Dataset Information

Quantitative cardiac phosphoproteomics profiling during ischemic/reperfusion in an immature swine model

ABSTRACT: Ischemia/Reperfusion (I/R) results in altered metabolic and molecular responses. Phosphorylation, a posttranslational modification, is one of the most noted regulatory mechanisms and differential phosphorylation affects numerous regulatory and signaling mechanisms. To further understand the phosphoproteomic changes that occur in the heart during I/R we utilized iTRAQ-based quantitative proteomic and LC-MS/MS techniques to obtain a profile of phosphopeptides expressed under control and I/R conditions. A total of 1896 phosphopeptides were identified, and 116 were assessed as significant. The 116 phosphopeptides represented 87 unique proteins. Analysis of the phosphopeptides using Motif-x identified 2 predominant motifs: arginine and proline-directed serine phosphorylation sites. Two proteins known to be altered by I/R were among the dataset obtained, phospholamban and pyruvate dehydrogenase, and were used to confirm validity of the profile. Functional characterization of the phosphopetides identified in this study could lead to further understanding of the signaling mechanisms involved during I/R damage in the heart, as well as identifying new areas to target therapeutic strategies.

INSTRUMENT(S): LTQ Orbitrap Velos

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

TISSUE(S): Cardiac Muscle, Cardiac Muscle Cell

DISEASE(S): Hypertrophic Cardiomyopathy

SUBMITTER: Matthew Monroe

LAB HEAD: Michael Portman, MD

PROVIDER: PXD006066 | Pride | 2017-05-02

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	MP_Heart_iTRAQ_01_Phos2_12May14_Frodo_14-01-36.mgf	Mgf
	MP_Heart_iTRAQ_01_Phos2_12May14_Frodo_14-01-36.pride.mgf.gz	Mgf
	MP_Heart_iTRAQ_01_Phos2_12May14_Frodo_14-01-36.raw	Raw
	MP_Heart_iTRAQ_01_Phos2_12May14_Frodo_14-01-36_msgfplus.mzid.gz	Mzid
	MP_Heart_iTRAQ_01_Phos2_12May14_Frodo_14-01-36_msgfplus.pride.mztab.gz	Mztab

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Publications

Quantitative cardiac phosphoproteomics profiling during ischemia-reperfusion in an immature swine model.

Ledee Dolena D Kang Min A MA Kajimoto Masaki M Purvine Samuel S Brewer Heather H Pasa-Tolic Ljiljana L Portman Michael A MA

American journal of physiology. Heart and circulatory physiology 20170428 1

Ischemia-reperfusion (I/R) results in altered metabolic and molecular responses, and phosphorylation is one of the most noted regulatory mechanisms mediating signaling mechanisms during physiological stresses. To expand our knowledge of the potential phosphoproteomic changes in the myocardium during I/R, we used Isobaric Tags for Relative and Absolute Quantitation-based analyses in left ventricular samples obtained from porcine hearts under control or I/R conditions. The data are available via P ...[more]

PMID: 28455290

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Project description:Phosphorylation is a regulatory mechanism by which intracellular apicomplexan parasites control the process of invading and modifying host cells. However, the sporulated oocysts’ phosphoprotein repertoires between virulent and avirulent strains of Toxoplasma gondii and the underlying mechanisms contributing to virulence is still a mystery. A quantitative analysis of the sporulated oocysts’ phosphoproteome profile of T. gondii virulent and avirulent strains belonging to different genotypes was conducted to reveal phosphoprotein expression patterns that contribute to the virulence of a particular phenotype. Phosphopeptides from the sporulated oocysts of the virulent strain PYS (Chinese ToxoDB#9) and the avirulent strain type II (PRU strain) were enriched by titanium dioxide (TiO2) affinity chromatography and quantified using iBT technology. A total of 10,645 unique phosphopeptides, 8,181 nonredundant phosphorylation sites and 2,792 phosphoproteins were identified. The quantitative analysis identified 4,129 differentially expressed phosphopeptides (DEPs) between sporulated oocysts of the PYS strain and PRU strain (|log1.5 fold change| > 1 and P < 0.05), including 2,485 upregulated and 1,644 downregulated phosphopeptides. Motif analysis identified 24 motifs from the upregulated phosphorylated peptides including 22 serine motifs and two threonine motifs (TPE and TP), and 15 motifs from the downregulated phosphorylated peptides including 12 serine motifs and three threonine motifs (TP, RxxT and KxxT) in PYS strain when comparing PYS/PRU. Several kinases were consistent with motifs of overrepresented phosphopeptides, such as PKA, PKG, CKII, IKK, MAPK, EGFR, INSR, Jak, Syk, Src, Ab1. GO analysis, KEGG pathway analysis and STRING analysis revealed differentially expressed phosphoproteins (DEPs) exhibiting significant functional properties. Kinase associated network analysis showed that AGC kinase had the greatest connected peptides. Our findings reveal significant difference in phosphopeptides of sporulated oocysts between virulent and avirulent T. gondii strains, which provides solid foundation for further exploring the mechanisms contributing to the virulence of T. gondii.