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Submitted on January 23, 2003
Revised on May 13, 2003
Accepted on May 15, 2003

New insights into the rat spermatogonial proteome: identification of 156 additional proteins

Emmanuelle COM, Bertrand Evrard, Peter Roepstorff, Florence Aubry, and Charles G. Pineau

GERM-INSERM U.435, Rennes

Corresponding Author: charles.pineau{at}rennes.inserm.fr

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 to 9 was created and protein entities fractionated in a 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 reflects 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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