---
title: "AGR2 inhibition increases GRP78 secretion and sensitizes GEJ adenocarcinoma to ER stress"
id: "pubmed-42330887"
canonical_url: "https://medichelpline.com/clinical-feed/pubmed-42330887"
content_type: "clinical_feed_article"
specialty: "Oncology"
source_name: "PubMed / NCBI"
source_url: "https://pubmed.ncbi.nlm.nih.gov/42330887/"
doi: "10.1016/j.bbrc.2026.154181"
published_at: "2026-09-03T00:00:00.000Z"
evidence_level: "Journal Article"
license: "CC-BY-NC-4.0 / Informational Use"
---
# AGR2 inhibition increases GRP78 secretion and sensitizes GEJ adenocarcinoma to ER stress
## Provenance & Clinical Metadata
- **Canonical URL:** https://medichelpline.com/clinical-feed/pubmed-42330887
- **Specialty:** [Oncology](https://medichelpline.com/clinical-feed/oncology.md)
- **Primary Source:** PubMed / NCBI
- **Source URL:** [Original Journal Publication](https://pubmed.ncbi.nlm.nih.gov/42330887/)
- **DOI:** [10.1016/j.bbrc.2026.154181](https://doi.org/10.1016%2Fj.bbrc.2026.154181)
- **Published At:** 2026-09-03T00:00:00.000Z
- **Evidence Rating:** Journal Article
## Executive GIST (TL;DR)
- The study used shRNA-mediated silencing of **AGR2** in OE19 gastroesophageal junction (GEJ) adenocarcinoma cells to investigate effects on the cancer cell secretome and unfolded protein response (UPR). - High-throughput LC-MS/MS proteomics compared protein secretion profiles under basal conditions and after tunicamycin-induced **ER stress**. - Proteomic screening identified 75 differentially secreted proteins; AGR2 knockdown produced a broad up-secretion phenotype across the secretome. - Bioinformatic pathway analysis showed enrichment among secreted proteins for glycolysis, antigen processing and presentation, and extracellular matrix components. - The ER-resident chaperone **GRP78** (HSPA5) emerged as a key hub within the altered secretome following AGR2 depletion. - AGR2 silencing reduced intracellular GRP78 expression and impaired activation of the **UPR**, indicating compromised ER proteostasis. - Under tunicamycin-induced ER stress, AGR2-deficient cells exhibited a marked extracellular secretion of **GRP78**, described as a massive release into the extracellular space. - This extracellular release of GRP78 in AGR2-depleted cells correlated with significantly increased sensitivity to tunicamycin-induced cell death. - The authors conclude that AGR2 functions as a regulator of **GRP78** proteostasis and ER retention, supporting adaptive ER stress responses that may promote tumor cell survival in GEJ adenocarcinoma. - Keywords emphasized in the report include AGR2, ER stress, GRP78 (HSPA5), and secretome; conflict of interest statement reports no competing interests declared.
