Nuclear microscopy of rat colon epithelial cells

2011 ◽  
Vol 269 (20) ◽  
pp. 2264-2268 ◽  
Author(s):  
M. Ren ◽  
Reshmi Rajendran ◽  
Mary Ng ◽  
Chammika Udalagama ◽  
Anna E. Rodrigues ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Rat Colon ◽  
Nuclear Microscopy

11 beta-hydroxysteroid dehydrogenase and corticosteroid hormone receptors in the rat colon

1993 ◽  
Vol 264 (6) ◽  
pp. E951-E957 ◽  
Author(s):  
C. B. Whorwood ◽  
P. C. Barber ◽  
J. Gregory ◽  
M. C. Sheppard ◽  
P. M. Stewart
Keyword(s):  
Epithelial Cells ◽  
Lamina Propria ◽  
Hormone Receptors ◽  
Rat Kidney ◽  
Distal Colon ◽  
Hydroxysteroid Dehydrogenase ◽  
Neuroendocrine Cells ◽  
Rat Colon ◽  
Mrna Levels

In the rat kidney 11 beta-hydroxysteroid dehydrogenase (11 beta-HSD) maintains normal in vivo specificity for mineralocorticoid receptor (MR) by converting the active steroid corticosterone to inactive 11-dehydrocorticosterone, leaving aldosterone to occupy the MR. Clinical observations support the hypothesis that 11 beta-HSD also protects the distal colonic MR from glucocorticoid excess. We have measured 11 beta-HSD mRNA and activity along the rat colon and have analyzed the distribution of 11 beta-HSD, MR, and glucocorticoid receptor (GR) mRNA within rat distal colon using in situ hybridization. Levels of 11 beta-HSD mRNA (1.7 and 3.4 kb) and activity were higher in distal vs. proximal colon, paralleling reported MR mRNA levels. Within the distal colon mucosa both 11 beta-HSD immunoreactivity and mRNA was observed in cells in the lamina propria but not in epithelial cells. MR mRNA was present in surface epithelial cells, but was also colocalized with the same 11 beta-HSD-expressing cells in the lamina propria. In contrast GR mRNA was more uniformly distributed. The localization of MR mRNA to nonepithelial cells in the lamina propria, possibly neuroendocrine cells, suggests that mineralocorticoid-regulated sodium transport across colonic epithelial cells may also involve a paracrine mechanism. As with the kidney, exposure of active mineralocorticoid to the MR in these cells in the lamina propria is dictated by 11 beta-HSD in an autocrine fashion.

Effects of Sennosides and Nonanthranoid Laxatives on Cytochemistry of Epithelial Cells in Rat Colon

Pharmacology ◽  
1993 ◽  
Vol 47 (1) ◽  
pp. 196-204 ◽  
Author(s):  
Kan Yang ◽  
Kunhua Fan ◽  
Ulrich Mengs ◽  
Martin Lipkin
Keyword(s):  
Epithelial Cells ◽  
Rat Colon

scholarly journals Histoplanimetrical Study on the Relationship between Cellular Kinetics of Epithelial Cells and Proliferation of Indigenous Bacteria in the Rat Colon

2009 ◽  
Vol 71 (6) ◽  
pp. 745-752 ◽  
Author(s):  
Wang-Mei QI ◽  
Kenkichi YAMAMOTO ◽  
Yuh YOKOO ◽  
Hidenori MIYATA ◽  
Kankanam Gamage Sanath UDAYANGA ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Rat Colon ◽  
Indigenous Bacteria ◽  
Cellular Kinetics ◽  
The Relationship ◽  
Kinetics Of

scholarly journals Postnatal development of rat colon epithelial cells is associated with changes in the expression of the β1,4-N-acetylgalactosaminyltransferase involved in the synthesis of Sda antigen of α2,6-sialyltransferase activity towards N-acetyl-lactosamine

