Dataset Information

Integrative analysis of proteomic and phosphoproteomic of granulosa cells during follicular atresia in porcine

ABSTRACT: Ovarian follicular atresia is a natural physiological process, but its mechanism is not fully understood. In this study, a quantitative proteomic and phosphoproteomic of granulosa cell (GC) in the healthy (H), slightly atretic (SA), and atretic follicles (A) of porcine were performed by TMT labeling, enrichment of phosphopeptides and LC-MS/MS analysis. Altogether, 6,201 proteins were quantified, and 4,723 phosphorylation sites of 1,760 proteins were quantified. There are 24 (11 up, 13 down) and 50 (29 up, 21 down) proteins with FC>5 in H/SA and H/A, respectively. In addition, there are 20 (H/SA, up) and 39 (H/A, up) phosphosites with FC>7, which could serve as potential biomarkers to distinguish different quality categories of follicles. The results of western blotting and immunofluorescence indicated the reliability of the proteomic analysis. Further analysis of the differential expressed proteins (DEPs) and phosphorylated proteins (DEPPs) revealed some key proteins (e.g. MIF, beta catenin, integrin β2), key phosphosites (e.g. S76 of Caspase6, S22 and S636 of Lamin A/C), pathways (e.g. apoptosis, regulation of actin cytoskeleton pathway), transcription factors (e.g. STAT5A, FOXO1, BCLAF1), and kinases (e.g. PBK, CDK5, CDK12, AKT3) that involved in atresia process. Our proteomic and phosphoproteomic profiling and functional research comprehensively analyze the dynamic changes of protein expression and phosphorylation during follicular atresia, and gave a new explanation for the regulation of this process.

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Sus Scrofa Domesticus (domestic Pig)

TISSUE(S): Cell Culture

SUBMITTER: Feng Feng

LAB HEAD: Shenming Zeng

PROVIDER: PXD020899 | Pride | 2021-09-09

REPOSITORIES: Pride

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Publications

Integrative Proteomic and Phosphoproteomic Analyses of Granulosa Cells During Follicular Atresia in Porcine.

Yang Feng F Liu Qiang Q Chen Yanhong Y Ye Huizhen H Wang Han H Zeng Shenming S

Frontiers in cell and developmental biology 20210115

Ovarian follicular atresia is a natural physiological process; however, the mechanism is not fully understood. In this study, quantitative proteomic and phosphoproteomic analyses of granulosa cells (GCs) in healthy (H), slightly atretic (SA), and atretic follicles (A) of porcine were performed by TMT labeling, enrichment of phosphopeptides, and liquid chromatography with tandem mass spectrometry (LC-MS/MS) analysis. In total, 6,201 proteins were quantified, and 4,723 phosphorylation sites of 1,7 ...[more]

PMID: 33520998

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Project description:Background: Cardiovascular diseases remain the leading cause of morbidity and mortality worldwide, most of which are caused by atherosclerosis. Discerning processes that participate in macrophage-to-foam cell formation are critical for understanding the basic mechanisms underlying atherosclerosis. To explore the molecular mechanisms of foam cell formation, the differentially expressed proteins were identified. Methods: In this paper, human monocytes, macrophage colony-stimulating factor induced macrophages, and oxidized low-density lipoprotein induced foam cells were cultured, and tandem mass tag (TMT) labeling combined with mass spectrometry (MS) were performed to find associations between foam cell transformation and proteome profiles. Results: Totally, 5146 quantifiable proteins were identified, among which 1515 and 182 differentially expressed proteins (DEPs) were found in macrophage/monocyte and foam cell/macrophage, respectively, using a cutoff of 1.5-fold change. Subcellular localization analysis revealed that downregulated DEPs of macrophages/monocytes were mostly located in the nucleus and upregulated DEPs of foam cells/macrophages mostly located in the plasma membrane and extracellular. Functional analysis of DEPs demonstrated that cholesterol metabolism related proteins were upregulated in foam cells, whereas the immune response-related proteins were downregulated in foam cells. The protein-interaction network showed that the DEPs with the highest interaction intensity between macrophages and foam cells were mainly concentrated in lysosomes and the endoplasmic reticulum. Conclusions: This study for the first time to perform quantitative proteomic investigation by TMT labeling and LC-MS/MS to identify differentially expressed proteins in human monocyte, macrophage, and foam cell. The results confirmed cholesterol metabolism was upregulated in foam cells, while immune response was suppressed, which suggested that foam cells were not the population that promote inflammation. In addition, KEGG enrichment analysis and protein-protein interaction indicated that the differentially expressed proteins locating in the endoplasmic reticulum and lysosomes may be key targets to regulate foam cell formation. These data provide a basis for identifying the potential proteins associated with the molecular mechanism involved in the transformation of macrophages to foam cells.

Dataset Information

Integrative analysis of proteomic and phosphoproteomic of granulosa cells during follicular atresia in porcine

Publications

Integrative Proteomic and Phosphoproteomic Analyses of Granulosa Cells During Follicular Atresia in Porcine.

Similar Datasets

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