scholarly journals Localization of Astrovirus in Experimentally Infected Turkeys as Determined by In Situ Hybridization

2002 ◽  
Vol 39 (5) ◽  
pp. 595-598 ◽  
Author(s):  
E. Behling-Kelly ◽  
S. Schultz-Cherry ◽  
M. Koci ◽  
L. Kelley ◽  
D. Larsen ◽  
...  
Keyword(s):  
Small Intestine ◽  
In Situ Hybridization ◽  
Experimental Period ◽  
Intestinal Epithelial ◽  
Distal Small Intestine ◽  
Turkey Poults ◽  
Proximal Small Intestine ◽  
Crypt Hyperplasia ◽  
Negative Sense

Twenty-one 3-day-old turkey poults from British United Turkeys of America were orally inoculated with a recently characterized astrovirus, TAstV-2, isolated from turkeys with poult enteritis and mortality syndrome. At 1, 2, 3, 4, 5, 7, and 9 days postinfection (dpi), three inoculated birds were euthanatized, and tissues (intestines, spleen, bursa, and thymus) were collected immediately into 10% neutral buffered formalin. Inoculated birds were diarrheic by 3 dpi, and frothy feces persisted throughout the experimental period. Histologically, there was only slight evidence of enteric damage, which was characterized by mild epithelial necrosis, lamina propria infiltrates, minimal villus atrophy, and mild crypt hyperplasia. In situ hybridization, using a negative sense digoxigenin-labeled riboprobe to the capsid gene of TAstV-2, revealed viral RNA in intestinal epithelial cells at the basal margins of the villi, in distal small intestine, and in cecum at 2 dpi, with subsequent extension to epithelium of the large intestine and proximal small intestine (3–5 dpi). Minimal virus remained by 9 dpi.

Intestinal myoelectrical activity and transit time in chronic portal hypertension

1992 ◽  
Vol 263 (4) ◽  
pp. G474-G479 ◽  
Author(s):  
J. J. Stewart ◽  
H. D. Battarbee ◽  
G. E. Farrar ◽  
K. W. Betzing
Keyword(s):  
Small Intestine ◽  
Portal Hypertension ◽  
Portal Vein ◽  
Transit Time ◽  
Experimental Period ◽  
Phase Iii ◽  
Adult Rats ◽  
Myoelectrical Activity ◽  
Distal Small Intestine ◽  
Proximal Small Intestine

This study was designed to determine the effects of portal hypertension on intestinal myoelectrical activity and propulsion. In a single surgery, adult rats were implanted with a serosal electrode at each quarter of the small intestine, and portal hypertension was produced by calibrated constriction of the portal vein. To determine intestinal transit, portal vein-stenosed (PVS) and sham-operated animals were chronically implanted with a catheter in the proximal small intestine. Transit time was determined by measuring the progression of radioactive chromium along the bowel. Studies were conducted 6, 9, and 14 days after surgical preparation. Portal hypertension was associated with both transient and persistent changes in intestinal myoelectrical activity during the experimental period. Slow wave frequency was significantly reduced in the proximal small intestine on all test days and in the distal small intestine on day 14. Occurrence of the migrating myoelectric complex was reduced on days 6 and 9. Phase III amplitude was significantly reduced in the distal small intestine on all test days. Changes in intestinal myoelectrical activity in PVS animals were not associated with measurable changes in intestinal propulsion. The results suggest that both transient and persistent changes in intestinal myoelectrical activity occur during the 2-wk period after portal vein stenosis. The functional significance of the changes is unknown.

Glucose and glutamine provide similar proportions of energy to mucosal cells of rat small intestine

1997 ◽  
Vol 273 (4) ◽  
pp. G968-G978 ◽  
Author(s):  
Sharon E. Fleming ◽  
Kirsten L. Zambell ◽  
Mark D. Fitch
Keyword(s):  
Small Intestine ◽  
Epithelial Cells ◽  
Metabolic Pathways ◽  
Glycolytic Flux ◽  
Net Energy ◽  
Intestinal Epithelial ◽  
Atp Production ◽  
Distal Small Intestine ◽  
Mucosal Cells ◽  
In Cells

The objectives of this study were to establish a reliable method for quantifying glycolytic flux in intestinal epithelial cells, to determine the proportion of energy provided to small intestine epithelial cells by glucose vs. glutamine, and to determine whether there was an energetic advantage to having both substrates present simultaneously. There was substantial retention of 3H in alanine and lactate when [2-3H]glucose was used as tracer for quantifying glycolysis, and the magnitude of the3H retention was influenced by the presence of other substrates and metabolites. Detritiation was at least 99% complete, however, when [3-3H]glucose was used as tracer in this system and the tritium was recovered as3H2O. Glycolytic flux was six- to sevenfold higher in cells of the proximal than distal small intestine but was not significantly different for young adult (4 mo) vs. aged adult (24 mo) rats. Net ATP production from exogenous substrates was higher when both glucose and glutamine were present simultaneously than when either substrate was present alone, and glucose was calculated to provide 50–60% of the net ATP produced from these two substrates. Most of the energy produced from glucose was produced via the anaerobic metabolic pathways (78% for glucose alone, 95% with glucose and glutamine). Net energy production was calculated to be 10% lower in cells from aged animals than in those from young animals, since CO2 production from these major substrates was lower in cells from aged animals.

