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      Acetylproteomic analysis reveals functional implications of lysine acetylation in human spermatozoa (sperm).

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          Abstract

          Male infertility is a medical condition that has been on the rise globally. Lysine acetylation of human sperm, an essential posttranslational modification involved in the etiology of sperm abnormality, is not fully understood. Therefore, we first generated a qualified pan-anti-acetyllysine monoclonal antibody to characterize the global lysine acetylation of uncapacitated normal human sperm with a proteomics approach. With high enrichment ratios that were up to 31%, 973 lysine-acetylated sites that matched to 456 human sperm proteins, including 671 novel lysine acetylation sites and 205 novel lysine-acetylated proteins, were identified. These proteins exhibited conserved motifs XXXKYXXX, XXXKFXXX, and XXXKHXXX, were annotated to function in multiple metabolic processes, and were localized predominantly in the mitochondrion and cytoplasmic fractions. Between the uncapacitated and capacitated sperm, different acetylation profiles in regard to functional proteins involved in sperm capacitation, sperm-egg recognition, sperm-egg plasma fusion, and fertilization were observed, indicating that acetylation of functional proteins may be required during sperm capacitation. Bioinformatics analysis revealed association of acetylated proteins with diseases and drugs. Novel acetylation of voltage-dependent anion channel proteins was also found. With clinical sperm samples, we observed differed lysine acetyltransferases and lysine deacetylases expression between normal sperm and abnormal sperm of asthenospermia or necrospermia. Furthermore, with sperm samples impaired by epigallocatechin gallate to mimic asthenospermia, we observed that inhibition of sperm motility was partly through the blockade of voltage-dependent anion channel 2 Lys-74 acetylation combined with reduced ATP levels and mitochondrial membrane potential. Taken together, we obtained a qualified pan-anti-acetyllysine monoclonal antibody, analyzed the acetylproteome of uncapacitated human sperm, and revealed associations between functional protein acetylation and sperm functions.

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          Author and article information

          Journal
          Mol. Cell Proteomics
          Molecular & cellular proteomics : MCP
          American Society for Biochemistry & Molecular Biology (ASBMB)
          1535-9484
          1535-9476
          Apr 2015
          : 14
          : 4
          Affiliations
          [1 ] From the NPFPC Key Laboratory of Contraceptives and Devices, Shanghai Institute of Planned Parenthood Research, Institutes of Reproduction and Development.
          [2 ] Shanghai Key Laboratory for Molecular Andrology, State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China.
          [3 ] School of Life Sciences, and Molecular and Cell Biology Lab, Fudan University, Shanghai 200032, China.
          [4 ] Department of General Surgery, Shanghai First People's Hospital, Medical College, Shanghai Jiaotong University, Shanghai 200080, China, and.
          [5 ] Department of Urology, Renji Hospital, School of Medicine, Shanghai Jiaotong University, Shanghai 200001, China.
          [6 ] School of Life Sciences, and Molecular and Cell Biology Lab, Fudan University, Shanghai 200032, China, zhaosm@fudan.edu.cn.
          [7 ] Shanghai Key Laboratory for Molecular Andrology, State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China, zhouych@sibs.ac.cn.
          [8 ] From the NPFPC Key Laboratory of Contraceptives and Devices, Shanghai Institute of Planned Parenthood Research, Institutes of Reproduction and Development, Shanghai Key Laboratory for Molecular Andrology, State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China, ylzhang@sibcb.ac.cn.
          Article
          M114.041384
          10.1074/mcp.M114.041384
          4390248
          25680958
          7c15f7fa-972e-45a9-9e62-955d5cf01b63
          History

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