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Molecular & Cellular Proteomics 2:248-261, 2003.
© 2003 by The American Society for Biochemistry and Molecular Biology, Inc.

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Research

New Insights into the Rat Spermatogonial Proteome

Identification of 156 Additional Proteins^*

Emmanuelle Com^,, Bertrand Evrard, Peter Roepstorff^¶, Florence Aubry and Charles Pineau^,|

GERM-INSERM U.435, Campus de Beaulieu, Université de Rennes I, 35042 Rennes Cedex, Bretagne, France
^¶ Department of Biochemistry and Molecular Biology, University of Southern Denmark, Odense University, DK-5230 Odense M, Denmark

Despite the essential role played by spermatogonia in testicular function, little is known about these cells. To improve our understanding of their biology, our group recently identified a set of 53 spermatogonial proteins using two-dimensional (2-D) gel electrophoresis and mass spectrometry. To continue this work, we investigated a subset of the spermatogonial proteome using narrow range immobilized pH gradients to favor the detection of less abundant proteins. A 2-D reference map of spermatogonia in the pH range 4–9 was created, and protein entities fractionated in a pH 5–6 2-D gel were further processed for protein identification. A new set of 156 polypeptides was identified by peptide mass fingerprinting and tandem mass spectrometry. These polypeptides corresponded to 102 different proteins, which reflect the complexity of post-translational modifications. Seventy-nine of these proteins were identified for the first time in spermatogonia. All identified proteins were classified into functional groups. This work represents a first step toward the establishment of a systematic spermatogonia protein database.

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