ArticleBreast cancer : basic and clinical research2015
Signaling Pathway of GP88 (Progranulin) in Breast Cancer Cells: Upregulation and Phosphorylation of c-myc by GP88/Progranulin in Her2-Overexpressing Breast Cancer Cells.
Article in Breast cancer : basic and clinical research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- Dysregulation of adipokines in the serum of breast cancer patients - role in pathogenesis and potential clinical application (preliminary studies).Frontiers in immunology · 2026Article
- Circulating Progranulin: A Promising Novel Diagnostic and Prognostic Biomarker in Canine Oncology.Animals : an open access journal from MDPI · 2025Article
- Progranulinopathy: A diverse realm of disorders linked to progranulin imbalances.Cytokine & growth factor reviews · 2024Review
- Progranulin A Promotes Compensatory Hepatocyte Proliferation via HGF/c-Met Signaling after Partial Hepatectomy in Zebrafish.International journal of molecular sciences · 2021Article
- Anti-progranulin/GP88 antibody AG01 inhibits triple negative breast cancer cell proliferation and migration.Breast cancer research and treatment · 2021Article
- Expression of GP88 (Progranulin) Protein Is an Independent Prognostic Factor in Prostate Cancer Patients.Cancers · 2019Article
- Progranulin and its biological effects in cancer.Medical oncology (Northwood, London, England) · 2017Review
- Clonorchis sinensis granulin: identification, immunolocalization, and function in promoting the metastasis of cholangiocarcinoma and hepatocellular carcinoma.Parasites & vectors · 2017Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Her2 is a receptor tyrosine kinase overexpressed in 25% of breast tumors. We have shown that the 88 kDa autocrine growth and survival factor GP88 (progranulin) stimulated Her2 phosphorylation and proliferation and conferred Herceptin resistance in Her2-overexpressing cells. Herein, we report that GP88 stimulates c-myc phosphorylation and upregulates c-myc levels in Her2-overexpressing cells. c-myc phosphorylation and upregulation by GP88 were not observed in non-Her2-overexpressing breast cancer cells. c-myc activation was inhibited upon treatment with ERK, PI3 kinase, and c-src pathway inhibitors, U0126, LY294002, and PP2. GP88 also stimulated c-src phosphorylation, a known upstream regulator of c-myc. Thus, we describe here a signaling pathway for GP88 in Her2-overexpressing cells, with GP88 stimulating Src phosphorylation, followed by phosphorylation and upregulation of c-myc. These data would suggest that targeting GP88 could provide a novel treatment approach in breast cancer.
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Registered trials
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