ArticleMolecular medicine reports2020
Proteomic analysis of differentially expressed proteins in the serum of patients with acute renal allograft rejection using iTRAQ labelling technology.
Article in Molecular medicine reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 10 citations in OpenAlex.
- Untargeted Plasma Proteomic Signatures and Late Graft Failure in Kidney Transplant Recipients.Transplantation · 2026Article
- The Role of Keratin in the Mechanisms of Kidney Diseases.BioMed research international · 2026Review
- Multi-omics Approach in Kidney Transplant: Lessons Learned from COVID-19 Pandemic.Current transplantation reports · 2023Article
- Biomarker-Development Proteomics in Kidney Transplantation: An Updated Review.International journal of molecular sciences · 2023Review
- Mass spectrometry-based proteomics for advancing solid organ transplantation research.Frontiers in transplantation · 2023Review
- Proteomics for Biomarker Discovery for Diagnosis and Prognosis of Kidney Transplantation Rejection.Proteomes · 2022Review
Corrections and comments
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Authors and funding
15 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transplantation is currently the best treatment for patients with end‑stage renal disease. However, acute rejection (AR) is the major source of failure in renal transplantation. The current best practice for the diagnosis of AR involves renal biopsy, but it is invasive, time‑consuming, costly and inconvenient. Sensitive and less invasive detection of AR episodes in renal transplant patients is essential to preserve allograft function. The present study applied isobaric tags for relative and absolute quantitation (iTRAQ) mass spectrometry to analyze serum protein expression in patients with AR and healthy controls. Overall, 1,399 proteins were identified. Using a cut‑off of Q<0.05 and a fold change of >1.2 for the variation in expression, 109 proteins were identified to be differentially expressed between the AR and control groups, 72 of which were upregulated and 37 were downregulated. Several proteins, including properdin, keratin 1, lipoprotein(a) and vitamin D‑binding protein, may have roles in the pathogenesis of AR. The present study focused on iTRAQ‑based proteomic profiling of serum samples in AR. Insight from the present study may help advance the understanding of the molecular mechanisms of AR and identify potential novel biomarkers of AR for further characterization.
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