Immunocytochemical demonstration of caldesmon (a calmodulin-binding, F-actin-interacting protein) in smooth muscle fibers and absorptive epithelial cells in the small intestine of the rat

1984 ◽  
Vol 235 (1) ◽  
Author(s):  
K. Ishimura ◽  
H. Fujita ◽  
T. Ban ◽  
H. Matsuda ◽  
K. Sobne ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Small Intestine ◽  
Epithelial Cells ◽  
Muscle Fibers ◽  
Interacting Protein ◽  
Calmodulin Binding

The Action of Cholecystokinin and Related Peptides on Guinea Pig Small Intestine

1974 ◽  
Vol 52 (2) ◽  
pp. 298-303 ◽  
Author(s):  
W. M. Yau ◽  
G. M. Makhlouf ◽  
L. E. Edwards ◽  
J. T. Farrar
Keyword(s):  
Smooth Muscle ◽  
Small Intestine ◽  
Guinea Pig ◽  
Mode Of Action ◽  
Muscle Fibers ◽  
Nerve Endings ◽  
Cholinergic Mechanisms ◽  
Molar Basis ◽  
Release Of Acetylcholine ◽  
Relative Potencies

The mode of action of cholecystokinin (CCK), an octapeptide fragment of CCK, caerulein, and pentagastrin on isolated guinea pig ileal muscle was investigated and their relative potencies determined. On a molar basis, octapeptide-CCK and caerulein were about twice as potent as CCK, whereas pentagastrin and Urecholine were respectively 23 and 46 times less potent. Scopolamine (6.84 × 10−4 M) inhibited the response to all four peptides relatively less than the response to Urecholine. Tetrodotoxin (0.1 μg/ml) inhibited the response to all peptides by 91%. It was concluded that the effect of these peptides on ileal muscle was largely mediated by cholinergic mechanisms. It could not be ascertained, however, whether the effect resulted solely from release of acetylcholine by nerve endings or from the participation of acetylcholine mainly as a synergist of the peptides' action on smooth muscle fibers.

Eimeria Organisms Develop in the Epithelial Cells of Equine Small Intestine

2002 ◽  
Vol 39 (4) ◽  
pp. 505-508 ◽  
Author(s):  
K. Hirayama ◽  
M. Okamoto ◽  
T. Sako ◽  
K. Kihara ◽  
K. Okai ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Small Intestine ◽  
Epithelial Cells ◽  
Host Cell ◽  
Lamina Propria ◽  
Smooth Muscle Actin ◽  
Eimeria Species ◽  
Neuron Specific Enolase ◽  
Neuroendocrine Cells ◽  
Host Cells

Histopathologic and immunohistochemical examinations were performed to determine the origin of host cells parasitized by Eimeria in the small intestines collected from five foals. Eimeria organisms at various stages (mainly microgametes and macrogametes) were frequently found in the cytoplasm of hypertrophied host cells in the lamina propria at the tips of villi of the jejunum and ileum. The cytoplasm of the host cell was immunohistochemically positive for cytokeratin AE1/AE3 and cytokeratin 13 and was negative for vimentin, desmin, α-smooth muscle actin, chromogranin A, neuron-specific enolase, and factor VIII. The host cells parasitized by Eimeria species had the immunostaining characteristics of epithelial cells but not of mesenchymal cells, endothelial cells of lacteals or capillaries, smooth muscle cells or neuroendocrine cells. These results suggest that the host cell of Eimeria species is possibly derived from intestinal epithelial cells and then displaced into the lamina propria of the small intestine.

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.

Influence of a lymphocyte-conditioned medium on the expression of smooth-muscle α-aktin in lens epithelial cells in situ

1999 ◽  
Vol 96 (3) ◽  
pp. 174-181
Author(s):  
Kerstin Wunderlich ◽  
Marcus Knorr ◽  
H. Northoff ◽  
Hans-J. Thiel
Keyword(s):  
Smooth Muscle ◽  
Epithelial Cells ◽  
Conditioned Medium ◽  
Lens Epithelial Cells

scholarly journals Influence of layer separation on the determination of stomach smooth muscle properties

2021 ◽  
Author(s):  
Mischa Borsdorf ◽  
Markus Böl ◽  
Tobias Siebert
Keyword(s):  
Smooth Muscle ◽  
Muscle Fibers ◽  
Smooth Muscles ◽  
Muscle Layer ◽  
Uniaxial Tensile ◽  
Muscle Properties ◽  
Layer Separation ◽  
Isotonic Contractions ◽  
Longitudinal Layer

AbstractUniaxial tensile experiments are a standard method to determine the contractile properties of smooth muscles. Smooth muscle strips from organs of the urogenital and gastrointestinal tract contain multiple muscle layers with different muscle fiber orientations, which are frequently not separated for the experiments. During strip activation, these muscle fibers contract in deviant orientations from the force-measuring axis, affecting the biomechanical characteristics of the tissue strips. This study aimed to investigate the influence of muscle layer separation on the determination of smooth muscle properties. Smooth muscle strips, consisting of longitudinal and circumferential muscle layers (whole-muscle strips [WMS]), and smooth muscle strips, consisting of only the circumferential muscle layer (separated layer strips [SLS]), have been prepared from the fundus of the porcine stomach. Strips were mounted with muscle fibers of the circumferential layer inline with the force-measuring axis of the uniaxial testing setup. The force–length (FLR) and force–velocity relationships (FVR) were determined through a series of isometric and isotonic contractions, respectively. Muscle layer separation revealed no changes in the FLR. However, the SLS exhibited a higher maximal shortening velocity and a lower curvature factor than WMS. During WMS activation, the transversally oriented muscle fibers of the longitudinal layer shortened, resulting in a narrowing of this layer. Expecting volume constancy of muscle tissue, this narrowing leads to a lengthening of the longitudinal layer, which counteracted the shortening of the circumferential layer during isotonic contractions. Consequently, the shortening velocities of the WMS were decreased significantly. This effect was stronger at high shortening velocities.

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