scholarly journals Peristaltic transport of a particulate suspension in the small intestine

2017 ◽  
Vol 44 ◽  
pp. 143-159 ◽  
Author(s):  
Matthew D. Sinnott ◽  
Paul W. Cleary ◽  
Simon M. Harrison
Keyword(s):  
Small Intestine ◽  
Peristaltic Transport ◽  
Particulate Suspension

scholarly journals High-molecular-weight polymers from dietary fiber drive aggregation of particulates in the murine small intestine

2018 ◽  
Author(s):  
Asher Preska Steinberg ◽  
Sujit S. Datta ◽  
Thomas Naragon ◽  
Justin C. Rolando ◽  
Said R. Bogatyrev ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Small Intestine ◽  
Dietary Fiber ◽  
High Molecular Weight ◽  
Ex Vivo ◽  
Dietary Fibers ◽  
Chemical Interactions ◽  
Specific Chemical ◽  
Molecular Weights ◽  
Particulate Suspension

AbstractThe lumen of the small intestine (SI) is filled with particulates: microbes, therapeutic particles, and food granules. The structure of this particulate suspension could impact uptake of drugs and nutrients and the function of microorganisms; however, little is understood about how this suspension is re-structured as it transits the gut. Here, we demonstrate that particles spontaneously aggregate in SI luminal fluidex vivo. We find that mucins and immunoglobulins are not required for aggregation. Instead, aggregation can be controlled using polymers from dietary fiber in a manner that is qualitatively consistent with polymer-induced depletion interactions, which do not require specific chemical interactions. Furthermore, we find that aggregation is tunable; by feeding mice dietary fibers of different molecular weights, we can control aggregation in SI luminal fluid. This work suggests that the molecular weight and concentration of dietary polymers play an underappreciated role in shaping the physicochemical environment of the gut.

Computation of peristaltic transport and mixing in the small intestine

2006 ◽  
Vol 39 ◽  
pp. S442-S443 ◽  
Author(s):  
H.S. Udaykumar ◽  
S. Krishman ◽  
S. Dillard ◽  
J.S. Marshall ◽  
K. Schulze
Keyword(s):  
Small Intestine ◽  
Peristaltic Transport ◽  
Transport And Mixing

Electron probe x-ray microanalysis and electron microscopy of amino acid absorption and transport by the small intestine: inhibition by chemical poisons and correlation to the elemental composition of the epithelial cells

1986 ◽  
Vol 44 ◽  
pp. 134-135
Author(s):  
A. J. Tousimis
Keyword(s):  
Small Intestine ◽  
Amino Acid ◽  
Epithelial Cells ◽  
Elemental Composition ◽  
Isotope Labeling ◽  
Structural Components ◽  
X Ray ◽  
Human Small Intestine ◽  
Transport Studies

The elemental composition of amino acids is similar to that of the major structural components of the epithelial cells of the small intestine and other tissues. Therefore, their subcellular localization and concentration measurements are not possible by x-ray microanalysis. Radioactive isotope labeling: I131-tyrosine, Se75-methionine and S35-methionine have been successfully employed in numerous absorption and transport studies. The latter two have been utilized both in vitro and vivo, with similar results in the hamster and human small intestine. Non-radioactive Selenomethionine, since its absorption/transport behavior is assumed to be the same as that of Se75- methionine and S75-methionine could serve as a compound tracer for this amino acid.

The protease phenotype and crystalline nature of the granules of intraepithelial mast cells in Trichinella spiralis-infected mice

1995 ◽  
Vol 53 ◽  
pp. 818-819
Author(s):  
D.S. Friend ◽  
N. Ghildyal ◽  
M.F. Gurish ◽  
K.F. Austen ◽  
R.L. Stevens
Keyword(s):  
Small Intestine ◽  
Mast Cells ◽  
Epithelial Cells ◽  
Lamina Propria ◽  
Trichinella Spiralis ◽  
Intestinal Epithelial ◽  
Carboxypeptidase A ◽  
C3h Mice ◽  
Granule Morphology ◽  
Crystalline Nature

Trichinella spiralis induces a profound mastocytosis and eosinophilia in the small intestine of the infected mouse. Mouse mast cells (MC) store in their granules various combinations of at least five chymotryptic chymases [designated mouse MC protease (mMCP) 1 to 5], two tryptic proteases designated mMCP-6 and mMCP-7 and an exopeptidase, carboxypeptidase A (mMC-CPA). Using antipeptide, protease -specific antibodies to these MC granule proteases, immunohistochemistry was done to determine the distribution, number and protease phenotype of the MCs in the small intestine and spleen 10 to >60 days after Trichinella infection of BALB/c and C3H mice. TEM was performed to evaluate the granule morphology of the MCs between intestinal epithelial cells and in the lamina propria (mucosal MCs) and in the submucosa, muscle and serosa of the intestine (submucosal MCs).As noted in the table below, the number of submucosal MCs remained constant throughout the study. In contrast, on day 14, the number of MCs in the mucosa increased ~25 fold. Increased numbers of MCs were observed between epithelial cells in the mucosal crypts, in the lamina propria and to a lesser extent, between epithelial cells of the intestinal villi.

Immunochemical visualization of cyclic AMP in myenteric neurons of guinea-pig small intestine+

2001 ◽  
Vol 120 (5) ◽  
pp. A683-A683
Author(s):  
J GUZMAN ◽  
S SHARP ◽  
J YU ◽  
F MCMORRIS ◽  
A WIEMELT ◽  
...  
Keyword(s):  
Small Intestine ◽  
Cyclic Amp ◽  
Guinea Pig ◽  
Myenteric Neurons

In situ demonstration of migration of dendritic cells released from rat small intestine to mesenteric lymph nodes

2001 ◽  
Vol 120 (5) ◽  
pp. A183-A183
Author(s):  
H KOBAYASHI ◽  
H NAGATA ◽  
S MIURA ◽  
T AZUMA ◽  
H SUZUKI ◽  
...  
Keyword(s):  
Dendritic Cells ◽  
Small Intestine ◽  
Lymph Nodes ◽  
Rat Small Intestine ◽  
Mesenteric Lymph Nodes ◽  
Mesenteric Lymph

Redox potential of the small intestine lumer in a model of experimental hemorrhage in rats

2001 ◽  
Vol 120 (5) ◽  
pp. A195-A195
Author(s):  
J PAULA ◽  
E SPINEDI ◽  
A DUBIN ◽  
D BUSTOS ◽  
J DAVOLOS
Keyword(s):  
Small Intestine ◽  
Redox Potential
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