Asian Pacific Journal of Cancer Prevention

  • 제15권17호
  • /
  • Pages.7245-7249
  • /
  • 2014
  • /
  • 1513-7368(pISSN)
  • /
  • 2476-762X(eISSN)
아시아태평양암예방학회 (Asian Pacific Journal of Cancer Prevention)
권호 표지
DOI QR코드

DOI QR Code

GRP78 Secreted by Colon Cancer Cells Facilitates Cell Proliferation via PI3K/Akt Signaling

  • Fu, Rong (Institute of Biotechnology, Key Laboratory of Chemical Biology and Molecular Engineering of National Ministry of Education, Shaxi University) ;
  • Yang, Peng (Institute of Biotechnology, Key Laboratory of Chemical Biology and Molecular Engineering of National Ministry of Education, Shaxi University) ;
  • Wu, Hai-Li (Institute of Biotechnology, Key Laboratory of Chemical Biology and Molecular Engineering of National Ministry of Education, Shaxi University) ;
  • Li, Zong-Wei (Institute of Biotechnology, Key Laboratory of Chemical Biology and Molecular Engineering of National Ministry of Education, Shaxi University) ;
  • Li, Zhuo-Yu (Institute of Biotechnology, Key Laboratory of Chemical Biology and Molecular Engineering of National Ministry of Education, Shaxi University)
  • 발행 : 2014.09.15
PDF 다운로드
⟨ 이전 논문 다음 논문 ⟩

초록

Glucose regulated protein 78 (GRP78) is usually recognized as a chaperone in the endoplasmic reticulum. However, increasing evidence indicates that GRP78 can be translocated to the cell surface, acting as a signaling receptor for a variety of ligands. Since little is known about the secretion of GRP78 and its role in the progression of colon cancer we here focused on GRP78 from colon cancer cells, and purified GRP78 protein mimicking the secreted GRP78 was able to utilize cell surface GRP78 as its receptor, activating downstream PI3K/Akt and Wnt/${\beta}$-catenin signaling and promote colon cancer cell proliferation. Our study revealed a new mode of action of autocrine GRP78 in cancer progression: secreted GRP78 binds to cell surface GRP78 as its receptor and activates intracellular proliferation signaling.

