Suppression of SCIN inhibits human prostate cancer cell proliferation and induces G0/G1 phase arrest

Wang,Dong; Sun,Shu-Qing; Yu,Ying-Hao; Wu,Wei-Zhen; Yang,Shun-Liang; Tan,Jian-Ming

doi:10.3892/ijo.2013.2170

Suppression of SCIN inhibits human prostate cancer cell proliferation and induces G0/G1 phase arrest

Authors:
- Dong Wang
- Shu-Qing Sun
- Ying-Hao Yu
- Wei-Zhen Wu
- Shun-Liang Yang
- Jian-Ming Tan
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Affiliations: Department of Urology, Fuzhou General Hospital, Fuzhou 350025, P.R. China, Department of Blood Purification, Fuzhou General Hospital, Fuzhou 350025, P.R. China, Department of Pathology, Fuzhou General Hospital, Fuzhou 350025, P.R. China
Published online on: November 8, 2013 https://doi.org/10.3892/ijo.2013.2170
Pages: 161-166

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Abstract

SCIN is a calcium regulated actin severing and capping protein. Its homologue in zebrafish is found to be related with cell death. In the present study, we found that SCIN is highly expressed in human prostate cancer specimens. However, the functions of SCIN in human prostate carcinoma cells are largely unknown. To address the function of SCIN in prostate carcinoma cells, we used lentivirus-mediated RNAi to knock down SCIN expression in PC3 cells, a prostate carcinoma cell line. We found that in vitro silencing of SCIN could inhibit the proliferation and colony formation ability of PC3 cells. Furthermore, cell cycle analysis showed that reduced SCIN expression lead to G0/G1 cell cycle arrest through the regulation of cell cycle-related genes, such as p21Waf1/Cip1, cyclin-dependent kinase inhibitor 2A (CDKN2A, p16Ink4A) and cyclin A2. These results suggest that SCIN plays an important role in the proliferation of prostate cancer cells and lentivirus-mediated inhibition of SCIN expression may be a potential therapeutic method for the treatment of prostate cancer.

