The effect of Escherichia coli heat-stable (STA) enterotoxin on in vitro uptake of amino acids by small intestine of sucking rats during fluid accumulation

1993 ◽  
Vol 69 (3) ◽  
pp. 757-766 ◽  
Author(s):  
◽  
Khin-Ma Ung-U * ◽  
◽  
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Small Intestine ◽  
Fluid Accumulation ◽  
Heat Stable

scholarly journals Evaluation of Escherichia coli STb toxin in an in vitro organ culture model (IVOC) / Avaliação de toxina STb de Escherichia coli em modelo de cultura de órgãos in vitro (IVOC)

2021 ◽  
Vol 4 (3) ◽  
pp. 3347-3354
Author(s):  
Cristina Paiva De Sousa ◽  
J. Daniel Dubreuil
Keyword(s):  
Escherichia Coli ◽  
Small Intestine ◽  
Organ Culture ◽  
Morphometric Analysis ◽  
Heat Stable ◽  
Absorptive Cells ◽  
Culture Model ◽  
In Vitro Organ Culture ◽  
Culture Supernatants

ETEC pathogenesis comprises adhesion to the small intestine, colonization and enterotoxin production. STb is one of the heat-stable toxins produced by ETEC. Previous reports, using culture supernatants of STb-positive ETEC strains, indicated loss of villous absorptive cells causing mild atrophy and microscopic alterations in jejunum mucosa. These culture supernatants contained many other compounds beside STb toxin and in addition the quantity of toxin in these supernatants was not determined. Thus, this study was undertaken to evaluate the effect of pure STb toxin on piglet jejunum explants in an in vitro organ culture (IVOC) model. Tissues of piglets of 11 weeks were used and put into culture. Morphometric analysis of tissues revealed that villous epithelial area was reduced in tissues treated with pure STb after 3, 4 and 5 hours (p 0.0001) compared to untreated tissues. STb-treated tissues presented atrophic villi due to loss of villi tip. Our data shows that, in piglet jejunum explants, pure STb toxin can lead to cell modification and consequently to destruction, seen as villi atrophy. These changes result in a reduced absorptive area and could be partly responsible for the diarrhea observed in the animal following STb intoxication.

In vivo and in vitro Absorption of Amino Acids and Dipeptides in the Small Intestine of Uremic Rats

Nephron ◽  
1982 ◽  
Vol 31 (3) ◽  
pp. 273-276 ◽  
Author(s):  
G. Sterner ◽  
T. Lindberg ◽  
T. Denneberg
Keyword(s):  
Amino Acids ◽  
Small Intestine

Inhibition of Escherichia coli heat-stable enterotoxin by indomethacin and chlorpromazine

1980 ◽  
Vol 29 (3) ◽  
pp. 908-913
Author(s):  
R N Greenberg ◽  
F Murad ◽  
B Chang ◽  
D C Robertson ◽  
R L Guerrant
Keyword(s):  
Escherichia Coli ◽  
Guanylate Cyclase ◽  
Fluid Secretion ◽  
Cyclic Guanosine Monophosphate ◽  
Guanosine Monophosphate ◽  
Enterotoxigenic Escherichia Coli ◽  
Fluid Accumulation ◽  
Intestinal Tissue ◽  
Suckling Mice ◽  
Heat Stable

Purified heat-stable enterotoxin (ST) from a procine strain of enterotoxigenic Escherichia coli activates quanylate cyclase in particulate fractions of rat intestinal tissue and induces fluid accumulation in suckling mice. These effects of ST were examined in the presence of either indomethacin or chlorpromazine. We also examined the effects of these two drugs on fluid accumulation in suckling mice induced by the 8-bromo analog of cyclic guanosine monophosphate. Either indomethacin or chlorpromazine reduced ST activation of guanylate cyclase. Both drugs also reduced intestinal fluid accumulation in suckling mice that resulted from submaximal doses of ST (both P < 0.001). However, there was no reduction in fluid secretion by either drug when a maximally effective dose of ST was used, suggesting that inhibition of fluid secretion by both drugs can be overcome by increasing the ST dose and that a threshold level of guanylate cyclase activity results in maximal secretory response. Both drugs also reduced basal guanylate cylase activity in rat intestinal tissue and fluid secreton in suckling mice. Chlorpromazine also reduced intestinal secretion mediated by 8-bromo cyclic guanosine monophosphate (P < 0.001). These findings indicate that chlorpromazine interferes with the effects of ST both before and after its activation of guanylate cyclase, whereas indomethacin interfers with ST only before its activation of guanylate cyclase.

