Use of titanium dioxide to find phosphopeptide and total protein changes during epididymal sperm maturation
Date
2011
Authors
Baker, M.A.
Smith, N.D.
Hetherington, L.
Pelzing, M.
Condina, M.R.
Aitken, R.J.
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Journal article
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Journal of Proteome Research, 2011; 10(3):1004-1017
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Abstract
Although the overall performance of modern mass spectrometers has increased, proteomic analysis of complex samples still requires prefractionation either at the protein or peptide level to allow for in-depth analysis of normal cellular function. Here, we report a novel way to identify protein changes occurring during sperm development through the epididymis. Phosphopeptides were first enriched from either the rat caput or caudal regions of the epididymides using TiO2, and the profiles then quantitatively compared. We show that 77 TiO2-enriched peptides become significantly modified in the epididymis, equating to 53 proteins. Through the use of immunoblot analysis, we confirmed that three proteins, ornithine-decarboxylase antizyme 3, heat-shock protein 90α, and testis-lipid binding protein, undergo major protein loss during epididymal passage. Many other proteins, including t-complex protein 10 and Spata18 show testis unique expression, appear to undergo phosphorylation during this same time frame. These data provide mechanistic insight into the means by which spermatozoa acquire functionality during epididymal transit.
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Data source: , This material is available free of charge via the Internet at http://pubs.acs.org., https://doi.org/10.1021/pr1007224
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Copyright 2010 American Chemical Society