Journal article
Sialylation of Asparagine 612 Inhibits Aconitase Activity during Mouse Sperm Capacitation; a Possible Mechanism for the Switch from Oxidative Phosphorylation to Glycolysis
Ana Izabel Silva Balbin Villaverde, Rachel A Ogle, Peter Lewis, Vincenzo Carbone, Tony Velkov, Jacob K Netherton, Mark A Baker
Molecular & Cellular Proteomics | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | Published : 2020
Abstract
After ejaculation, mammalian spermatozoa must undergo a process known as capacitation in order to successfully fertilize the oocyte. Several post-translational modifications occur during capacitation, including sialylation, which despite being limited to a few proteins, seems to be essential for proper sperm-oocyte interaction. Regardless of its importance, to date, no single study has ever identified nor quantified which glycoproteins bearing terminal sialic acid (Sia) are altered during capacitation. Here we characterize sialylation during mouse sperm capacitation. Using tandem MS coupled with liquid chromatography (LC-MS/MS), we found 142 nonreductant peptides, with 9 of them showing pote..
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Funding Acknowledgements
This work was supported by the Brazilian National Council for Scientific and Technological Development (CNPq).