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1.	Jemal A, Bray F, Center MM, Ferlay J, Ward E and Forman D: Global cancer statistics. CA Cancer J Clin. 61:69–90. 2011. View Article : Google Scholar
2.	Gronberg H: Prostate cancer epidemiology. Lancet. 361:859–864. 2003. View Article : Google Scholar : PubMed/NCBI
3.	Dong JT, Li CL, Sipe TW and Frierson HF Jr: Mutations of PTEN/MMAC1 in primary prostate cancers from Chinese patients. Clin Cancer Res. 7:304–308. 2001.PubMed/NCBI
4.	Li J, Yen C, Liaw D, et al: PTEN, a putative protein tyrosine phosphatase gene mutated in human brain, breast, and prostate cancer. Science. 275:1943–1947. 1997. View Article : Google Scholar : PubMed/NCBI
5.	Hall A: The cytoskeleton and cancer. Cancer Metastasis Rev. 28:5–14. 2009. View Article : Google Scholar
6.	Bernal SD, Baylin SB, Shaper JH, Gazdar AF and Chen LB: Cytoskeleton-associated proteins of human lung cancer cells. Cancer Res. 43:1798–1808. 1983.PubMed/NCBI
7.	Chang WT, You BJ, Yang WH, Wu CY, Bau DT and Lee HZ: Protein kinase C delta-mediated cytoskeleton remodeling is involved in aloe-emodin-induced photokilling of human lung cancer cells. Anticancer Res. 32:3707–3713. 2012.PubMed/NCBI
8.	Niu J, Mo Q, Wang H, Li M, Cui J and Li Z: Invasion inhibition by a MEK inhibitor correlates with the actin-based cytoskeleton in lung cancer A549 cells. Biochem Biophys Res Commun. 422:80–84. 2012. View Article : Google Scholar : PubMed/NCBI
9.	Chen QY, Xu LQ, Jiao DM, et al: Silencing of Rac1 modifies lung cancer cell migration, invasion and actin cytoskeleton rearrangements and enhances chemosensitivity to antitumor drugs. Int J Mol Med. 28:769–776. 2011.PubMed/NCBI
10.	Chen CH, Lin H, Chuang SM, Lin SY and Chen JJ: Acidic stress facilitates tyrosine phosphorylation of HLJ1 to associate with actin cytoskeleton in lung cancer cells. Exp Cell Res. 316:2910–2921. 2010. View Article : Google Scholar : PubMed/NCBI
11.	Marcu MG, Zhang L, Elzagallaai A and Trifaro JM: Localization by segmental deletion analysis and functional characterization of a third actin-binding site in domain 5 of scinderin. J Biol Chem. 273:3661–3668. 1998. View Article : Google Scholar : PubMed/NCBI
12.	Dumitrescu Pene T, Rose SD, Lejen T, Marcu MG and Trifaro JM: Expression of various scinderin domains in chromaffin cells indicates that this protein acts as a molecular switch in the control of actin filament dynamics and exocytosis. J Neurochem. 92:780–789. 2005.
13.	Trifaro JM, Gasman S and Gutierrez LM: Cytoskeletal control of vesicle transport and exocytosis in chromaffin cells. Acta Physiol (Oxf). 192:165–172. 2008. View Article : Google Scholar : PubMed/NCBI
14.	Nurminsky D, Magee C, Faverman L and Nurminskaya M: Regulation of chondrocyte differentiation by actin-severing protein adseverin. Dev Biol. 302:427–437. 2007. View Article : Google Scholar : PubMed/NCBI
15.	Jia S, Nakaya N and Piatigorsky J: Differential expression patterns and developmental roles of duplicated scinderin-like genes in zebrafish. Dev Dyn. 238:2633–2640. 2009. View Article : Google Scholar : PubMed/NCBI
16.	Zunino R, Li Q, Rose SD, et al: Expression of scinderin in megakaryoblastic leukemia cells induces differentiation, maturation, and apoptosis with release of plateletlike particles and inhibits proliferation and tumorigenesis. Blood. 98:2210–2219. 2001. View Article : Google Scholar
17.	Abouzahr S, Bismuth G, Gaudin C, et al: Identification of target actin content and polymerization status as a mechanism of tumor resistance after cytolytic T lymphocyte pressure. Proc Natl Acad Sci USA. 103:1428–1433. 2006. View Article : Google Scholar : PubMed/NCBI
18.	Franken NA, Rodermond HM, Stap J, Haveman J and van Bree C: Clonogenic assay of cells in vitro. Nat Protoc. 1:2315–2319. 2006. View Article : Google Scholar : PubMed/NCBI
19.	Thorsen K, Schepeler T, Oster B, et al: Tumor-specific usage of alternative transcription start sites in colorectal cancer identified by genome-wide exon array analysis. BMC Genomics. 12:5052011. View Article : Google Scholar : PubMed/NCBI
20.	Miura N, Takemori N, Kikugawa T, Tanji N, Higashiyama S and Yokoyama M: Adseverin: a novel cisplatin-resistant marker in the human bladder cancer cell line HT1376 identified by quantitative proteomic analysis. Mol Oncol. 6:311–322. 2012. View Article : Google Scholar : PubMed/NCBI
21.	Harichand-Herdt S and Ramalingam SS: Gender-associated differences in lung cancer: clinical characteristics and treatment outcomes in women. Semin Oncol. 36:572–580. 2009. View Article : Google Scholar : PubMed/NCBI
22.	Cepeda OA and Gammack JK: Cancer in older men: a gender-based review. Aging Male. 9:149–158. 2006. View Article : Google Scholar : PubMed/NCBI
23.	Reddy C, Chilla D and Boltax J: Lung cancer screening: a review of available data and current guidelines. Hosp Pract (Minneap). 39:107–112. 2011. View Article : Google Scholar : PubMed/NCBI
24.	Bach PB, Mirkin JN, Oliver TK, et al: Benefits and harms of CT screening for lung cancer: a systematic review. JAMA. 307:2418–2429. 2012. View Article : Google Scholar : PubMed/NCBI
25.	Grana X and Reddy EP: Cell cycle control in mammalian cells: role of cyclins, cyclin dependent kinases (CDKs), growth suppressor genes and cyclin-dependent kinase inhibitors (CKIs). Oncogene. 11:211–219. 1995.PubMed/NCBI
26.	Schafer KA: The cell cycle: a review. Vet Pathol. 35:461–478. 1998. View Article : Google Scholar
27.	Molinari M: Cell cycle checkpoints and their inactivation in human cancer. Cell Prolif. 33:261–274. 2000. View Article : Google Scholar : PubMed/NCBI