Difference of proteomic protein in brains between amyloid protein precursor transgenic mice and normal mice

Aim: To study the difference of protein expression in brain with the proteomic technique between amyloid protein precusor (APP) transgenic mice and normal mice, and investigate the molecular mechanisms of Alzheimer disease. Methods: The experiments were carried out in the Sec ond Hospital of Hebei Medical University, the Institute of Geriatrics, General Hospital of Chinese PLA, and the National Key Laboratory of Protein Engineering, Peking University between March 2002 and October 2003. After brain proteins were extracted in 4 APP transgenic mice and normal mice, the brain tissues were fixed with immobilized pH gradient (IPG) isoelectric focusing electrophoresis as the first dimension, and then run vertical odium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) as the second dimension. The electrophoretogram was analyzed with ImageMaster 2D Elite imaging analytical software. The proteins of interest were in-gel digested and identified with MALDI-TOF mass spectrometry or MALDI-TOF/TOF tandem mass spectrometry. Results: All th e 8 mice entered the analysis of results. Eleven protein spots were differentially expressed in APP transgenic mice as compared with the control mice brains, which were identified as heat shock protein 86 ku-1, neurofilament triplet L, oxidoreductase 75 ku subunit precursor, serum albumin precursor, glyceraldehyde 3-phosphate dehydrogenase, ATP synthase alpha subunit, alpha enolase, gamma enolase, ubiquitin-conjugating enzyme E2, creatine kinase and aspartate transaminase. Conclusion: The differentially displayed proteins between APP transgenic mice and control mice brains were found and identified with the proteomic technique.