDa bands from the different mucins were found to have similar amino acid profiles and to contain carbohydrate. It would appear therefore that a ‘link’ glycopeptide of molecular mass approx. 118 kDa is common to all of the gastrointestinal mucins studied.

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LOCALIZATION OF β-GALACTOSIDASES AND ACID PHOSPHATASE IN THE SMALL INTESTINAL WALL COMPARISON OF ADULT AND SUCKLING RAT

Journal of Histochemistry & Cytochemistry ◽

10.1177/17.5.341 ◽

1969 ◽

Vol 17 (5) ◽

pp. 341-347 ◽

Cited By ~ 21

Author(s):

CHRISTER NORDSTRÖM ◽

OTAKAR KOLDOVSKÝ ◽

ARNE DAHLQVIST

Keyword(s):

Acid Phosphatase ◽

Intestinal Wall ◽

Quantitative Comparison ◽

Distribution Profile ◽

Before And After ◽

Fresh Frozen ◽

Old Rats ◽

Small Intestinal ◽

Different Parts ◽

Flat Distribution

By horizontal sectioning of fresh frozen pieces of rat intestinal wall different parts of the villi and crypts were isolated. The sections were collected in groups, homogenized and used for enzyme analyses. Single sections for histologic examination were taken before and after each collection. A quantitative comparison of the distribution of the two intestinal β-galactosidases, EC 3.2.1.23 (neutral and acid β-galactosidase), and the acid phosphatase, EC 3.1.3.2, in jejunum and ileum of adult and suckling (12 days old) rats was performed. The neutral β-galactosidase, which corresponds to the enzyme usually called lactase, was always present along the villi with the highest activities in the apical halves of the villi. This distribution profile is typical for digestion enzymes. The acid β-galactosidase, which is chiefly a heterogalactosidase, and acid phosphatase were found to have a rather flat distribution profile with about the same activities along the villi and in the crypts. The only exception was the ileum of suckling rat, in which especially the acid β-galactosidase showed higher activity in the villi and decreased toward the crypts. The results support the concept that the neutral β-galactosidase is responsible for the digestion of dietary lactose, while the acid β-galactosidase seems to have a different functional significance. That this enzyme is distributed in parallel with the acid phosphatase is consistent with the suggestion that the acid β-galactosidase may be a lysosomal enzyme.

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Interferon β-1b effects on cytokine mRNA in peripheral mononuclear cells in multiple sclerosis

Multiple Sclerosis Journal ◽

10.1177/135245859600100502 ◽

1996 ◽

Vol 1 (5) ◽

pp. 262-269 ◽

Cited By ~ 41

Author(s):

PV Byskosh ◽

AT Reder

Keyword(s):

Multiple Sclerosis ◽

Mononuclear Cells ◽

Mrna Levels ◽

Cytokine Mrna ◽

Serum Triglycerides ◽

Tnf Α ◽

Before And After ◽

Peripheral Mononuclear Cells ◽

Ifn Γ ◽

Polymerase Chain

IFN-β reduces the number and severity of exacerbations of multiple sclerosis (MS), presumably by modifying immune regulation. We used semiquantitative polymerase chain reaction (RT-PCR) to measure mRNA levels for cytokines before and after IFN β-1b therapy. mRNA was extracted from mononuclear cells of nine healthy controls and 31 patients with MS. Before therapy, IL-10 and leukemia inhibitory factor (UF) mRNA levels were elevated in stable MS compared to active MS. Twenty four hours after IFN β-1b treatment, mRNA levels for IL-1, IL-2, IL-4, IL-6, IL-10, IL-12, IL-13, IFN-γ, TNF-α and UF had not changed. At 1 week, TNF-α mRNA increased and IL-10 and UF mRNA rose in 75% of patients. IL-2, IL-4, IL-12, IL-13 and IFN-γ did not change. At 3 months, cytokine mRNA returned to baseline levels. mRNA for the IFN-induced antiviral enzyme, 2, 5-OAS, rose by 24 h, peaked at 1 week, and remained elevated thereafter. Serum triglycerides and liver enzymes rose after therapy. Increased SGPT at 3 months correlated with TNF-α mRNA levels, suggesting that cytokines may cause some side effects of IFN β-1b. Baseline cytokine mRNA levels reflect disease activity, but the therapeutic effect of IFN β-1b does not appear to be explained by changes in cytokine mRNA levels.

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The effect of dietary protein source and guar gum on gastrointestinal growth and enteroglucagon secretion in the rat

British Journal Of Nutrition ◽

10.1079/bjn19870070 ◽

1987 ◽

Vol 58 (1) ◽

pp. 65-72 ◽

Cited By ~ 16

Author(s):

Susan Southon ◽

Jennifer M. Gee ◽

I. T. Johnson

Keyword(s):

Dietary Protein ◽

Wistar Rats ◽

Guar Gum ◽

Protein Source ◽

Endocrine Activity ◽

Intestinal Length ◽

Daily Food ◽

Male Wistar Rats ◽

Small Intestinal ◽

Dietary Protein Source

1. Male Wistar rats (approximately 100 g) were given fibre-free semi-synthetic diets containing either casein or albumin (168 g/kg diet) as the protein source with or without guar gum (75 g/kg diet) (casein, albumin, casein- guar gum and albumin-guar gum groups).2. Small intestinal length, weights of caecal tissue and contents and plasma enteroglucagon concentration were significantly increased in guar-gum-fed animals compared with the fibre-free groups.3. Total caecal weight and plasma enteroglucagon concentration were higher in the albumin-guar gum group compared with the casein-guar gum group. The weights of caecal tissue and contents were significantly increased in rats given the fibre-free albumin diet compared with those consuming a similar diet with casein as the protein source, although daily food intake tended to be lower.4. It is concluded that the effect of materials classed as dietary fibre may be significantly influenced by the non- polysaccharide component of the diet, and that such interactions may influence both the growth and endocrine activity of the gastrointestinal tract.

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