Generic placeholder image

Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Research Article

Gelsolin Inhibits the Proliferation of Colon Cancer Cells by Enhancing the Expression of TNFR2/CASP10 as a Death Receptor Pathway

Author(s): Zihang Wang and Wuqi Song*

Volume 30, Issue 3, 2023

Published on: 03 February, 2023

Page: [214 - 220] Pages: 7

DOI: 10.2174/0929866530666230124113639

Price: $65

Abstract

Background: Colon cancer has the second highest incidence rate of digestive system tumors. It relies on surgical treatment, radiotherapy and chemotherapy, and targeted drug therapy.

Objective: To study the mechanism of GSN in the proliferation of colon cancer cells.

Materials and Methods: The expression of gelsolin (GSN) was analyzed with the data of colon cancer patients in the TCGA database. SW620 cells were treated by GSN in vitro and the gene expression was detected by immunoblotting and quantitative PCR.

Results: The expression of GSN was found significantly low in colon cancer cells and correlated with the prognosis of patients. The SW620 cell line cultured in vitro was treated with exogenous GSN. SW620 can be significantly inhibited above the concentration of 250 μg/ml. The results of immunoblotting and quantitative PCR showed that exogenous GSN can effectively improve the transcription level of death receptor-related pathway genes such as TNFR2 and CASP10.

Conclusion: This study found that GSN inhibited the proliferation of SW620 cells in vitro by upregulating the expression of death receptor pathway-related proteins.