1990 ◽  
Vol 270 (2) ◽  
pp. 519-524 ◽  
Author(s):  
F Dall'Olio ◽  
N Malagolini ◽  
G Di Stefano ◽  
M Ciambella ◽  
F Serafini-Cessi
Keyword(s):  
Cell Differentiation ◽  
Epithelial Cells ◽  
Large Intestine ◽  
Postnatal Period ◽  
Maximum Activity ◽  
Rat Colon ◽  
Transferase Activity ◽  
Colon Cells ◽  
Postnatal Maturation ◽  
Sialyltransferase Activity

beta 1,4-N-Acetylgalactosaminyltransferase (beta 1,4GalNAc-transferase) and alpha 2,3-sialyltransferase are both involved in the biosynthesis of the Sda blood group antigen, which is also present in cells of large intestine. The expression of these enzymes and of alpha 2,6-sialyltransferase activity towards N-acetyl-lactosamine was investigated in rat intestinal cells and correlated with both cell differentiation and extent of postnatal maturation. The beta 1,4GalNAc-transferase activity was exclusively found in epithelial cells of the large intestine, preferentially in the proximal segments suggesting a proximal-distal gradient of expression. The beta 1,4GalNAc-transferase and alpha 2,3-sialyltransferase activity towards N-acetyl-lactosamine were expressed in all cell fractions of the colonic crypt, with a maximum activity in the deeply located cells; therefore Sda antigen biosynthesis appears to occur preferentially at a specific stage of cell differentiation. By using N-acetyl-lactosamine as an acceptor, the predominant sialyltransferase in the colon cells was that capable of adding sialic acid in the alpha 2,3- linkage, whereas in the ileum cells the major enzyme was that forming the alpha 2,6-isomer. There were dramatic changes in the expression of colonic beta 1,4GalNac-transferase and of alpha 2,6-sialyltransferase activity towards N-acetyl-lactosamine during postnatal maturation. The former enzyme, practically absent at birth, increased slowly in the first days of life and then rapidly after weaning; by contrast, the latter enzyme was largely expressed only in newborn animals. As the colonic alpha 2,3-sialyltransferase activity towards N-acetyl-lactosamine did not change during the postnatal period, the ratio between the alpha 2,6- and alpha 2,3-sialyltransferase activities was reversed after weaning.

Metabolism of 1,2‐dimethylhydrazine by cultured rat colon epithelial cells

1983 ◽  
Vol 5 (2) ◽  
pp. 78-86 ◽  
Author(s):  
Howard P. Glauert ◽  
Maurice R. Bennink
Keyword(s):  
Epithelial Cells ◽  
Rat Colon

scholarly journals Neoplastic Transformation of Rat Colon Epithelial Cells by Expression of Activated Human K-ras

1998 ◽  
Vol 89 (6) ◽  
pp. 615-625 ◽  
Author(s):  
Kenji Sugiyama ◽  
Kazuhiko Otori ◽  
Hiroyasu Esumi
Keyword(s):  
Epithelial Cells ◽  
Neoplastic Transformation ◽  
Rat Colon

A systems-level analysis of bile acids effects on rat colon epithelial cells

2021 ◽  
Author(s):  
Jonathan Yde ◽  
Qi Wu ◽  
Johan Borg ◽  
Robert A. Fenton ◽  
Hanne Bjerregaard Moeller
Keyword(s):  
Mass Spectrometry ◽  
Bile Acid ◽  
Epithelial Cells ◽  
Bile Acids ◽  
Rna Sequencing ◽  
Urine Volume ◽  
Rat Colon ◽  
Acid Transport ◽  
Bile Acid Transport ◽  
Underlying Mechanisms

Bile acid diarrhoea is a chronic condition caused by increased delivery of bile acids to the colon. The underlying mechanisms remain to be elucidated. To investigate genes involved in bile acid diarrhoea, systems-level analyses were employed on a rat bile acid diarrhoea model. Twelve male Wistar Munich rats, housed in metabolic cages, were fed either control or bile acid-mixed (1% w/w) diets for ten days. Food intake, water intake, urine volume, bodyweight and faecal output were monitored daily. After euthanasia, colonic epithelial cells were isolated using calcium-chelation and processed for systems-level analyses, i.e. RNA-sequencing transcriptomics and mass spectrometry proteomics. Bile acid-fed rats suffered diarrhoea, indicated by increased drinking, faeces weight and faecal water content compared with control rats. Urine output was unchanged. With bile acid-feeding, RNA-sequencing revealed 204 increased and 401 decreased mRNAs; mass spectrometry 183 increased and 111 decreased proteins. Among the altered genes were genes associated with electrolyte and water transport (including Slc12a7, Clca4 and Aqp3) and genes associated with bile acid transport (Slc2b1, Abcg2, Slc51a, Slc51b and Fabps). Correlation analysis showed a significant positive correlation (Pearson's r=0.28) between changes in mRNA-expression and changes in protein-expression. However, caution must be exercised in making a direct correlation between experimentally determined transcriptomes and proteomes. Genes associated with bile acid transport responded to bile acid-feeding, suggesting that colonic bile acid transport also occur by regulated protein facilitated mechanisms in addition to passive diffusion. In summary, the study provides annotated rat colonic epithelial cell transcriptome and proteome with response to bile acid-feeding.

