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PMID: 25038526 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Insights into the lysine acetylproteome of human sperm.

Journal of proteomics ·Vol. 109 ·2014-09-23 ·Pages 199-211

Sun G, Jiang M, Zhou T, Guo Y, Cui Y, Guo X, Sha J

Abstract

Protein lysine acetylation is a dynamic and reversible post-modification that is known to play diverse functions in eukaryotes. Nevertheless, the composition and function of non-histone lysine acetylation in gametes remain unknown. In humans, only capacitated sperm have the capacity to fertilize an egg. In the present study, we found complex composition of lysine acetylated proteins in capacitated human sperm. In vitro fertilization inhibition assay by anti-acetyllysine antibody showed essential roles of lysine acetylation in fertilization. And inhibition of lysine deacetylases, the histone deacetylases, by trichostatin A and nicotinamide, could significantly suppress sperm motility. After immunopurification enrichment of acetylpeptides with anti-acetyllysine antibody and high-throughput liquid chromatography-tandem mass spectrometry identification, we characterized 1206 lysine acetylated sites, corresponding to 576 lysine acetylated proteins in human capacitated sperm. Bioinformatics analysis showed that these proteins are associated with sperm functions, including motility, capacitation, acrosome reaction and sperm-egg interaction. Thus, lysine acetylation is expected to be an important regulatory mechanism for sperm functions. And our characterization of lysine acetylproteome could be a rich resource for the study of male fertility. Mature sperm are almost transcriptionally and translationally silent, thus post-translational modifications play important roles in sperm functions. Till now, only two types of PTMs, phosphorylation and glycosylation, are well studied in normal human sperm based on large scale proteomics. In the present study, we established the acetylproteome of capacitated human sperm. Over 1000 lysine acetylated sites were identified. Bioinformatics analysis shows that lysine acetylated proteins participate in many biological events of sperm functions. We further provided functional data that the lysine acetylation is essential for sperm motility and fertilization using histone acetylase inhibitors and anti-acetyllysine antibody. These data can be strong evidences for the important function of lysine acetylation in human sperm.

Keywords
Acetylproteome Capacitation Human sperm Lysine acetylation Proteomics
MeSH Terms
Acetylation Acrosome Reaction/drug effects,physiology Adult Histone Deacetylase Inhibitors/pharmacology Histone Deacetylases/metabolism Humans Hydroxamic Acids/pharmacology Lysine/metabolism Male Proteome/metabolism Sperm Motility/drug effects,physiology Spermatozoa/metabolism
Chemicals
Histone Deacetylase Inhibitors Hydroxamic Acids Proteome trichostatin A Histone Deacetylases Lysine
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Sun Guohai
State Key Laboratory of Reproductive Medicine, Department of Histology and Embryology, Nanjing Medical University, Nanjing 210029, China.
Jiang Min
State Key Laboratory of Reproductive Medicine, Department of Histology and Embryology, Nanjing Medical University, Nanjing 210029, China.
Zhou Tao
State Key Laboratory of Reproductive Medicine, Department of Histology and Embryology, Nanjing Medical University, Nanjing 210029, China.
Guo Yueshuai
State Key Laboratory of Reproductive Medicine, Department of Histology and Embryology, Nanjing Medical University, Nanjing 210029, China.
Cui Yiqiang
State Key Laboratory of Reproductive Medicine, Department of Histology and Embryology, Nanjing Medical University, Nanjing 210029, China.
Guo Xuejiang
State Key Laboratory of Reproductive Medicine, Department of Histology and Embryology, Nanjing Medical University, Nanjing 210029, China. Electronic address: [email protected].
Sha Jiahao
State Key Laboratory of Reproductive Medicine, Department of Histology and Embryology, Nanjing Medical University, Nanjing 210029, China. Electronic address: [email protected].
Article Info
Journal
Journal of proteomics
Abbr.
J Proteomics
ISSN
1876-7737
Published
2014-09-23
Epub
2014-00-17
Pages
199-211
Language
English
Region
Netherlands
NLM ID
101475056
Subset
IM
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