PXD001528

PXD001528 is an original dataset announced via ProteomeXchange.

Title	Paraquat Exposure and Sod2 Knockdown have Dissimilar Impacts on the Drosophila melanogaster Carbonylated Protein Proteome
Description	Exposure to Paraquat and RNA interference knockdown of mitochondrial superoxide dismutase (Sod2) are known to result in significant lifespan reduction, locomotor dysfunction, and mitochondrial degeneration in Drosophila melanogaster. Both perturbations increase the flux of superoxide, a progenitor reactive oxygen species, but the molecular underpinnings of the resulting phenotypes are poorly understood. Improved understanding of such processes could lead to advances in the treatment of numerous age-related disorders. Superoxide toxicity can act through protein carbonylation. Analysis of carbonylated proteins is attractive since reactive carbonyl groups are not present in the twenty canonical amino acids and are amenable to labeling and enrichment strategies. Here, carbonylated proteins were labeled with biotin hydrazide and enriched on streptavidin-coated beads. On-bead digestion was used to release carbonylated protein peptides, with relative abundance ratios versus controls obtained using the iTRAQ mass spectrometry-based proteomics approach. While Paraquat exposure and Sod2 knockdown have similar phenotypes, differences in protein carbonylation were anticipated because Paraquat exposure was expected to increase the concentration of superoxide throughout the cell while Sod2 knockdown was only expected to raise the concentration of superoxide in the mitochondrial matrix. Paraquat exposure resulted in widespread increases in carbonylated protein relative abundance: the median Paraquat-exposed to control carbonylated protein relative abundance ratio was 1.53. For Sod2 knockdown, in contrast, the median carbonylated protein relative abundance ratios were 1.13 versus the RNA interference driver control and 1.05 versus the RNA interference transgene control. However, some proteins did show large increases in carbonylated protein relative abundance on Sod2 knockdown, most notably cytochrome c oxidase subunit Vb, possibly providing some indication of the molecular basis of the Sod2-knockdown phenotype.
HostingRepository	PRIDE
AnnounceDate	2014-11-26
AnnouncementXML	Submission_2014-11-26_04:43:26.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD001528
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	David Simpson
SpeciesList	scientific name: Drosophila melanogaster (Fruit fly); NCBI TaxID: 7227;
ModificationList	monohydroxylated residue; dehydrated residue; iTRAQ4plex-116 reporter+balance reagent acylated residue; iodoacetamide derivatized residue; deaminated residue
Instrument	LTQ Orbitrap Velos

Revision	Datetime	Status	ChangeLog Entry
0	2014-11-24 01:01:00	ID requested
⏵ 1	2014-11-26 04:43:28	announced

Narayanasamy SK, Simpson DC, Martin I, Grotewiel M, Gronert S, Paraquat exposure and Sod2 knockdown have dissimilar impacts on the Drosophila melanogaster carbonylated protein proteome. Proteomics, 14(21-22):2566-77(2014) [pubmed]

curator keyword: Biological

submitter keyword: Drosophila melanogaster, protein carbonylation, Orbitrap, HCD, iTRAQ

Scott Gronert
contact affiliation	Virginia Commonwealth University
contact email	sgronert@vcu.edu
lab head
David Simpson
contact affiliation	Virginia Commonwealth University, Department of Chemistry
contact email	dsimpson3@vcu.edu
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD001528
     1. Label: PRIDE project
     2. Name: Paraquat Exposure and Sod2 Knockdown have Dissimilar Impacts on the Drosophila melanogaster Carbonylated Protein Proteome