Characterization and Quantification of RNA Post-transcriptional Modifications Using Stable Isotope Labeling of RNA in Conjunction with Mass Spectrometry Analysis

2011 ◽  
Vol 83 (12) ◽  
pp. 4894-4901 ◽  
Author(s):  
Sakharam P. Waghmare ◽  
Mark J. Dickman
Keyword(s):  
Mass Spectrometry ◽  
Stable Isotope ◽  
Isotope Labeling ◽  
Stable Isotope Labeling ◽  
Mass Spectrometry Analysis ◽  
Spectrometry Analysis

Methodology for the Validation of Isotopic Analyses by Mass Spectrometry in Stable-Isotope Labeling Experiments

2018 ◽  
Vol 90 (3) ◽  
pp. 1852-1860 ◽  
Author(s):  
Maud Heuillet ◽  
Floriant Bellvert ◽  
Edern Cahoreau ◽  
Fabien Letisse ◽  
Pierre Millard ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Stable Isotope ◽  
Isotope Labeling ◽  
Stable Isotope Labeling ◽  
Isotopic Analyses ◽  
Isotope Labeling Experiments

scholarly journals Characterization of the Primary Human Trophoblast Cell Secretome Using Stable Isotope Labeling With Amino Acids in Cell Culture

2021 ◽  
Vol 9 ◽  
Author(s):  
Fredrick J. Rosario ◽  
Sammy Pardo ◽  
Trond M. Michelsen ◽  
Kathryn Erickson ◽  
Lorna Moore ◽  
...  
Keyword(s):  
Amino Acids ◽  
Cell Culture ◽  
Stable Isotope ◽  
Human Placenta ◽  
Isotope Labeling ◽  
Stable Isotope Labeling ◽  
Mass Spectrometry Analysis ◽  
Secreted Proteins ◽  
Placental Villus ◽  
Human Trophoblast

The placental villus syncytiotrophoblast, the nutrient-transporting and hormone-producing epithelium of the human placenta, is a critical regulator of fetal development and maternal physiology. However, the identities of the proteins synthesized and secreted by primary human trophoblast (PHT) cells remain unknown. Stable Isotope Labeling with Amino Acids in Cell Culture followed by mass spectrometry analysis of the conditioned media was used to identify secreted proteins and obtain information about their relative rates of synthesis in syncytialized multinucleated PHT cells isolated from normal term placental villus tissue (n = 4/independent placenta). A total of 1,344 proteins were identified, most of which have not previously been reported to be secreted by the human placenta or trophoblast. The majority of secreted proteins are involved in energy and carbon metabolism, glycolysis, biosynthesis of amino acids, purine metabolism, and fatty acid degradation. Histone family proteins and mitochondrial proteins were among proteins with the slowest synthesis rate whereas proteins associated with signaling and the plasma membrane were synthesized rapidly. There was a significant overlap between the PHT secretome and proteins known be secreted to the fetal circulation by the human placenta in vivo. The generated data will guide future experiments to determine the function of individual secreted proteins and will help us better understand how the placenta controls maternal and fetal physiology.

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