Cited by 115Protein Degradation and InhibitorsChemical Synthesis and AnalysisUbiquitin and proteasome pathways

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Peptide-based PROTAC degrader of FOXM1 suppresses cancer and decreases GLUT1 and PD-L1 expression

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Wang, Kun, Dai, Xiaoyong, Yu, Albert, Feng, Chunyan, Liu, Kewei, Huang, Laiqiang·2022·Journal of Experimental & Clinical Cancer Research

DOI 10.1186/s13046-022-02483-2PMC PMC9520815

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Abstract

Background: Peptide proteolysis-targeting chimeras (p-PROTACs) with advantages of high specificity and low toxicity have emerged as a powerful technology of targeted protein degradation for biomedical applications. FOXM1, a proliferation-associated transcription factor, is overexpressed in a variety of human tumors as a key driver of tumorigenesis and cancer progression, and is a potential anticancer therapeutic target. However, FOXM1-targeting p-PROTACs has not been researched. Methods: Here, we first analyzed the expression of FOXM1, GLUT1 and PD-L1 in liver cancer through database and clinical samples of patients. FOXM1-targeting peptides, selected by screening phage display library, are verified its targeting effect by immunofluorescence and CCK-8 test. The novel p-PROTAC degrader of FOXM1 is chemically synthesis, named FOXM1-PROTAC, by linking a FOXM1-binding antagonistic peptide, with the E3 ubiquitin ligase recruitment ligand Pomalidomide and with the cell membrane penetrating peptide TAT. Its degradation effect on FOXM1 was detected by Western blotting, qPCR, and we verified its effect on the behavior of cancer cells by flow cytometry, scratch assay, and Transwell in vitro. The tumor xenografted mice model was used for evaluating FOXM1-PROTAC therapeutic response in vivo. Finally, we detected the expression of GLUT1 and PD-L1 after FOXM1-PROTAC degraded FOXM1 by using Western Blotting and hippocampal detectors and dual immunofluorescence. Results: We found that the novel FOXM1-PROTAC efficiently entered cells and induced degradation of FOXM1 protein, which strongly inhibits viability as well as migration and invasion in various cancer cell lines, and suppressed tumor growth in HepG2 and MDA-MB-231 cells xenograft mouse models, without detected toxicity in normal tissues. Meanwhile, FOXM1-PROTAC decreased the cancer cells glucose metabolism via downregulating the protein expression levels of glucose transporter GLUT1 and the immune checkpoint PD-L1, which suggests involvement of FOXM1 in cancer cell metabolism and immune regulation. Conclusions: Our results indicate that biologically targeted degradation of FOXM1 is an attractive therapeutic strategy, and antagonist peptide-containing FOXM1-PROTACs as both degrader and inhibitor of FOXM1 could be developed as a safe and promising drug for FOXM1-overexpressed cancer therapy.

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Fig. 1 High expression of FOXM1 in cancers is closely correlated with poor prognosis, and with the expression of GLUT1 and PD-L1. A Expression of FOXM1 in hepatocellular carcinoma samples. B Relationship between FOXM1 expression and prognosis in hepatocellular carcinoma. C Correlation between GLUT1 and PD-L1 expression in hepatocellular carcinoma. D Expression of GLUT1 in hepatocellular carcinoma samples. E Expression of PD-L1 in hepatocellular carcinoma samples. F Detection of FOXM1 protein expression in different cancer cell linesCC BY · PubMed Central

Fig. 2 FIP-1 binds to FOXM1 and inhibits viability of cancer cells. A Screening and identification of FOXM1 targeted peptides using an in vitro phage display. B Name and sequence of FOXM1 targeted peptides. C Effect of three rounds of screening peptides was verified by CCK8 in HepG2 cells. D Peptides were renamed after labeling the TAT sequence at the C-terminal. E Viability of cells, treated with three screened peptides for 24 h, were performed using CCK-8, and the results showed that FIP-1 inhibited the growth of HepG2 cells. F Localization of FOXM1 (red) and FITC-labeled FIP-1 (green) was imaged with fluorescent Con-focal microscopy. Cell nuclei was stained by DAPI (blue). Lift: F-1, Right: FIP-1. G The level of cellular uptake was quantified with flow cytometryCC BY · PubMed Central

Fig. 3 FOXM1-PROTAC induces FOXM1 protein degradation. A Structure of FOXM1-PROTAC. B Viability of cells, treated with FIP-1 and FOXM1-PROTAC for 24 h, were performed using CCK-8, and the results showed that FOXM1-PROTAC has a better inhibitory effect on cells. C, Western blotting examination for FOXM1 of HepG2 cells treated with 20 μM FOXM1-PROTAC for different time (0, 3, 6, 12, 24, 48 h). D Western blotting test for FOXM1 of HepG2 cells treated for 24 h with increasing concentrations of FOXM1-PROTAC (0, 2, 5, 10, 20, 30, 50 μM). E Expression of FOXM1 in HepG2 and MDA-MB-231 cells treated with 20 μM FDI-6, FIP-1 and FOXM1-PROTAC for 24 h. F Detection of FOXM1 mRNA by Real-time PCR in HepG2 and MDA-MB-231 cells treated with 20 μM FOXM1-PROTAC for 24 h. G HepG2, A549, MDA-MB-231, HCT116 cells viability, treated with 20 μM FOXM1-PROTAC for 24 h respectively, were performed using CCK-8CC BY · PubMed Central