## Clinical Analysis & Structured Key Points
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Epub 2026 Jun 20. # Inhibition of AGR2 triggers secretion of GRP78 and sensitizes gastroesophageal junction adenocarcinoma cells to ER stress [Quentin Bourgery](https://pubmed.ncbi.nlm.nih.gov/?term=Bourgery+Q&cauthor_id=42330887)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42330887/#full-view-affiliation-1 "OncoLille Interdisciplinary Cancer Research Institute, CRCLille "Cancer Research Center of Lille" Laboratory, CNRS UMR9020 - Inserm U1366 - University of Lille, CHU Lille, Pasteur Institute of Lille, Lille, 59000, France."), [Nathalie Martin](https://pubmed.ncbi.nlm.nih.gov/?term=Martin+N&cauthor_id=42330887)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42330887/#full-view-affiliation-1 "OncoLille Interdisciplinary Cancer Research Institute, CRCLille "Cancer Research Center of Lille" Laboratory, CNRS UMR9020 - Inserm U1366 - University of Lille, CHU Lille, Pasteur Institute of Lille, Lille, 59000, France."), [Clémentine De Schutter](https://pubmed.ncbi.nlm.nih.gov/?term=De+Schutter+C&cauthor_id=42330887)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42330887/#full-view-affiliation-1 "OncoLille Interdisciplinary Cancer Research Institute, CRCLille "Cancer Research Center of Lille" Laboratory, CNRS UMR9020 - Inserm U1366 - University of Lille, CHU Lille, Pasteur Institute of Lille, Lille, 59000, France."), [Stéphanie Flament](https://pubmed.ncbi.nlm.nih.gov/?term=Flament+S&cauthor_id=42330887)[ 2 ](https://pubmed.ncbi.nlm.nih.gov/42330887/#full-view-affiliation-2 "MSAP, Miniaturization for Synthesis, Analysis & Proteomics, UAR 3290, University of Lille, Lille, 59000, France."), [Fabrice Bray](https://pubmed.ncbi.nlm.nih.gov/?term=Bray+F&cauthor_id=42330887)[ 2 ](https://pubmed.ncbi.nlm.nih.gov/42330887/#full-view-affiliation-2 "MSAP, Miniaturization for Synthesis, Analysis & Proteomics, UAR 3290, University of Lille, Lille, 59000, France."), [Olivier Pluquet](https://pubmed.ncbi.nlm.nih.gov/?term=Pluquet+O&cauthor_id=42330887)[ 3 ](https://pubmed.ncbi.nlm.nih.gov/42330887/#full-view-affiliation-3 "OncoLille Interdisciplinary Cancer Research Institute, CRCLille "Cancer Research Center of Lille" Laboratory, CNRS UMR9020 - Inserm U1366 - University of Lille, CHU Lille, Pasteur Institute of Lille, Lille, 59000, France. Electronic address: olivier.pluquet@cnrs.fr.") Affiliations Expand ### Affiliations * 1 OncoLille Interdisciplinary Cancer Research Institute, CRCLille "Cancer Research Center of Lille" Laboratory, CNRS UMR9020 - Inserm U1366 - University of Lille, CHU Lille, Pasteur Institute of Lille, Lille, 59000, France. * 2 MSAP, Miniaturization for Synthesis, Analysis & Proteomics, UAR 3290, University of Lille, Lille, 59000, France. * 3 OncoLille Interdisciplinary Cancer Research Institute, CRCLille "Cancer Research Center of Lille" Laboratory, CNRS UMR9020 - Inserm U1366 - University of Lille, CHU Lille, Pasteur Institute of Lille, Lille, 59000, France. Electronic address: olivier.pluquet@cnrs.fr. * PMID: **42330887** * DOI: [ 10.1016/j.bbrc.2026.154181 ](https://doi.org/10.1016/j.bbrc.2026.154181) Free article Item in Clipboard # Inhibition of AGR2 triggers secretion of GRP78 and sensitizes gastroesophageal junction adenocarcinoma cells to ER stress Quentin Bourgery et al. Biochem Biophys Res Commun. 2026. Free article Show details Display options Display options Format Abstract PubMed PMID Biochem Biophys Res Commun Actions * [ Search in PubMed ](https://pubmed.ncbi.nlm.nih.gov/?term=%22Biochem+Biophys+Res+Commun%22%5Bjour%5D&sort=date&sort_order=desc) * [ Search in NLM Catalog ](https://www.ncbi.nlm.nih.gov/nlmcatalog?term=%22Biochem+Biophys+Res+Commun%22%5BTitle+Abbreviation%5D) * [ Add to Search ](https://pubmed.ncbi.nlm.nih.gov/42330887/) . 