Increased expression of midkine in the rat colon during healing of experimental colitis

2006 ◽  
Vol 291 (4) ◽  
pp. G735-G743 ◽  
Author(s):  
Takafumi Yuki ◽  
Shunji Ishihara ◽  
M. A. K. Rumi ◽  
Cesar F. Ortega-Cava ◽  
Yasunori Kadowaki ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Proinflammatory Cytokines ◽  
Wound Repair ◽  
Intestinal Inflammation ◽  
Tyrosine Phosphatase ◽  
Northern Blotting ◽  
Rat Colon ◽  
Rt Pcr ◽  
Mucosal Regeneration

Midkine (MK) is a unique growth and differentiation factor that modulates the proliferation and migration of various cells; however, little is known regarding its relationship to intestinal diseases. The aim of this study was to investigate MK expression and its role in dextran sulfate sodium (DSS)-induced colitis in rats. The expressions of MK, receptor-like protein-tyrosine phosphatase (RPTP)-β, and proinflammatory cytokines were examined in rat colonic tissues after the development of DSS-induced colitis using Northern blotting, immunohistochemistry, and laser-capture microdissection (LCM) coupled with RT-PCR. The effects of MK on the migration of intestinal epithelial cells (IEC-6) were also evaluated in vitro using an intestinal wound repair model. MK expression was significantly increased in damaged colonic mucosa, mainly from day 3 to day 5 after the end of DSS administration, with abundant MK immunoreactive signals detected in submucosal fibroblasts. Expressions of proinflammatory cytokines were most strongly induced on day 1, which preceded the augmentation of MK expression. Results of LCM coupled with RT-PCR clearly indicated RPTP-β expression in colonic epithelial cells. The migration assay showed that wound repair in the MK-treated groups was accelerated dose dependently. The present results showed for the first time that intestinal inflammation upregulates the MK-RPTP-β system, which may stimulate mucosal regeneration during the process of healing of colitis. Additional investigations regarding the role of MK may contribute to the development of new options for the treatment of inflammatory bowel diseases.

Identification of a membrane protein from T84 cells using antibodies made against a DIDS-binding peptide

1992 ◽  
Vol 262 (1) ◽  
pp. C136-C147 ◽  
Author(s):  
E. J. Sorscher ◽  
C. M. Fuller ◽  
R. J. Bridges ◽  
A. Tousson ◽  
R. B. Marchase ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Chloride Channel ◽  
Tumor Cell Line ◽  
Band 3 ◽  
Disulfonic Acid ◽  
Rat Colon ◽  
Affinity Column ◽  
Lipid Bilayer Membranes ◽  
T84 Cells ◽  
Western Blots

The outwardly rectified chloride channel of secretory epithelial cells is inhibited by disulfonic stilbene (DS) compounds such as 4,4'-diisothiostilbene-2,2'-disulfonic acid (DIDS) [R. J. Bridges, R. T. Worrell, R. A. Frizzell, and D. J. Benos, Am. J. Physiol. 256 (Cell Physiol. 25): C902-C912, 1989]. A 13-amino acid peptide (P49) corresponding to the putative DS binding site region of the murine anion exchange protein was synthesized, and polyclonal antibodies were generated against it and then purified over a P49 affinity column. The resulting monospecific antibodies reacted on Western blots with a 95- to 100-kDa protein from human erythrocytes and a 55- to 60-kDa protein from the human colonic tumor cell line, T84. The reaction with T84 protein did not appear to represent recognition of an anion exchanger because anion efflux from T84 cells was independent of external Cl-. In addition, monoclonal antibodies raised against human band 3 recognized the band 3 protein in human red cell ghost preparations but recognized nothing in T84 cell membrane preparations. In T84 cells, DIDS protected the 60-kDa protein from antibody binding. The anti-P49 antibody blocked outwardly rectified Cl- channels incorporated into planar lipid bilayer membranes from rat colon. Immunocytochemical data reveal specific binding of the anti-P49 antibody to perinuclear cytoplasmic vesicles. Forskolin caused these antibody-labeled vesicles to migrate from the perinuclear region to the plasma membrane under conditions and with a time course identical to that seen for stimulation of Cl- transport in these cells. Our results suggest that the protein may be a part of a chloride channel complex of secretory epithelial cells.

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