Fig. 4 FOXM1-PROTAC inhibits proliferation, migration and invasion of cancer cells. A Analysis for DNA content of HepG2 and MDA-MB-231 cells on a Flow cytometer, treated with FIP-1 and FOXM1-PROTAC for 24 h and stained with propidium iodide. B Scratch assay of HepG2 and MDA-MB-231 cells, which were treated with FIP-1 and FOXM1-PROTAC for 24 h. C Colony formation results and analysis of HepG2 and MDA-MB-231 cells, which were treated with FIP-1 and FOXM1-PROTAC for 24 h and cultured for 14 days. D Transwell experiment and Statistical histogram, which reflects different invasion ability of HepG2 and MDA-MB-231 cells treated with FIP-1 and FOXM1-PROTAC for 24 h. E Examination of E-cadherin, N-cadherin and Vimentin level of HepG2 and MDA-MB-231 cells, treated with FIP-1 and FOXM1-PROTAC for 48 hCC BY · PubMed Central

Fig. 5 FOXM1-PROTAC suppresses tumor growth in vivo. A The protocol of FOXM1-PROTAC treatment in vivo. BALB/c nude mice (n = 21) were subcutaneously (S.C.) injected with HepG2 and MDA-MB-231 cells (106 cells/mouse) into the right axilla. When the tumor volumes reached 50–100 mm3, the mice were randomly divided into three group. FIP-1 or FOXM1-PROTAC (20 mg/kg) was injected directly into tumors (caudal vein injection) once a day for 14 days. The size of engrafted tumors was measured at the interval of two days and tumor samples were collected at Day 28 post the injection of cancer cells. B Changes of tumor volume with administration days in mice injecting with HepG2 cells. C Hepatoma tumor picture after 28 days. D Breast tumor picture after 28 days. E Statistical diagram of tumor volume of mice injected with HepG2 cells in experimental group and control group. F Changes of body weight of mice injected with HepG2 cells. G, Immunohistochemistry of Heart, Liver, Spleen, Lung and Kidney Treated by FIP-1 and FOXM1-PROTAC for 14 Days (20 mg/kg). H, Serum ELISA of xenografted mice treated by FIP-1 and FOXM1-PROTACs (20 mg/Kg). I, ELISA of Heart, Liver, Spleen, Lung and Kidney treated by FIP-1 and FOXM1-PROTACs (20 mg/kg)CC BY · PubMed Central

Fig. 6 FOXM1-PROTAC inhibits the expression of GLUT1 and PD-L1. A Detection of PD-L1, GLUT1 in HepG2 cells treated with FIP-1 and FOXM1-PROTAC for 24 h. B Decreasing lactate level in HepG2 cells, treated with FIP-1 and FOXM1-PROTAC for 24 h, was showed by Microplate Reader. C, Seahorse extracellular flux analyzer (SEFA) measurement of ECAR metabolic profile in HepG2 cells treated with FIP-1 and FOXM1-PROTAC for 24 h. D Expression of PD-L1 in HepG2 cells after treating with 2-DG for 24 h. E HepG2 cells treated with FIP-1 and FOXM1-PROTAC for 24 h uptake analysis of 2-NBDG (200 μM) on a Flow cytometer. F Flow cytometer analysis of PD-L1 expression on tumor cell surface before or after FOXM1-PROTACs treatment. G Immunofluorescence of tumor samples, FOXM1 (red single), GLUT1 and PD-L1 (red and green merged), ki-67 (green single) and Cell nuclei was stained (blue)CC BY · PubMed Central

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Authors: Wang, K., Dai, X., Yu, A., Feng, C., Liu, K., & Huang, L.
Affiliations: Tsinghua–Berkeley Shenzhen Institute (CN)
Corresponding author: Huang, Laiqiang
ORCID: Wang, Kun
Dai, Xiaoyong
Liu, Kewei
Huang, Laiqiang
Venue: Journal of Experimental & Clinical Cancer Research
Publisher: Springer Science and Business Media LLC
Published: 2022-09-29
Volume: 41
Issue: 1
Pages: 289-289
ISSN: 0392-9078 (ISSN-L)
1756-9966
DOI: 10.1186/s13046-022-02483-2
PMC: PMC9520815
OpenAlex: W4297521487
Cited by: 115
References: 46
Citations by year: 2026: 28 · 2025: 40 · 2024: 26 · 2023: 19 · 2022: 2
FWCI: 7.10
Type: journal article
Language: en
Open access: gold
doi.org
Licence: cc-by
creativecommons.org/licenses/by/4.0 (tdm)
creativecommons.org/licenses/by/4.0 (vor)
Locations: Journal of Experimental & Clinical Cancer Research (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders: National Natural Science Foundation of China (81872368, 81641051)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Keywords: FOXM1, targeted protein degradation, GLUT1, PD-L1, glucose metabolism, cancer immunotherapy, liver cancer, breast cancer, tumor xenografts, pomalidomide, TAT peptide, tumor cell migration and invasion, tumor cell proliferation
MeSH terms: Forkhead Box Protein M1, Animals, Glucose, Humans, Ligands, Neoplasms, Ubiquitin-Protein Ligases, Glucose Transporter Type 1, Mice, Cell-Penetrating Peptides, Proteolysis, B7-H1 Antigen

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Peptide-based PROTAC degrader of FOXM1 suppresses cancer and decreases GLUT1 and PD-L1 expression

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