期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 55, 期 7, 页码 2454-2458出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201510411
关键词
embryo; mass spectrometry; proteins; single-cell studies; Xenopus laevis
资金
- National Science Foundation [DBI-1455474]
- George Washington University Department of Chemistry Start-Up Funds
- Columbian College Facilitating Funds
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [1121711] Funding Source: National Science Foundation
- Div Of Biological Infrastructure
- Direct For Biological Sciences [1455474] Funding Source: National Science Foundation
We advance mass spectrometry from a cell population- averaging tool to one capable of quantifying the expression of diverse proteins in single embryonic cells. Our instrument combines capillary electrophoresis (CE), electrospray ionization, and a tribrid ultrahigh-resolution mass spectrometer (HRMS) to enable untargeted (discovery) proteomics with ca. 25 amol lower limit of detection. CE-mESI-HRMS enabled the identification of 500-800 nonredundant protein groups by measuring 20 ng, or < 0.2% of the total protein content in single blastomeres that were isolated from the 16-cell frog (Xenopus laevis) embryo, amounting to a total of 1709 protein groups identified between n= 3 biological replicates. By quantifying. 150 nonredundant protein groups between all blastomeres and replicate measurements, we found significant translational cell heterogeneity along multiple axes of the embryo at this very early stage of development when the transcriptional program of the embryo has yet to begin.
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