scholarly journals Stimulation of constitutive nitric oxide uniquely and compensatorily regulates intestinal epithelial cell brush border membrane Na absorption

2019 ◽  
Vol 7 (9) ◽  
pp. e14086
Author(s):  
Balasubramanian Palaniappan ◽  
Palanikumar Manoharan ◽  
Subha Arthur ◽  
Soudamani Singh ◽  
Usha Murughiyan ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Epithelial Cell ◽  
Brush Border ◽  
Intestinal Epithelial Cell ◽  
Brush Border Membrane ◽  
Intestinal Epithelial ◽  
Stimulation Of

T1864 Regulation of Epithelial Cell Brush Border Membrane NHE3 by SGLT-1 is Mediated by Constitutive Nitric Oxide

2010 ◽  
Vol 138 (5) ◽  
pp. S-594-S-595
Author(s):  
Steven D. Coon ◽  
Ramesh Kekuda ◽  
Uma Sundaram
Keyword(s):  
Nitric Oxide ◽  
Epithelial Cell ◽  
Brush Border ◽  
Brush Border Membrane

scholarly journals 32 – Unique Regulation of Intestinal Epithelial Cell Na-Glucose Co-Transporter Sglt1 by Constitutive Nitric Oxide

2019 ◽  
Vol 156 (6) ◽  
pp. S-13
Author(s):  
Balasubramanian Palaniappan ◽  
Subha Arthur ◽  
Uma Sundaram
Keyword(s):  
Nitric Oxide ◽  
Epithelial Cell ◽  
Intestinal Epithelial Cell ◽  
Intestinal Epithelial

scholarly journals Tropomyosin distinguishes between the two actin-binding sites of villin and affects actin-binding properties of other brush border proteins.

1987 ◽  
Vol 104 (1) ◽  
pp. 29-40 ◽  
Author(s):  
D R Burgess ◽  
K O Broschat ◽  
J M Hayden
Keyword(s):  
Epithelial Cell ◽  
Protein Interactions ◽  
Brush Border ◽  
Binding Sites ◽  
Intestinal Epithelial Cell ◽  
Actin Binding ◽  
Intestinal Epithelial ◽  
Binding Properties ◽  
Order Of Magnitude ◽  
Protein Components

The intestinal epithelial cell brush border exhibits distinct localizations of the actin-binding protein components of its cytoskeleton. The protein interactions that dictate this subcellular organization are as yet unknown. We report here that tropomyosin, which is found in the rootlet but not in the microvillus core, can bind to and saturate the actin of isolated cores, and can cause the dissociation of up to 30% of the villin and fimbrin from the cores but does not affect actin binding by 110-kD calmodulin. Low speed sedimentation assays and ultrastructural analysis show that the tropomyosin-containing cores remain bundled, and that 110-kD calmodulin remains attached to the core filaments. The effects of tropomyosin on the binding and bundling activities of villin were subsequently determined by sedimentation assays. Villin binds to F-actin with an apparent Ka of 7 X 10(5) M-1 at approximate physiological ionic strength, which is an order of magnitude lower than that of intestinal epithelial cell tropomyosin. Binding of villin to F-actin presaturated with tropomyosin is inhibited relative to that to pure F-actin, although full saturation can be obtained by increasing the villin concentration. Villin also inhibits the binding of tropomyosin to F-actin, although not to the same extent. However, tropomyosin strongly inhibits bundling of F-actin by villin, and bundling is not recovered even at a saturating villin concentration. Since villin has two actin-binding sites, both of which are required for bundling, the fact that tropomyosin inhibits bundling of F-actin under conditions where actin is fully saturated with villin strongly suggests that tropomyosin's and one of villin's F-actin-binding sites overlap. These results indicate that villin and tropomyosin could compete for actin filaments in the intestinal epithelial cell, and that tropomyosin may play a major role in the regulation of microfilament structure in these and other cells.

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