키워드

참고문헌

  1. Gronow M, Selim MA, Papalas J, et al (2009). GRP78: a multifunctional receptor on the cell surface. Antioxid Redox Signal, 11, 2299-306. https://doi.org/10.1089/ars.2009.2568
  2. Kelber JA, Panopoulos AD, Shani G, et al (2009). Blockade of Cripto binding to cell surface GRP78 inhibits oncogenic Cripto signaling via MAPK/PI3K and Smad2/3 pathways. Oncogene, 28, 2324-36. https://doi.org/10.1038/onc.2009.97
  3. Kern J, Untergasser G, Zenzmaier C, et al (2009). GRP-78 secreted by tumor cells blocks the antiangiogenic activity of bortezomib. Blood, 114, 3960-7. https://doi.org/10.1182/blood-2009-03-209668
  4. Lee AS (2007). GRP78 induction in cancer: therapeutic and prognostic implications. Cancer Res, 67, 3496-9. https://doi.org/10.1158/0008-5472.CAN-07-0325
  5. Li Z, Li Z (2012). Glucose regulated protein 78: a critical link between tumor microenvironment and cancer hallmarks. Biochim Biophys Acta, 1826, 13-22.
  6. Li Z, Zhang L, Zhao Y, et al (2013). Cell-surface GRP78 facilitates colorectal cancer cell migration and invasion. Int J Biochem Cell Biol, 45, 987-94. https://doi.org/10.1016/j.biocel.2013.02.002
  7. Mannoury la Cour C, Salles MJ, Pasteau V, et al (2011). Signaling pathways leading to phosphorylation of Akt and GSK-3beta by activation of cloned human and rat cerebral D (2)and D (3) receptors. Mol Pharmacol, 79, 91-105. https://doi.org/10.1124/mol.110.065409
  8. Misra UK, Deedwania R, Pizzo SV (2006). Activation and cross-talk between Akt, NF-kappaB, and unfolded protein response signaling in 1-LN prostate cancer cells consequent to ligation of cell surface-associated GRP78. J Biol Chem, 281, 13694-707. https://doi.org/10.1074/jbc.M511694200
  9. Misra UK, Mowery Y, Kaczowka S, et al (2009). Ligation of cancer cell surface GRP78 with antibodies directed against its COOH-terminal domain up-regulates p53 activity and promotes apoptosis. Mol Cancer Ther, 8, 1350-62. https://doi.org/10.1158/1535-7163.MCT-08-0990
  10. Misra UK, Pizzo SV (2010a). Ligation of cell surface GRP78 with antibody directed against the COOH-terminal domain of GRP78 suppresses Ras/MAPK and PI 3-kinase/AKT signaling while promoting caspase activation in human prostate cancer cells. Cancer Biol Ther, 9, 142-52. https://doi.org/10.4161/cbt.9.2.10422
  11. Misra UK, Pizzo SV (2010b). Modulation of the unfolded protein response in prostate cancer cells by antibody-directed against the carboxyl-terminal domain of GRP78. Apoptosis, 15, 173-82. https://doi.org/10.1007/s10495-009-0430-y
  12. Pandurangan AK (2013). Potential targets for prevention of colorectal cancer: a focus on PI3K/Akt/mTOR and Wnt pathways. Asian Pac J Cancer Prev, 14, 2201-5. https://doi.org/10.7314/APJCP.2013.14.4.2201
  13. Qi RF, Liu ZX, Xu SQ, et al (2010). Small peptides derived from the Lys active fragment of the mung bean trypsin inhibitor are fully active against trypsin. FEBS J, 277, 224-32. https://doi.org/10.1111/j.1742-4658.2009.07476.x
  14. Rabilloud T, Carpentier G, Tarroux P (1988). Improvement and simplification of low-background silver staining of proteins by using sodium dithionite. Electrophoresis, 9, 288-91. https://doi.org/10.1002/elps.1150090608
  15. Shani G, Fischer WH, Justice NJ, et al (2008). GRP78 and Cripto form a complex at the cell surface and collaborate to inhibit transforming growth factor beta signaling and enhance cell growth. Mol Cell Biol, 28, 666-77. https://doi.org/10.1128/MCB.01716-07
  16. Shevchenko A, Wilm M, Vorm O, et al (1996). Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal Chem, 68, 850-8. https://doi.org/10.1021/ac950914h
  17. Thornton M, Aslam MA, Tweedle EM, et al (2013). The unfolded protein response regulator GRP78 is a novel predictive biomarker in colorectal cancer. Int J Cancer, 133, 1408-18. https://doi.org/10.1002/ijc.28137
  18. Valenta T, Hausmann G, Basler K (2012). The many faces and functions of beta-catenin. EMBO J, 31, 2714-36. https://doi.org/10.1038/emboj.2012.150
  19. Vlashi E, Lagadec C, Vergnes L, et al (2011). Metabolic state of glioma stem cells and nontumorigenic cells. Proc Natl Acad Sci USA, 108, 16062-7. https://doi.org/10.1073/pnas.1106704108
  20. Wang CM, Li SJ, Wu CH, et al (2014). Transient knock down of Grp78 reveals roles in serum ferritin mediated proinflammatory cytokine secretion in rat primary activated hepatic stellate cells. Asian Pac J Cancer Prev, 15, 605-10. https://doi.org/10.7314/APJCP.2014.15.2.605
  21. Xiang KM, Li XR (2014). MiR-133b acts as a tumor suppressor and negatively regulates TBPl1 in colorectal cancer cells. Asian Pac J Cancer Prev, 15, 3767-72. https://doi.org/10.7314/APJCP.2014.15.8.3767
  22. Yue P, Zhang X, Paladino D, et al (2012). Hyperactive EGF receptor, Jaks and Stat3 signaling promote enhanced colonyforming ability, motility and migration of cisplatin-resistant ovarian cancer cells. Oncogene, 31, 2309-22. https://doi.org/10.1038/onc.2011.409
  23. Zheng J, Hu JD, Chen YY, et al (2012). Baicalin induces apoptosis in leukemia HL-60/ADR cells via possible downregulation of the PI3K/Akt signaling pathway. Asian Pac J Cancer Prev, 13, 1119-24. https://doi.org/10.7314/APJCP.2012.13.4.1119
  24. Zhu Q-C, Gao R-Y, Wu W, et al (2013). Epithelial-mesenchymal transition and its role in the pathogenesis of colorectal cancer. Asian Pac J Cancer Prev, 14, 2689-98. https://doi.org/10.7314/APJCP.2013.14.5.2689

피인용 문헌

  1. Derlin-1 is overexpressed in human colon cancer and promotes cancer cell proliferation vol.408, pp.1-2, 2015, https://doi.org/10.1007/s11010-015-2496-x
  2. Glucose-regulated protein 78 contributes to the proliferation and tumorigenesis of human colorectal carcinoma via AKT and ERK pathways vol.36, pp.5, 2016, https://doi.org/10.3892/or.2016.5097
  3. Inhibitory effect of Par-4 combined with cisplatin on human Wilms’ tumor cells vol.39, pp.7, 2017, https://doi.org/10.1177/1010428317716689
  4. GRP78 Impairs Production of Lipopolysaccharide-Induced Cytokines by Interaction with CD14 vol.8, pp.1664-3224, 2017, https://doi.org/10.3389/fimmu.2017.00579
  5. GIV/Girdin promotes cell survival during endoplasmic reticulum stress pp.1573-4919, 2018, https://doi.org/10.1007/s11010-018-3433-6