Journal
MOLECULAR & CELLULAR PROTEOMICS
Volume 13, Issue 7, Pages 1690-1704Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/mcp.M113.036392
Keywords
-
Categories
Funding
- NCI, National Institutes of Health, NCI Clinical Proteomics Tumor Analysis Consortium [U24CA160034, U24CA160019, U24CA160035, U24CA159988, U24CA160036]
- Susan G. Komen for the Cure [BCTR0707808, KG090422]
- NCI, National Institutes of Health [P30CA091842, 3P50 CA68438]
- CTSA [UL1 RR024992]
- MD Anderson Cancer Center Support Grant (CCSG) from National Institutes of Health [CA016672]
- [PO1CA099031]
- [U54CA112970]
- [KG081694]
- [P30 CA16672]
Ask authors/readers for more resources
Protein abundance and phosphorylation convey important information about pathway activity and molecular pathophysiology in diseases including cancer, providing biological insight, informing drug and diagnostic development, and guiding therapeutic intervention. Analyzed tissues are usually collected without tight regulation or documentation of ischemic time. To evaluate the impact of ischemia, we collected human ovarian tumor and breast cancer xenograft tissue without vascular interruption and performed quantitative proteomics and phosphoproteomics after defined ischemic intervals. Although the global expressed proteome and most of the >25,000 quantified phosphosites were unchanged after 60 min, rapid phosphorylation changes were observed in up to 24% of the phosphoproteome, representing activation of critical cancer pathways related to stress response, transcriptional regulation, and cell death. Both pan-tumor and tissue-specific changes were observed. The demonstrated impact of pre-analytical tissue ischemia on tumor biology mandates caution in interpreting stress-pathway activation in such samples and motivates reexamination of collection protocols for phosphoprotein analysis.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available