ArticleBMC cancer2015
Mechanism study of peptide GMBP1 and its receptor GRP78 in modulating gastric cancer MDR by iTRAQ-based proteomic analysis.
Article in BMC cancer, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers, 1 of them a synthesis that pooled it.
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17 citing papers in PubMed, 1 synthesis or guideline pooled it, 33 citations in OpenAlex.
- Expression of microRNA-99a-3p in Prostate Cancer Based on Bioinformatics Data and Meta-Analysis of a Literature Review of 965 Cases.Medical science monitor : international medical journal of experimental and clinical research · 2018Pooled it
- Peptide Drugs in Gastrointestinal Tumors: Integrating Targeting, Delivery, and Therapeutic Actions for Synergistic Strategies.Biomolecules · 2026Review
- Cell surface GRP78: a potential mechanism of therapeutic resistant tumors.Cancer cell international · 2023Review
- Tumor microenvironment responsive MnJournal of nanobiotechnology · 2022Article
- Proteomic analysis of inhibitor of apoptosis protein‑like protein‑2 on breast cancer cell proliferation.Molecular medicine reports · 2022Article
- Chaperone-mediated autophagy controls the turnover of E3 ubiquitin ligase MARCHF5 and regulates mitochondrial dynamics.Autophagy · 2021Article
- Proteomes Are of Proteoforms: Embracing the Complexity.Proteomes · 2021Review
- Molecular targeted treatment and drug delivery system for gastric cancer.Journal of cancer research and clinical oncology · 2021Review
- GRP78 targeting: Hitting two birds with a stone.Life sciences · 2020Review
- Mass spectrometry-based iTRAQ analysis of serum markers in patients with pancreatic cancer.Oncology letters · 2020Article
- GMBP1-conjugated manganese oxide nanoplates forRSC advances · 2020Article
- ITRAQ-based proteomic analysis reveals possible target-related proteins in human adrenocortical adenomas.BMC genomics · 2019Article
- A metabolomics and proteomics study of the Lactobacillus plantarum in the grass carp fermentation.BMC microbiology · 2018Article
- iTRAQ-based quantitative proteomic analysis of Yamanaka factors reprogrammed breast cancer cells.Oncotarget · 2017Article
- Identification of diagnostic markers involved in the pathogenesis of gastric cancer through iTRAQ-based quantitative proteomics.Data in brief · 2017Article
- Identification of specific biomarkers for gastric adenocarcinoma by ITRAQ proteomic approach.Scientific reports · 2016Article
- Dysregulation of non-coding RNAs in gastric cancer.World journal of gastroenterology · 2015Review
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12 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundMultidrug resistance (MDR) is a major obstacle to the treatment of gastric cancer (GC). Using a phage display approach, we previously obtained the peptide GMBP1, which specifically binds to the surface of MDR gastric cancer cells and is subsequently internalized. Furthermore, GMBP1 was shown to have the potential to reverse the MDR phenotype of gastric cancer cells, and GRP78 was identified as the receptor for this peptide. The present study aimed to investigate the mechanism of peptide GMBP1 and its receptor GRP78 in modulating gastric cancer MDR.
methodsFluorescence-activated cell sorting (FACS) and immunofluorescence staining were used to investigate the subcellular location and mechanism of GMBP1 internalization. iTRAQ was used to identify the MDR-associated downstream targets of GMBP1. Differentially expressed proteins were identified in GMBP1-treated compared to untreated SGC7901/ADR and SGC7901/VCR cells. GO and KEGG pathway analyses of the differentially expressed proteins revealed the interconnection of these proteins, the majority of which are involved in MDR. Two differentially expressed proteins were selected and validated by western blotting.
resultsGMBP1 and its receptor GRP78 were found to be localized in the cytoplasm of GC cells, and GRP78 can mediate the internalization of GMBP1 into MDR cells through the transferrin-related pathway. In total, 3,752 and 3,749 proteins were affected in GMBP1-treated SGC7901/ADR and SGC7901/VCR cells, respectively, involving 38 and 79 KEGG pathways. Two differentially expressed proteins, CTBP2 and EIF4E, were selected and validated by western blotting.
conclusionThis study explored the role and downstream mechanism of GMBP1 in GC MDR, providing insight into the role of endoplasmic reticulum stress protein GRP78 in the MDR of cancer cells.
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