ArticleMolecular & cellular proteomics : MCP2018
Stable Isotope Dynamic Labeling of Secretomes (SIDLS) Identifies Authentic Secretory Proteins Released by Cancer and Stromal Cells.
Article in Molecular & cellular proteomics : MCP, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 27 citations in OpenAlex.
- Article
- Unlocking the black box: multimodal imaging and quantitative analysis of plant vesicular trafficking.Advanced biotechnology · 2026Review
- A Conserved Mycobacterial Nucleomodulin Hijacks the Host COMPASS Complex to Reprogram Pro-Inflammatory Transcription and Promote Intracellular Survival.bioRxiv : the preprint server for biology · 2026Article
- Deuterium labeling enables proteome-wide turnover kinetics analysis in cell culture.Cell reports methods · 2025Article
- Role of Long Non-Coding RNA X-Inactive-Specific Transcript (Non-coding RNA · 2025Article
- Proteomics applications in next generation induced pluripotent stem cell models.Expert review of proteomics · 2024Review
- Custom Workflow for the Confident Identification of Sulfotyrosine-Containing Peptides and Their Discrimination from Phosphopeptides.Journal of proteome research · 2023Article
- Elevated Serum Gastrin Is Associated with Melanoma Progression: Putative Role in Increased Migration and Invasion of Melanoma Cells.International journal of molecular sciences · 2023Article
- Mesenchymal Stromal Cell Secretome Is Affected by Tissue Source and Donor Age.Stem cells (Dayton, Ohio) · 2023Article
- Characterizing the secretome of EGFR mutant lung adenocarcinoma.Frontiers in oncology · 2023Article
- Secretomics-A Key to a Comprehensive Picture of Unconventional Protein Secretion.Frontiers in cell and developmental biology · 2022Article
- Chemerin acts via CMKLR1 and GPR1 to stimulate migration and invasion of gastric cancer cells: putative role of decreased TIMP-1 and TIMP-2.Oncotarget · 2019Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Analysis of secretomes critically underpins the capacity to understand the mechanisms determining interactions between cells and between cells and their environment. In the context of cancer cell micro-environments, the relevant interactions are recognized to be an important determinant of tumor progression. Global proteomic analyses of secretomes are often performed at a single time point and frequently identify both classical secreted proteins (possessing an N-terminal signal sequence), as well as many intracellular proteins, the release of which is of uncertain biological significance. Here, we describe a mass spectrometry-based method for stable isotope dynamic labeling of secretomes (SIDLS) that, by dynamic SILAC, discriminates the secretion kinetics of classical secretory proteins and intracellular proteins released from cancer and stromal cells in culture. SIDLS is a robust classifier of the different cellular origins of proteins within the secretome and should be broadly applicable to nonproliferating cells and cells grown in short term culture.
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