Open AccessN-Glycoproteome of E14.Tg2a Mouse Embryonic Stem Cells
Author(s) -
Bingyun Sun,
Li Ma,
Xiaowei Yan,
Denis Lee,
Vinita M. Alexander,
Laura Hohmann,
Cynthia G. Lorang,
Lalangi Chandrasena,
Qiang Tian,
Leroy Hood
Publication year - 2013
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0055722
Subject(s) - glycosylation , embryonic stem cell , proteome , glycoprotein , biology , microbiology and biotechnology , stem cell , gene , hek 293 cells , transmembrane protein , extracellular matrix , computational biology , chemistry , receptor , biochemistry
E14.Tg2a mouse embryonic stem (mES) cells are a widely used host in gene trap and gene targeting techniques. Molecular characterization of host cells will provide background information for a better understanding of functions of the knockout genes. Using a highly selective glycopeptide-capture approach but ordinary liquid chromatography coupled mass spectrometry (LC-MS), we characterized the N-glycoproteins of E14.Tg2a cells and analyzed the close relationship between the obtained N-glycoproteome and cell-surface proteomes. Our results provide a global view of cell surface protein molecular properties, in which receptors seem to be much more diverse but lower in abundance than transporters on average. In addition, our results provide a systematic view of the E14.Tg2a N-glycosylation, from which we discovered some striking patterns, including an evolutionarily preserved and maybe functionally selected complementarity between N-glycosylation and the transmembrane structure in protein sequences. We also observed an environmentally influenced N-glycosylation pattern among glycoenzymes and extracellular matrix proteins. We hope that the acquired information enhances our molecular understanding of mES E14.Tg2a as well as the biological roles played by N-glycosylation in cell biology in general.