Evidence map›Paper›PMID 25680958›Full record

ArticleMolecular & cellular proteomics : MCP2015

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

Heguo Yu, Hua Diao, Chunmei Wang, Yan Lin, Fudong Yu, Hui Lu, Wei Xu, Zheng Li, Huijuan Shi, Shimin Zhao and 2 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
8.4field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

26 citing papers in PubMed, 68 citations in OpenAlex.

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  8. Review
  9. Article
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  12. Article
  13. Functions and Mechanisms of Lysine Glutarylation in Eukaryotes.Frontiers in cell and developmental biology · 2021
    Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Proteomic Changes in Human Sperm During SequentialFrontiers in cell and developmental biology · 2019
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors at 5 institutions in 1 country.

Heguo YuFrom the NPFPC Key Laboratory of Contraceptives and Devices, Shanghai Institute of Planned Parenthood Research, Institutes of Reproduction and Development.
Hua DiaoFrom the NPFPC Key Laboratory of Contraceptives and Devices, Shanghai Institute of Planned Parenthood Research, Institutes of Reproduction and Development.
Chunmei WangShanghai 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.
Yan LinSchool of Life Sciences, and Molecular and Cell Biology Lab, Fudan University, Shanghai 200032, China.
Fudong YuDepartment of General Surgery, Shanghai First People's Hospital, Medical College, Shanghai Jiaotong University, Shanghai 200080, China, and.
Hui LuDepartment of Urology, Renji Hospital, School of Medicine, Shanghai Jiaotong University, Shanghai 200001, China.
Wei XuSchool of Life Sciences, and Molecular and Cell Biology Lab, Fudan University, Shanghai 200032, China.
Zheng LiDepartment of Urology, Renji Hospital, School of Medicine, Shanghai Jiaotong University, Shanghai 200001, China.
Huijuan ShiFrom the NPFPC Key Laboratory of Contraceptives and Devices, Shanghai Institute of Planned Parenthood Research, Institutes of Reproduction and Development.
Shimin ZhaoSchool of Life Sciences, and Molecular and Cell Biology Lab, Fudan University, Shanghai 200032, China, zhaosm@fudan.edu.cn.
Yuchuan ZhouShanghai 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.
Yonglian ZhangFrom 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.
Fudan University · CNChinese Academy of Sciences · CNShanghai Institute of Planned Parenthood Research · CNCenter for Excellence in Molecular Cell Science · CNRenji Hospital · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

AcetylationAmino Acid MotifsAmino Acid SequenceAnimalsAntibodies, MonoclonalAntibody SpecificityCatechinConsensus SequenceCyclosporineHumansLysineMaleMembrane Potential, MitochondrialMiceMolecular Sequence DataPeptide LibraryAntibodies, MonoclonalCatechinCyclosporineepigallocatechin gallateLysinePeptide LibraryPeptidesVDAC2 protein, humanVoltage-Dependent Anion Channel 2

Identifiers

PMID25680958
PMCPMC4390248
OpenAlexW2097861942

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.