Transport of butyric acid in vascularly perfused anuran small intestine: importance of pH and anion transport

1986 ◽  
Vol 250 (4) ◽  
pp. G469-G474
Author(s):  
D. Hollander ◽  
E. M. Gerard ◽  
C. A. Boyd
Keyword(s):  
Small Intestine ◽  
Butyric Acid ◽  
Nonlinear Function ◽  
Anion Transport ◽  
Transport Protein ◽  
Disulfonic Acid ◽  
Flux Analysis ◽  
Acid Transport ◽  
Distal Small Intestine ◽  
Proximal Small Intestine

Butyric acid transport was studied in the isolated, vascularly perfused frog small intestine. At luminal butyric acid concentrations of 5-50 mM, absorption was a nonlinear function of the luminal concentration, whereas the relationship of absorption to concentration remained linear at 0-1,000 microM. The most important factor regulating the rate and direction of butyric acid transport was the pH. We used unidirectional flux analysis to determine net transport across the epithelium while the pH of the luminal or vascular compartments was changed. We found a four- to fivefold decrease in butyric acid transport into the portal circulation as the lumen pH was increased from 6.0 to 8.0. The pH of the vascular perfusate influenced the vascular-to-lumen transport of butyric acid in the same proportions. The second important regulatory factor of butyric acid transport was the 4,4'-diisothiocyananostilbene-2,2'-disulfonic acid (DIDS)-sensitive anion transport protein. DIDS added to the lumen at 10(-6) M decreased butyric acid transport by approximately 40% at pH 7.4. DIDS also inhibited butyric acid transport when added to the vascular perfusate or when transport was measured in a vascular-to-lumen direction. We suggest that, at the relatively low pH of the proximal small intestine, butyric acid becomes protonated and lipophilic and is mainly transported directly through the cell membrane. At the more alkaline pH of the distal small intestine butyric acid is in the ionized form and transport by the DIDS-sensitive anion transport protein may predominate.

scholarly journals DES2 protein is responsible for phytoceramide biosynthesis in the mouse small intestine

2004 ◽  
Vol 379 (3) ◽  
pp. 687-695 ◽  
Author(s):  
Fumio OMAE ◽  
Masao MIYAZAKI ◽  
Ayako ENOMOTO ◽  
Minoru SUZUKI ◽  
Yusuke SUZUKI ◽  
...  
Keyword(s):  
Small Intestine ◽  
Epithelial Cells ◽  
Intestinal Epithelial ◽  
Vitro Assay ◽  
Peptide Antibody ◽  
Mouse Small Intestine ◽  
Mrna Content ◽  
Crypt Cells

The C-4 hydroxylation of sphinganine and dihydroceramide is a rate-limiting reaction in the biosynthesis of phytosphingolipids. Mouse DES1 (MDES1) cDNA homologous to the Drosophila melanogaster degenerative spermatocyte gene-1 (des-1) cDNA leads to sphingosine Δ4-desaturase activity, and another mouse homologue, MDES2, has bifunctional activity, producing C-4 hydroxysphinganine and Δ4-sphingenine in yeast [Ternes, Franke, Zahringer, Sperling and Heinz (2002) J. Biol. Chem. 277, 25512–25518]. Here, we report the characterization of mouse DES2 (MDES2) using an in vitro assay with a homogenate of COS-7 cells transfected with MDES2 cDNA and N-octanoyl-sphinganine and sphinganine as substrates. MDES2 protein prefers dihydroceramide as a substrate to sphinganine, and exhibits dihydroceramide Δ4-desaturase and C-4 hydroxylase activities. MDES2 mRNA content was high in the small intestine and abundant in the kidney. In situ hybridization detected signals of MDES2 mRNA in the crypt cells. Immunohistochemistry using an anti-MDES2 peptide antibody stained the crypt cells and the adjacent epithelial cells. These results suggest that MDES2 is the dihydroceramide C-4 hydroxylase responsible for the biosynthesis of enriched phytosphingoglycolipids in the microvillous membranes of intestinal epithelial cells.

scholarly journals Intestinal absorption of calcium in rats given diets containing casein or amino acid mixture: the role of casein phosphopeptides

1983 ◽  
Vol 49 (1) ◽  
pp. 67-76 ◽  
Author(s):  
Yeon Sook Lee ◽  
Tadashi Noguchi ◽  
Hiroshi Naito
Keyword(s):  
Small Intestine ◽  
Amino Acid ◽  
Calcium Absorption ◽  
Specific Effect ◽  
Basal Diet ◽  
Amino Acid Mixture ◽  
Acid Mixture ◽  
Distal Small Intestine ◽  
Casein Phosphopeptides

