scholarly journals Metabolomic Analysis Evidences That Uterine Epithelial Cells Enhance Blastocyst Development in a Microfluidic Device

Cells ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 1194
Author(s):  
Vanessa Mancini ◽  
Alexandra C. Schrimpe-Rutledge ◽  
Simona G. Codreanu ◽  
Stacy D. Sherrod ◽  
John A. McLean ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Embryo Development ◽  
Microfluidic Device ◽  
Microfluidic System ◽  
Mass Spectrometry Analysis ◽  
Blastocyst Development ◽  
Uterine Epithelial Cells ◽  
Spectrometry Analysis ◽  
Endometrial Cells ◽  
Phase Liquid

Here we report the use of a microfluidic system to assess the differential metabolomics of murine embryos cultured with endometrial cells-conditioned media (CM). Groups of 10, 1-cell murine B6C3F1×B6D2F1 embryos were cultured in the microfluidic device. To produce CM, mouse uterine epithelial cells were cultured in potassium simplex optimized medium (KSOM) for 24 h. Media samples were collected from devices after 5 days of culture with KSOM (control) and CM, analyzed by reverse phase liquid chromatography and untargeted positive ion mode mass spectrometry analysis. Blastocyst rates were significantly higher (p < 0.05) in CM (71.8%) compared to control media (54.6%). We observed significant upregulation of 341 compounds and downregulation of 214 compounds in spent media from CM devices when compared to control. Out of these, 353 compounds were identified showing a significant increased abundance of metabolites involved in key metabolic pathways (e.g., arginine, proline and pyrimidine metabolism) in the CM group, suggesting a beneficial effect of CM on embryo development. The metabolomic study carried out in a microfluidic environment confirms our hypothesis on the potential of uterine epithelial cells to enhance blastocyst development. Further investigations are required to highlight specific pathways involved in embryo development and implantation.

scholarly journals Modification of Lipooligosaccharide with Phosphoethanolamine by LptA in Neisseria meningitidis Enhances Meningococcal Adhesion to Human Endothelial and Epithelial Cells

2008 ◽  
Vol 76 (12) ◽  
pp. 5777-5789 ◽  
Author(s):  
Hideyuki Takahashi ◽  
Russel W. Carlson ◽  
Artur Muszynski ◽  
Biswa Choudhury ◽  
Kwang Sik Kim ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Neisseria Meningitidis ◽  
Lipid A ◽  
Inner Core ◽  
Mass Spectrometry Analysis ◽  
Wild Type ◽  
Spectrometry Analysis ◽  
Flight Mass Spectrometry ◽  
Epithelial Cell Lines

ABSTRACT The lipooligosaccharide (LOS) of Neisseria meningitidis can be decorated with phosphoethanolamine (PEA) at the 4′ position of lipid A and at the O-3 and O-6 positions of the inner core of the heptose II residue. The biological role of PEA modification in N. meningitidis remains unclear. During the course of our studies to elucidate the pathogenicity of the ST-2032 (invasive) meningococcal clonal group, disruption of lptA, the gene that encodes the PEA transferase for 4′ lipid A, led to a approximately 10-fold decrease in N. meningitidis adhesion to four kinds of human endothelial and epithelial cell lines at an multiplicity of infection of 5,000. Complementation of the lptA gene in a ΔlptA mutant restored wild-type adherence. By matrix-assisted laser desorption ionization-time-of-flight mass spectrometry analysis, PEA was lost from the lipid A of the ΔlptA mutant compared to that of the wild-type strain. The effect of LptA on meningococcal adhesion was independent of other adhesins such as pili, Opc, Opa, and PilC but was inhibited by the presence of capsule. These results indicate that modification of LOS with PEA by LptA enhances meningococcal adhesion to human endothelial and epithelial cells in unencapsulated N. meningitidis.

High sensitive matrix-free mass spectrometry analysis of peptides using silicon nanowires-based digital microfluidic device

Lab on a Chip ◽  
2011 ◽  
Vol 11 (9) ◽  
pp. 1620 ◽  
Author(s):  
Florian Lapierre ◽  
Gaëlle Piret ◽  
Hervé Drobecq ◽  
Oleg Melnyk ◽  
Yannick Coffinier ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Microfluidic Device ◽  
Silicon Nanowires ◽  
Mass Spectrometry Analysis ◽  
Spectrometry Analysis ◽  
Digital Microfluidic ◽  
Matrix Free

Lactobacillus reuteri glyceraldehyde-3-phosphate dehydrogenase functions in adhesion to intestinal epithelial cells

2015 ◽  
Vol 61 (5) ◽  
pp. 373-380 ◽  
Author(s):  
Wen-Ming Zhang ◽  
Hai-Feng Wang ◽  
Kan Gao ◽  
Cong Wang ◽  
Li Liu ◽  
...  
Keyword(s):  
Surface Layer ◽  
Epithelial Cells ◽  
Lactobacillus Reuteri ◽  
Intestinal Epithelial Cells ◽  
Lactobacillus Rhamnosus ◽  
Protein Band ◽  
Surface Proteins ◽  
Mass Spectrometry Analysis ◽  
Intestinal Epithelial ◽  
Spectrometry Analysis

This study was aimed to identify key surface proteins mediating the adhesion of lactobacilli to intestinal epithelial cells. By using Caco-2 and IPEC-J2 cells labeled with sulfo-NHS-biotin in the western blotting, a protein band of an approximately 37 kDa was detected on the surface layer of Lactobacillus reuteri strains ZJ616, ZJ617, ZJ621, and ZJ623 and Lactobacillus rhamnosus GG. Mass spectrometry analysis using the adhesion-related protein from L. reuteri ZJ617 showed that it was 100% homologous to the glyceraldehyde-3-phosphate dehydrogenase (GAPDH) of L. reuteri JCM 1112 (GenBank: YP_001841377). The ability of L. reuteri ZJ617 to adhere to epithelial cells decreased significantly by treatment with LiCl or by blocking with an anti-GAPDH antibody, in comparison with the untreated strain (p < 0.05). Immunoelectron microscopic and immunofluorescence analyses confirmed that GAPDH is located on the surface layer of L. reuteri ZJ617. The results indicated that the GAPDH protein of L. reuteri ZJ617 acts as an adhesion component that plays an important role in binding to the intestinal epithelial cells.

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