2026 Sep 3:829:154181. doi: 10.1016/j.bbrc.2026.154181. Epub 2026 Jun 20. ### Authors [Quentin Bourgery](https://pubmed.ncbi.nlm.nih.gov/?term=Bourgery+Q&cauthor_id=42330887)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42330887/#short-view-affiliation-1 "OncoLille Interdisciplinary Cancer Research Institute, CRCLille "Cancer Research Center of Lille" Laboratory, CNRS UMR9020 - Inserm U1366 - University of Lille, CHU Lille, Pasteur Institute of Lille, Lille, 59000, France."), [Nathalie Martin](https://pubmed.ncbi.nlm.nih.gov/?term=Martin+N&cauthor_id=42330887)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42330887/#short-view-affiliation-1 "OncoLille Interdisciplinary Cancer Research Institute, CRCLille "Cancer Research Center of Lille" Laboratory, CNRS UMR9020 - Inserm U1366 - University of Lille, CHU Lille, Pasteur Institute of Lille, Lille, 59000, France."), [Clémentine De Schutter](https://pubmed.ncbi.nlm.nih.gov/?term=De+Schutter+C&cauthor_id=42330887)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42330887/#short-view-affiliation-1 "OncoLille Interdisciplinary Cancer Research Institute, CRCLille "Cancer Research Center of Lille" Laboratory, CNRS UMR9020 - Inserm U1366 - University of Lille, CHU Lille, Pasteur Institute of Lille, Lille, 59000, France."), [Stéphanie Flament](https://pubmed.ncbi.nlm.nih.gov/?term=Flament+S&cauthor_id=42330887)[ 2 ](https://pubmed.ncbi.nlm.nih.gov/42330887/#short-view-affiliation-2 "MSAP, Miniaturization for Synthesis, Analysis & Proteomics, UAR 3290, University of Lille, Lille, 59000, France."), [Fabrice Bray](https://pubmed.ncbi.nlm.nih.gov/?term=Bray+F&cauthor_id=42330887)[ 2 ](https://pubmed.ncbi.nlm.nih.gov/42330887/#short-view-affiliation-2 "MSAP, Miniaturization for Synthesis, Analysis & Proteomics, UAR 3290, University of Lille, Lille, 59000, France."), [Olivier Pluquet](https://pubmed.ncbi.nlm.nih.gov/?term=Pluquet+O&cauthor_id=42330887)[ 3 ](https://pubmed.ncbi.nlm.nih.gov/42330887/#short-view-affiliation-3 "OncoLille Interdisciplinary Cancer Research Institute, CRCLille "Cancer Research Center of Lille" Laboratory, CNRS UMR9020 - Inserm U1366 - University of Lille, CHU Lille, Pasteur Institute of Lille, Lille, 59000, France. Electronic address: olivier.pluquet@cnrs.fr.") ### Affiliations * 1 OncoLille Interdisciplinary Cancer Research Institute, CRCLille "Cancer Research Center of Lille" Laboratory, CNRS UMR9020 - Inserm U1366 - University of Lille, CHU Lille, Pasteur Institute of Lille, Lille, 59000, France. * 2 MSAP, Miniaturization for Synthesis, Analysis & Proteomics, UAR 3290, University of Lille, Lille, 59000, France. * 3 OncoLille Interdisciplinary Cancer Research Institute, CRCLille "Cancer Research Center of Lille" Laboratory, CNRS UMR9020 - Inserm U1366 - University of Lille, CHU Lille, Pasteur Institute of Lille, Lille, 59000, France. Electronic address: olivier.pluquet@cnrs.fr. * PMID: **42330887** * DOI: [ 10.1016/j.bbrc.2026.154181 ](https://doi.org/10.1016/j.bbrc.2026.154181) Item in Clipboard Full text links Cite Display options Display options Format Abstract PubMed PMID ## Abstract The endoplasmic reticulum (ER) chaperone Anterior Gradient 2 (AGR2) is overexpressed in various adenocarcinomas, promoting tumor progression and chemoresistance. However, its exact role in modulating the Unfolded Protein Response (UPR) and remodeling the cancer cell secretome under