1. In an attempt to investigate calcium absorption in the rat during the postprandial period, with the least alteration of the physical environment, the undisturbed small intestine was ligated in situ 2·5 or 3·0 h after ingestion of a diet containing 200 g casein/kg or an equivalent amino acid mixture, or 925 g casein/kg. Estimation of Ca absorption was made by comparing the amount of soluble 40Ca or 45Ca in the contents of segments from the rats receiving 45Ca by intubation 30 min after withdrawal of food, ligated after a further 30 min, then killed after 0 or 30 min.2. Under conditions such that the estimated amount of a marker, polyethylene glycol, in segments ligated in a defined position was little changed in rats killed 30 min apart, the difference in the amount of soluble 40Ca was much higher in the rats fed on the basal diet containing 200 g casein/kg than in other groups.3. This specific effect on Ca absorption, particularly in the distal portion of the small intestine, could be seen also after 45Ca was directly injected into ligated segments in situ. The amount of 45Ca in the portal blood 15 min after injection of the label was also highest in the rats given the basal diet.4. The results were in agreement with our previous findings that the formation and accumulation of casein phosphopeptides causes an increase in the amount of soluble Ca in the distal small intestine.

scholarly journals Tumor necrosis factor mRNA localized to Paneth cells of normal murine intestinal epithelium by in situ hybridization.

1990 ◽  
Vol 171 (1) ◽  
pp. 327-332 ◽  
Author(s):  
S Keshav ◽  
L Lawson ◽  
L P Chung ◽  
M Stein ◽  
V H Perry ◽  
...  
Keyword(s):  
Small Intestine ◽  
In Situ Hybridization ◽  
Lamina Propria ◽  
Northern Blot Analysis ◽  
Surface Membrane ◽  
Paneth Cells ◽  
Intestinal Physiology ◽  
Tumor Necrosis Factor Mrna ◽  
Necrosis Factor

Paneth cells in normal murine small intestine contain TNF mRNA that is readily detectable by in situ hybridization, unlike resident macrophages in lamina propria, which are negative. Northern blot analysis of whole tissue shows the presence of mRNA that has the same electrophoretic mobility as TNF mRNA from activated macrophages. A low level of TNF bioactivity, but no immunoreactivity, was detected in normal small intestine, and TNF production in resting Paneth cells appears to be post-transcriptionally controlled. Typical leukocyte surface membrane markers were not found on Paneth cells, but were expressed by the surrounding lamina propria macrophages. Paneth cells are thus epithelial cells with leukocyte-like secretory potential that may be important in intestinal physiology and pathology.

scholarly journals Expression of c-myc proto-oncogene in normal human intestinal epithelium.

1989 ◽  
Vol 37 (4) ◽  
pp. 541-545 ◽  
Author(s):  
J ten Kate ◽  
S Eidelman ◽  
F T Bosman ◽  
I Damjanov
Keyword(s):  
In Situ Hybridization ◽  
Epithelial Cell ◽  
Intestinal Epithelial Cell ◽  
Human Colon ◽  
Intestinal Epithelial ◽  
Cell Compartments ◽  
Entire Thickness ◽  
Normal Human ◽  
Human Intestinal Epithelium

We studied the expression of the human c-myc proto-oncogene in normal human colon epithelium by both in situ hybridization and immunohistochemistry. c-myc was found to be expressed uniformly throughout the entire thickness of the colon epithelium. The present findings do not support the contention that the c-myc proto-oncogene is primarily expressed in proliferating intestinal epithelial cell compartments.

scholarly journals Localization of amidating enzymes (PAM) in rat gastrointestinal tract.

1993 ◽  
Vol 41 (11) ◽  
pp. 1617-1622 ◽  
Author(s):  
A Martínez ◽  
M A Burrell ◽  
M Kuijk ◽  
L M Montuenga ◽  
A Treston ◽  
...  
Keyword(s):  
Small Intestine ◽  
In Situ Hybridization ◽  
Gastrointestinal Tract ◽  
Digestive Tract ◽  
Endocrine Cells ◽  
Regulatory Peptides ◽  
Serial Sections ◽  
Gastric Glands ◽  
Amidating Enzymes

We studied the distribution of the two enzymes involved in post-translational C-terminal alpha-amidation of regulatory peptides in rat digestive tract, using immunocytochemical methods and in situ hybridization techniques. The enzymes were located in most of the fibers and neurons of the myenteric and submucous plexus throughout the entire digestive tract and in endocrine cells of the stomach and colon. Staining of reverse-face serial sections demonstrated that the enzymes in endocrine cells of the stomach co-localized with gastrin in the bottom of the gastric glands. Some gastrin-immunoreactive cells near the neck of the gland were negative for PAM, suggesting that amidation takes place only in the more mature cells. In the colon all cells immunoreactive for glucagon and GLP1 were also positive for peptidylglycine alpha-hydroxylating monooxygenase (PHM) but not for peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL). The absence of immunoreactivity for the amidating enzymes in endocrine cells of the small intestine, known to produce C-terminally amidated peptides, suggests the existence of other amidating enzymes.

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