Elucidation of O-glycosylation structures of the beta-amyloid precursor protein by liquid chromatography-mass spectrometry using electron transfer dissociation and collision induced dissociation.
作者： Irina Perdivara , Robert Petrovich , Bernadette Allinquant , Leesa J. Deterding , Kenneth B. Tomer
DOI: 10.1021/PR800758G
关键词:
摘要: Accumulation and deposition of β-amyloid peptide, a major constituent in neuritic plaques are hallmarks Alzheimer’s disease (AD) AD-related neurodegenerative diseases. β-Amyloid (Aβ) is derived from the proteolytic cleavage amyloid precursor protein (APP), transmembrane present three isoforms brain comprising 695, 751 770 amino acids, respectively. Among other post-translational modifications, APP modified during maturation by N- O-glycosylation, which thought to be responsible for its expression secretion. Unlike N-glycosylation, no sites O-glycosylation have previously been reported. We report here identification specific secreted APP695 (sAPP695) produced CHO cells, using combination high-performance liquid chromatography electrospray−tandem mass spectrometry. With use electron transfer dissociation collision induced (ETD CID), we identified type, composition an...
acs.org
uni-konstanz.de
sci-hub.se 参考文章(45)
Leann M. Mikesh, Beatrix Ueberheide, An Chi, Joshua J. Coon, John E.P. Syka, Jeffrey Shabanowitz, Donald F. Hunt, The utility of ETD mass spectrometry in proteomic analysis. Biochimica et Biophysica Acta. ,vol. 1764, pp. 1811- 1822 ,(2006) , 10.1016/J.BBAPAP.2006.10.003
Numa R Gottardi-Littell, Chhinder P Sodhi, Ruth G Perez, Phosphorylation of beta-amyloid precursor protein (APP) cytoplasmic tail facilitates amyloidogenic processing during apoptosis The FASEB Journal. ,vol. 22, ,(2008)
Kanae Ando, Masaki Oishi, Shizu Takeda, Ko-ichi Iijima, Toshio Isohara, Angus C. Nairn, Yutaka Kirino, Paul Greengard, Toshiharu Suzuki, Role of Phosphorylation of Alzheimer’s Amyloid Precursor Protein during Neuronal Differentiation The Journal of Neuroscience. ,vol. 19, pp. 4421- 4427 ,(1999) , 10.1523/JNEUROSCI.19-11-04421.1999
M. Isabel Catalina, Carolien A. M. Koeleman, André M. Deelder, Manfred Wuhrer, Electron transfer dissociation of N‐glycopeptides: loss of the entire N‐glycosylated asparagine side chain Rapid Communications in Mass Spectrometry. ,vol. 21, pp. 1053- 1061 ,(2007) , 10.1002/RCM.2929
Jeffrey D Esko, Ajit Varki, Gerald W Hart, Pamela Stanley, Carolyn R Bertozzi, Richard D Cummings, Marilynn E Etzler, Hudson H Freeze, Essentials of Glycobiology ,(1999)
G. Müller, S. Ruppert, E. Schmid, G. Schütz, Functional analysis of alternatively spliced tyrosinase gene transcripts. The EMBO Journal. ,vol. 7, pp. 2723- 2730 ,(1988) , 10.1002/J.1460-2075.1988.TB03126.X
Melanie J. Schroeder, Donna J. Webb, Jeffrey Shabanowitz, Alan F. Horwitz, Donald F. Hunt, Methods for the detection of paxillin post-translational modifications and interacting proteins by mass spectrometry. Journal of Proteome Research. ,vol. 4, pp. 1832- 1841 ,(2005) , 10.1021/PR0502020
Dennis J. Selkoe, Cell biology of the amyloid beta-protein precursor and the mechanism of Alzheimer's disease. Annual Review of Cell Biology. ,vol. 10, pp. 373- 403 ,(1994) , 10.1146/ANNUREV.CB.10.110194.002105
Chhinder P. Sodhi, Ruth G. Perez, Numa R. Gottardi-Littell, Phosphorylation of β-amyloid precursor protein (APP) cytoplasmic tail facilitates amyloidogenic processing during apoptosis Brain Research. ,vol. 1198, pp. 204- 212 ,(2008) , 10.1016/J.BRAINRES.2008.01.031
Mikhail M. Savitski, Michael L. Nielsen, Roman A. Zubarev, Side-chain losses in electron capture dissociation to improve peptide identification. Analytical Chemistry. ,vol. 79, pp. 2296- 2302 ,(2007) , 10.1021/AC0619332