proteotoxic stress remains poorly understood. Using shRNA-mediated silencing of AGR2 combined with high-throughput LC-MS/MS proteomic analysis in OE19 gastroesophageal junction adenocarcinoma cells, we profiled the global changes in protein secretion under basal and tunicamycin-induced ER stress conditions. Proteomic screening identified 75 differentially secreted proteins, with AGR2 depletion triggering a widespread up-secretion phenotype. Bioinformatic analysis revealed enrichment in pathways related to glycolysis, antigen processing and presentation, and extracellular matrix components. Notably, the ER-resident chaperone GRP78 was identified as a critical hub protein within the secretome. AGR2 knockdown downregulated intracellular GRP78 expression, and compromised UPR activation. Under ER stress, the absence of AGR2 triggered a massive secretion of GRP78 in the extracellular space, which correlated with a significantly increased sensitivity to tunicamycin-induced cell death. These findings identify AGR2 as a key regulator of GRP78 proteostasis and ER retention. By controlling the balance between intracellular retention and extracellular release of GRP78, AGR2 supports adaptive ER stress response and may contribute to tumor cell survival in gastroesophageal junction adenocarcinoma. **Keywords:** AGR2 (Anterior gradient 2); ER stress; GRP78 (HSPA5); Secretome. Copyright © 2026 The Authors. Published by Elsevier Inc. All rights reserved. [PubMed Disclaimer](https://pubmed.ncbi.nlm.nih.gov/disclaimer/) ## Conflict of interest statement Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper. ## Similar articles * [ ER stress protein AGR2 precedes and is involved in the regulation of pancreatic cancer initiation. ](https://pubmed.ncbi.nlm.nih.gov/27941872/) Dumartin L, Alrawashdeh W, Trabulo SM, Radon TP, Steiger K, Feakins RM, di Magliano MP, Heeschen C, Esposito I, Lemoine NR, Crnogorac-Jurcevic T.Dumartin L, et al.Oncogene. 2017 Jun 1;36(22):3094-3103. doi: 10.1038/onc.2016.459. Epub 2016 Dec 12.Oncogene. 2017.PMID: 27941872Free PMC article. * [ CLPTM1L/CRR9 ectodomain interaction with GRP78 at the cell surface signals for survival and chemoresistance upon ER stress in pancreatic adenocarcinoma cells. ](https://pubmed.ncbi.nlm.nih.gov/30468251/) Clarke WR, Amundadottir L, James MA.Clarke WR, et al.Int J Cancer. 2019 Mar 15;144(6):1367-1378. doi: 10.1002/ijc.32012. Epub 2019 Jan 3.Int J Cancer. 2019.PMID: 30468251 * [ AGR2-mediated unconventional secretion of 14-3-3ε and α-actinin-4, responsive to ER stress and autophagy, drives chemotaxis in canine mammary tumor cells. ](https://pubmed.ncbi.nlm.nih.gov/38822246/) Yuan SH, Wu CC, Wang YC, Chan XY, Chu HW, Yang Y, Liu HP.Yuan SH, et al.Cell Mol Biol Lett. 2024 May 31;29(1):84. doi: 10.1186/s11658-024-00601-w.Cell Mol Biol Lett. 2024.PMID: 38822246Free PMC article. * [ Endoplasmic Reticulum Stress and Cancer: Could Unfolded Protein Response Be a Druggable Target for Cancer Therapy? ](https://pubmed.ncbi.nlm.nih.gov/36675080/) Bonsignore G, Martinotti S, Ranzato E.Bonsignore G, et al.Int J Mol Sci. 2023 Jan 13;24(2):1566. doi: 10.3390/ijms24021566.Int J Mol Sci. 2023.PMID: 36675080Free PMC article.Review. * [ Agr2 in cancer and beyond: unraveling its role during protein synthesis, ER stress, and as a predictive biomarker. ](https://pubmed.ncbi.nlm.nih.gov/40471515/) Salu P, Reindl KM.Salu P, et al.Mol Cell Biochem. 2025 Oct;480(10):5205-5219. doi: 10.1007/s11010-025-05318-8. Epub 2025 Jun 5.Mol Cell Biochem. 2025.PMID: 40471515Free PMC article.Review. 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