Graphical Abstract

[1]
Sun, Y.; Cao, Z.; Shan, J.; Gao, Y.; Liu, X.; Ma, D.; Li, Z. Hsa_circ_0020095 promotes oncogenesis and cisplatin resistance in colon cancer by sponging mir-487a-3p and modulating SOX9. Front. Cell Dev. Biol., 2021, 8, 604869.
[http://dx.doi.org/10.3389/fcell.2020.604869] [PMID: 33520987]
[2]
Noreen, F.; Chaber-Ciopinska, A.; Regula, J.; Schär, P.; Truninger, K. Longitudinal analysis of healthy colon establishes aspirin as a suppressor of cancer-related epigenetic aging. Clin. Epigenetics, 2020, 12(1), 164.
[http://dx.doi.org/10.1186/s13148-020-00956-9] [PMID: 33143725]
[3]
Fukuoka, H.; Fukunaga, Y.; Nagasaki, T.; Akiyoshi, T.; Konishi, T.; Nagayama, S.; Ueno, M. Lymph node mapping in transverse colon cancer treated using laparoscopic colectomy with D3 lymph node dissection. Dis. Colon Rectum, 2022, 65(3), 340-352.
[http://dx.doi.org/10.1097/DCR.0000000000002108] [PMID: 35138285]
[4]
Ren, D.; Wang, W.L.; Wang, G.; Chen, W.W.; Li, X.K.; Li, G.D.; Bai, S.X.; Dong, H.M.; Chen, W.H. Development and internal validation of a nomogram-based model to predict three-year and five-year overall survival in patients with stage II/III colon cancer. Cancer Manag. Res., 2022, 14, 225-236.
[http://dx.doi.org/10.2147/CMAR.S335665] [PMID: 35058717]
[5]
Li, G.H.; Arora, P.D.; Chen, Y.; McCulloch, C.A.; Liu, P. Multifunctional roles of gelsolin in health and diseases. Med. Res. Rev., 2012, 32(5), 999-1025.
[http://dx.doi.org/10.1002/med.20231] [PMID: 22886630]
[6]
Strudwick, X.L.; Cowin, A.J. Multifunctional roles of the actin-binding protein flightless I in inflammation, cancer and wound healing. Front. Cell Dev. Biol., 2020, 8, 603508.
[http://dx.doi.org/10.3389/fcell.2020.603508] [PMID: 33330501]
[7]
Lee, H.J.; Kim, M.J.; Kim, Y.S.; Choi, M.Y.; Cho, G.J.; Choi, W.S. UHRF1 silences gelsolin to inhibit cell death in early stage cervical cancer. Biochem. Biophys. Res. Commun., 2020, 526(4), 1061-1068.
[http://dx.doi.org/10.1016/j.bbrc.2020.03.185] [PMID: 32312517]
[8]
Chen, Z.; Li, K.; Yin, X.; Li, H.; Li, Y.; Zhang, Q.; Wang, H.; Qiu, Y. Lower expression of gelsolin in colon cancer and its diagnostic value in colon cancer patients. J. Cancer, 2019, 10(5), 1288-1296.
[http://dx.doi.org/10.7150/jca.28529] [PMID: 30854138]
[9]
Kim, H.L.; Seligson, D.; Liu, X.; Janzen, N.; Bui, M.H.T.; Yu, H.; Shi, T.; Figlin, R.A.; Horvath, S.; Belldegrun, A.S. Using protein expressions to predict survival in clear cell renal carcinoma. Clin. Cancer Res., 2004, 10(16), 5464-5471.
[http://dx.doi.org/10.1158/1078-0432.CCR-04-0488] [PMID: 15328185]
[10]
Ansari, D.; Aronsson, L.; Sasor, A.; Welinder, C.; Rezeli, M.; Marko-Varga, G.; Andersson, R. The role of quantitative mass spectrometry in the discovery of pancreatic cancer biomarkers for translational science. J. Transl. Med., 2014, 12(1), 87.
[http://dx.doi.org/10.1186/1479-5876-12-87] [PMID: 24708694]
[11]
Tsai, T.J.; Lim, Y.P.; Chao, W.Y.; Chen, C.C.; Chen, Y.J.; Lin, C.Y.; Lee, Y.R. Capping actin protein overexpression in human colorectal carcinoma and its contributed tumor migration. Anal. Cell. Pathol. , 2018, 2018, 8623937.
[http://dx.doi.org/10.1155/2018/8623937] [PMID: 30155403]
[12]
Guo, Y.; Zhang, H.; Xing, X.; Wang, L.; Zhang, J.; Yan, L.; Zheng, X.; Zhang, M. Gelsolin regulates proliferation, apoptosis and invasion in natural killer/T-cell lymphoma cells. Biol. Open, 2018, 7(1), bio027557.
[PMID: 29175858]
[13]
Chaponnier, C.; Kocher, O.; Gabbiani, G. Modulation of gelsolin content in rat aortic smooth muscle cells during development, experimental intimal thickening and culture. An immunohisto-chemical and biochemical study. Eur. J. Biochem., 1990, 190(3), 559-565.
[http://dx.doi.org/10.1111/j.1432-1033.1990.tb15610.x] [PMID: 2164930]
[14]
Scholz, A.; Hinssen, H. Biphasic pattern of gelsolin expression and variations in gelsolin-actin interactions during myogenesis. Exp. Cell Res., 1995, 219(2), 384-391.
[http://dx.doi.org/10.1006/excr.1995.1243] [PMID: 7641789]
[15]
Kwiatkowski, D.J. Predominant induction of gelsolin and actin-binding protein during myeloid differentiation. J. Biol. Chem., 1988, 263(27), 13857-13862.
[http://dx.doi.org/10.1016/S0021-9258(18)68322-X] [PMID: 2843540]
[16]
