Separate and Conjugated in vitro Effects of Clofibrate and of an Organic Extract of Rat Amniotic Fluid on Microperoxisomes of Fetal Mouse Small Intestine

Neonatology ◽  
1993 ◽  
Vol 63 (3) ◽  
pp. 163-170
Author(s):  
R. Calvert ◽  
M. Dauça
Keyword(s):  
Small Intestine ◽  
Amniotic Fluid ◽  
Organic Extract ◽  
Fetal Mouse ◽  
Mouse Small Intestine ◽  
In Vitro Effects

scholarly journals In vitro effects of tyre debris organic extract on the kinetic and morphologic traits of rabbit spermatozoa

2010 ◽  
Vol 17 (4) ◽  
Author(s):  
  Moretti E. ◽  
Dal Bosco A. ◽  
Mourvaki E. ◽  
Cardinali R. ◽  
Collodel G. ◽  
...  
Keyword(s):  
Organic Extract ◽  
In Vitro Effects ◽  
Rabbit Spermatozoa

scholarly journals DES2 protein is responsible for phytoceramide biosynthesis in the mouse small intestine

2004 ◽  
Vol 379 (3) ◽  
pp. 687-695 ◽  
Author(s):  
Fumio OMAE ◽  
Masao MIYAZAKI ◽  
Ayako ENOMOTO ◽  
Minoru SUZUKI ◽  
Yusuke SUZUKI ◽  
...  
Keyword(s):  
Small Intestine ◽  
Epithelial Cells ◽  
Intestinal Epithelial ◽  
Vitro Assay ◽  
Peptide Antibody ◽  
Mouse Small Intestine ◽  
Mrna Content ◽  
Crypt Cells

The C-4 hydroxylation of sphinganine and dihydroceramide is a rate-limiting reaction in the biosynthesis of phytosphingolipids. Mouse DES1 (MDES1) cDNA homologous to the Drosophila melanogaster degenerative spermatocyte gene-1 (des-1) cDNA leads to sphingosine Δ4-desaturase activity, and another mouse homologue, MDES2, has bifunctional activity, producing C-4 hydroxysphinganine and Δ4-sphingenine in yeast [Ternes, Franke, Zahringer, Sperling and Heinz (2002) J. Biol. Chem. 277, 25512–25518]. Here, we report the characterization of mouse DES2 (MDES2) using an in vitro assay with a homogenate of COS-7 cells transfected with MDES2 cDNA and N-octanoyl-sphinganine and sphinganine as substrates. MDES2 protein prefers dihydroceramide as a substrate to sphinganine, and exhibits dihydroceramide Δ4-desaturase and C-4 hydroxylase activities. MDES2 mRNA content was high in the small intestine and abundant in the kidney. In situ hybridization detected signals of MDES2 mRNA in the crypt cells. Immunohistochemistry using an anti-MDES2 peptide antibody stained the crypt cells and the adjacent epithelial cells. These results suggest that MDES2 is the dihydroceramide C-4 hydroxylase responsible for the biosynthesis of enriched phytosphingoglycolipids in the microvillous membranes of intestinal epithelial cells.

Permeation of Hydroxypropyl-Beta-Cyclodextrin and Its Inclusion Complex through Mouse Small Intestine, Determined by a Spectrophotometry

2021 ◽  
Vol 17 ◽  
Author(s):  
Ping Yang ◽  
Jinhua Luo ◽  
Shuo Yan ◽  
Xiaohong Li ◽  
Qian Yao
Keyword(s):  
Small Intestine ◽  
Inclusion Complex ◽  
Host Molecules ◽  
Beta Cyclodextrin ◽  
Mouse Small Intestine ◽  
Ft Ir ◽  
Hydroxypropyl Beta Cyclodextrin ◽  
Assay Conditions

Background: Cyclodextrins (CDs) are commonly used host molecules of inclusion complex. However, due to the lack of sensitive method to determine CDs, the absorption process of CDs remains unclear. Objective: In this study, oleuropein (OL) inclusion complex employing hydroxylpropyl-beta-cyclodextrin (HP-beta-CD) as host molecules was prepared and the formation of inclusion complex was ascertained by FT-IR and DSC. A spectrophotometry was established for the determination of HP-beta-CD, based on the fact that the absorbance of phenolphthalein (PP) decreased in the presence of HP-beta-CD. Methods: The assay conditions were optimized to augment the method sensitivity. Molecular docking was employed to verify the strong interaction between PP and HP-beta-CD. The permeation process of free HP-beta-CD, HP-beta-CD of OL inclusion complex, free OL, and OL in the inclusion complex, was examined, respectively, using an in vitro mouse small intestine model. Results: Though HP-beta-CD possessed hydrophilic outside shell, it could permeate through mouse small intestine quickly with cumulative permeating amount over 90% in 2 h. Free HP-beta-CD, the host molecule HP-beta-CD, and guest molecule OL of the inclusion complex exhibited the consistent permeating profiles across mouse small intestine. Conclusion: The approach for the determination of HP-beta-CD was accurate and precise (%RSD=2.98).

scholarly journals PhoB Regulates Motility, Biofilms, and Cyclic di-GMP in Vibrio cholerae

2009 ◽  
Vol 191 (21) ◽  
pp. 6632-6642 ◽  
Author(s):  
Jason T. Pratt ◽  
EmilyKate McDonough ◽  
Andrew Camilli
Keyword(s):  
Small Intestine ◽  
Life Cycle ◽  
Vibrio Cholerae ◽  
Late Stage ◽  
Signaling Mechanism ◽  
Infant Mouse ◽  
Mouse Small Intestine ◽  
External Stimuli ◽  
Late Stages

ABSTRACT Signaling through the second messenger cyclic di-GMP (c-di-GMP) is central to the life cycle of Vibrio cholerae. However, relatively little is known about the signaling mechanism, including the specific external stimuli that regulate c-di-GMP concentration. Here, we show that the phosphate responsive regulator PhoB regulates an operon, acgAB, which encodes c-di-GMP metabolic enzymes. We show that induction of acgAB by PhoB positively regulates V. cholerae motility in vitro and that PhoB regulates expression of acgAB at late stages during V. cholerae infection in the infant mouse small intestine. These data support a model whereby PhoB becomes activated at a late stage of infection in preparation for dissemination of V. cholerae to the aquatic environment and suggest that the concentration of exogenous phosphate may become limited at late stages of infection.

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