In Vitro Absorption of Amino Acids by the Small Intestine of Sheep

1976 ◽  
Vol 42 (1) ◽  
pp. 201-207 ◽  
Author(s):  
W. A. Phillips ◽  
K. E. Webb ◽  
J. P. Fontenot
Keyword(s):  
Amino Acids ◽  
Small Intestine

scholarly journals Nutritional availability of amino acids from protein cross-linked to protect against degradation in the rumen

1984 ◽  
Vol 52 (2) ◽  
pp. 239-247 ◽  
Author(s):  
John R. Ashes ◽  
Jim L. Mangan ◽  
Gurcharn S. Sidhu
Keyword(s):  
Amino Acids ◽  
Small Intestine ◽  
Medicago Sativa ◽  
Terminal Ileum ◽  
Milk Protein ◽  
The Other ◽  
Molar Basis ◽  
Lactating Goats ◽  
Total Milk

1. Casein was labelled with pairs of radioactive amino acids, lysine, tyrosine and leucine, one with I4C and the other with 3H, by jugular infusion into lactating goats followed by isolation of the double-labelled casein from the milk. Total milk protein was similarly labelled by jugular infusion of [35S]cystine. U-14C-labelled fraction- 1 leaf protein was isolated from lucerne (Medicago sativa) grown in an atmosphere of 14C022. The proteins were treated withdifferent levels(333 and667 mmol/kgprotein) offormaldehyde, glutaraldehyde and glyoxal.3. Absorption from the small intestine was measured in sheep with fistulas in the abomasum and terminal ileum, using Cr-EDTA as the digesta flow marker, by introducing radioactive casein into the abomasum.4. Lysine, tyrosine and cystine became increasingly unavailable for absorption from the small intestine of sheep with increasing levels of aldehyde. At the lower level (333 mmol/kg) the proportions of the amino acids that were unavailable were 0.192, 0.051 and 0.123 respectively. At the higher level of formaldehyde (667 mmol/kg) the corresponding values were 0.335, 0.201 and 0.432 respectively. Leucine was not made unavailable with formaldehyde.5. The proportions of lysine, tyrosine and leucine that were unavailable were higher, on a molar basis, after treatment of the proteins with the dialdehydes glutaraldehyde and glyoxal than after treatment with formaldehyde. However, the extent of protein protection provided by the dialdehydes in the rumen, measured using an in vitro procedure, was lower.

Escherichia coli heat-stable toxin: its effect on motility of the small intestine

1982 ◽  
Vol 242 (4) ◽  
pp. G360-G363 ◽  
Author(s):  
J. R. Mathias ◽  
J. Nogueira ◽  
J. L. Martin ◽  
G. M. Carlson ◽  
R. A. Giannella
Keyword(s):  
Escherichia Coli ◽  
Small Intestine ◽  
Action Potential ◽  
Myoelectric Activity ◽  
Complex Activity ◽  
E Coli ◽  
Heat Stable ◽  
Rabbit Small Intestine ◽  
Weight Substance

Escherichia coli heat-stable enterotoxin is a low-molecular-weight substance that has been shown to induce the active secretion of fluid and electrolytes in the small intestine. In this study, we have characterized the effects of purified E. coli heat-stable toxin (ST, strain 18D, serotype 042:K86:H37) on the motility of rabbit small intestine by using myoelectric recording techniques. Substances, such as cholera toxin, that activate the adenylate cyclase-cAMP system induced predominantly migrating action-potential complex activity. E. coli ST, a toxin that activates the guanylate cyclase-cGMP system, was infused into isolated in vivo ileal loops of New Zealand White rabbits. Inactivated toxin was also studied by exposing the ST to 1 mM dithiothreitol for 90 min. Active E. coli ST induced only repetitive bursts of action potentials. When the toxin was inactivated with dithiothreitol, no alteration in myoelectric activity was observed. We speculate that repetitive bursts of action-potential activity may represent a virulent factor of the bacterium, altering motor activity to slow transit and allowing for bacterial proliferation and invasion.

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