Dynamic proteome signatures in gametes, embryos and their maternal environment
Georg J. Arnold A B C and T. Frohlich A
+ Author Affiliations
- Author Affiliations
A Laboratory for Functional Genome Analysis LAFUGA, GENE Center, Ludwig-Maximilians-Universitaet, München, Germany.
B Present address: Feodor-Lynen-Straße 25, D-81377 München, Germany.
C Corresponding author. Email: arnold@genzentrum.uni-muenchen.de
Reproduction, Fertility and Development 23(1) 81-93 https://doi.org/10.1071/RD10223
Published: 7 December 2010
Abstract
Comprehensive molecular analysis at the level of proteins represents a technically demanding, but indispensable, task since several post-transcriptional regulation mechanisms disable a valid prediction of quantitative protein expression profiles from transcriptome analysis. In crucial steps of gamete and early embryo development, de novo transcription is silenced, meaning that almost all macromolecular events take place at the level of proteins. In this review, we describe selected examples of dynamic proteome signatures addressing capacitation of spermatozoa, in vitro maturation of oocytes, effect of oestrous cycle on oviduct epithelial cells and embryo-induced alterations to the maternal environment. We also present details of the experimental strategies applied and the experiments performed to verify quantitative proteomic data. Far from being comprehensive, examples were selected to cover several mammalian species as well as the most powerful proteomic techniques currently applied. To enable non-experts in the field of proteomics to appraise published proteomic data, our examples are preceded by a customised description of quantitative proteomic methods, covering 2D difference gel electrophoresis (2D-DIGE), nano-liquid chromatography combined with tandem mass spectrometry, and label-free as well as stable-isotope labelling strategies for mass spectrometry-based quantifications.
Additional keywords: 2D-DIGE, 2D-PAGE, mass spectrometry, nano-chromatography, proteomics, stable-isotope labelling, tandem mass spectrometry.
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