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Data on comparative proteomic profiling of human sperm affected by 4-tert-octylphenol in vitro.

ABSTRACT: This data article presents proteomic profiling and posttranslational modifications of sperm proteins relating to the research paper "4-tert-octylphenol injures motility and viability of human sperm by affecting cAMP-PKA/PKC-tyrosine phosphorylation signals." (Huang et al., 2018). Comparative proteomics was applied to identify the target biomarkers and the relevant molecular events of human sperm which were exposed to 0 (Dimethyl sulfoxide, DMSO), 0.1, or 0.3?mM 4-tert-octylphenol (4t-OP) for two hours in vitro. All differentially expressed (DE) proteins were then mapped to the human sperm proteome 2.0 (Wang et al., 2016) to clarify the posttranslational modifications (PTMs) of the DE proteins. We provide the associated mass spectrometry raw files; the PTMs in all the DE proteins, in DE proteins related to apoptosis, and in DE proteins related to motility. These data highlight the molecular mechanism relating to injured motility and viability of human sperm affected by 4t-OP.

SUBMITTER: Huang S

PROVIDER: S-EPMC6276628 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature

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Data on comparative proteomic profiling of human sperm affected by 4-tert-octylphenol in vitro.

Huang Shaoping S Cao Senyang S Zhou Tao T Kong Lu L Liang Geyu G

Data in brief 20181116

This data article presents proteomic profiling and posttranslational modifications of sperm proteins relating to the research paper "4-tert-octylphenol injures motility and viability of human sperm by affecting cAMP-PKA/PKC-tyrosine phosphorylation signals." (Huang et al., 2018). Comparative proteomics was applied to identify the target biomarkers and the relevant molecular events of human sperm which were exposed to 0 (Dimethyl sulfoxide, DMSO), 0.1, or 0.3 mM 4-tert-octylphenol (4t-OP) for two ...[more]

PMID: 30555862

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Project description:The male gamete is not completely mature after ejaculation and requires further events in the female genital tract to acquire fertilizing ability, including the processes of capacitation and acrosome reaction. In order to shed light on protein changes experienced by the sperm cell in preparation for fertilization, a comprehensive quantitative proteomic profiling based on isotopic peptide labeling and liquid chromatography followed by tandem mass spectrometry was performed on spermatozoa from three donors of proven fertility under three sequential conditions: purification with density gradient centrifugation, incubation with capacitation medium, and induction of acrosome reaction by exposure to the calcium ionophore A23187. After applying strict selection criteria for peptide quantification and for statistical analyses, 36 proteins with significant changes in their relative abundance within sperm protein extracts were detected. Moreover, the presence of peptide residues potentially harboring sites for post-translational modification was revealed, suggesting that protein modification may be an important mechanism in sperm maturation. In this regard, increased levels of proteins mainly involved in motility and signaling, both regulated by protein modifiers, were detected in sperm lysates following incubation with capacitation medium. In contrast, less abundant proteins in acrosome-reacted cell lysates did not contain potentially modifiable residues, suggesting the possibility that all those proteins might be relocated or released during the process. Protein-protein interaction analysis revealed a subset of proteins potentially involved in sperm maturation, including the proteins Erlin-2 (ERLIN2), Gamma-glutamyl hydrolase (GGH) and Transmembrane emp24 domain-containing protein 10 (TMED10). These results contribute to the current knowledge of the molecular basis of human fertilization. It should now be possible to further validate the potential role of the detected altered proteins as modulators of male infertility.

Dataset Information

Data on comparative proteomic profiling of human sperm affected by 4-tert-octylphenol in vitro.

Publications

Data on comparative proteomic profiling of human sperm affected by 4-tert-octylphenol in vitro.

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