Paunio, T.; Kangas, H.; Kiuru, S.; Palo, J.; Peltonen, L.; Syvänen, A.C. Tissue distribution and levels of gelsolin mRNA in normal individuals and patients with gelsolin-related amyloidosis. FEBS Lett., 1997, 406(1-2), 49-55.
[http://dx.doi.org/10.1016/S0014-5793(97)00237-8] [PMID: 9109384]
[17]
Ahn, J.S.; Jang, I.S.; Kim, D.I.; Cho, K.A.; Park, Y.H.; Kim, K.; Kwak, C.S.; Chul Park, S. Aging-associated increase of gelsolin for apoptosis resistance. Biochem. Biophys. Res. Commun., 2003, 312(4), 1335-1341.
[http://dx.doi.org/10.1016/j.bbrc.2003.11.061] [PMID: 14652020]
[18]
Lee, P.S.; Sampath, K.; Karumanchi, S.A.; Tamez, H.; Bhan, I.; Isakova, T.; Gutierrez, O.M.; Wolf, M.; Chang, Y.; Stossel, T.P.; Thadhani, R. Plasma gelsolin and circulating actin correlate with hemodialysis mortality. J. Am. Soc. Nephrol., 2009, 20(5), 1140-1148.
[http://dx.doi.org/10.1681/ASN.2008091008] [PMID: 19389844]
[19]
Wang, H.; Cheng, B.; Chen, Q.; Wu, S.; Lv, C.; Xie, G.; Jin, Y.; Fang, X. Time course of plasma gelsolin concentrations during severe sepsis in critically ill surgical patients. Crit. Care, 2008, 12(4), R106.
[http://dx.doi.org/10.1186/cc6988] [PMID: 18706105]
[20]
Zheng, T.; Wang, A.; Hu, D.; Wang, Y. Molecular mechanisms of breast cancer metastasis by gene expression profile analysis. Mol. Med. Rep., 2017, 16(4), 4671-4677.
[http://dx.doi.org/10.3892/mmr.2017.7157] [PMID: 28791367]
[21]
Yang, J.L.; Wang, C.C.N.; Cai, J.H.; Chou, C.Y.; Lin, Y.C.; Hung, C.C. Identification of GSN and LAMC2 as key prognostic genes of bladder cancer by integrated bioinformatics analysis. Cancers , 2020, 12(7), 1809.
[http://dx.doi.org/10.3390/cancers12071809] [PMID: 32640634]
[22]
Chen, C.C.; Chiou, S.H.; Yang, C.L.; Chow, K.C.; Lin, T.Y.; Chang, H.W.; You, W.C.; Huang, H.W.; Chen, C.M.; Chen, N.C.; Chou, F.P.; Chou, M.C. Secreted gelsolin desensitizes and induces apoptosis of infiltrated lymphocytes in prostate cancer. Oncotarget, 2017, 8(44), 77152-77167.
[http://dx.doi.org/10.18632/oncotarget.20414] [PMID: 29100377]
[23]
Huang, B.; Deng, S.; Loo, S.Y.; Datta, A.; Yap, Y.L.; Yan, B.; Ooi, C.H.; Dinh, T.D.; Zhuo, J.; Tochhawng, L.; Gopinadhan, S.; Jegadeesan, T.; Tan, P.; Salto-Tellez, M.; Yong, W.P.; Soong, R.; Yeoh, K.G.; Goh, Y.C.; Lobie, P.E.; Yang, H.; Kumar, A.P.; Maciver, S.K.; So, J.B.Y.; Yap, C.T. Gelsolin-mediated activation of PI3K/Akt pathway is crucial for hepatocyte growth factor-induced cell scattering in gastric carcinoma. Oncotarget, 2016, 7(18), 25391-25407.
[http://dx.doi.org/10.18632/oncotarget.8603] [PMID: 27058427]
[24]
Ke, H.; Zhang, J.Y.; Akiyama, S.K.; French, J.E. BCL2 interaction with actin in vitro may inhibit cell motility by enhancing actin polymerization. Cell Adhes. Migr., 2011, 5(1), 6-10.
[http://dx.doi.org/10.4161/cam.5.1.13175] [PMID: 20716950]
[25]
Bohgaki, M.; Matsumoto, M.; Atsumi, T.; Kondo, T.; Yasuda, S.; Horita, T.; Nakayama, K.I.; Okumura, F.; Hatakeyama, S.; Koike, T. Plasma gelsolin facilitates interaction between β2 glycoprotein I and α5β1 integrin. J. Cell. Mol. Med., 2011, 15(1), 141-151.
[http://dx.doi.org/10.1111/j.1582-4934.2009.00940.x] [PMID: 19840195]
[26]
Li, W.X.; Yang, M.X.; Hong, X.Q.; Dong, T.G.; Yi, T.; Lin, S.L.; Qin, X.Y.; Niu, W.X. Overexpression of gelsolin reduces the proliferation and invasion of colon carcinoma cells. Mol. Med. Rep., 2016, 14(4), 3059-3065.
[http://dx.doi.org/10.3892/mmr.2016.5652] [PMID: 27573444]
[27]
Furuya, K.; Yamamoto, N.; Ohyabu, Y.; Morikyu, T.; Ishige, H.; Albers, M.; Endo, Y. Mechanism of the tissue-specific action of the selective androgen receptor modulator S-101479. Biol. Pharm. Bull., 2013, 36(3), 442-451.
[http://dx.doi.org/10.1248/bpb.b12-00885] [PMID: 23449329]
[28]
Tang, Z.; Li, C.; Kang, B.; Gao, G.; Li, C.; Zhang, Z. GEPIA: A web server for cancer and normal gene expression profiling and interactive analyses. Nucleic Acids Res., 2017, 45(W1), W98-W102.
[http://dx.doi.org/10.1093/nar/gkx247] [PMID: 28407145]
[29]
Moriwaki, K.; Chan, F.K.M.; Miyoshi, E. Sweet modification and regulation of death receptor signalling pathway. J. Biochem., 2021, 169(6), 643-652.
[http://dx.doi.org/10.1093/jb/mvab034] [PMID: 33752241]

Rights & Permissions Print Cite
© 2024 Bentham Science Publishers | Privacy Policy