Role of transmembrane proteins in malignant tumors

doi:10.3760/cma.j.cn371439-20191227-00035

Abstract

Abstract:

Transmembrane proteins (TMEMs) are a class of membrane proteins, also known as integral membrane proteins, that contain at least one transmembrane structure. A variety of membrane protein function has been found closely related to the proliferation, invasion and metastasis of malignant tumors: TMEM48, TMEM45A/B, TMEM14A, TMEM158 and TMEM206 have tumor promoting effects; TMEM25 and TMEM7 have antitumor effects; TMEM16A, TMEM17, TMEM97, TMEM88 and TMEM176 play heterogeneity roles in different tumors. These TMEMs can be used as potential prognostic indicators and new therapeutic targets.

Key words: Neoplasms, Transmembrane proteins

Miao Qiuju, Xu Xiulian. Role of transmembrane proteins in malignant tumors[J]. Journal of International Oncology, 2020, 47(6): 355-359.

References 47

[1]	Du Z, Lovly CM. Mechanisms of receptor tyrosine kinase activation in cancer[J]. Mol Cancer, 2018,17(1):58. DOI: 10.1186/s12943-018-0782-4. doi: 10.1186/s12943-018-0782-4 pmid: 29455648
[2]	Rodriguez-Bravo V, Pippa R, Song WM, et al. Nuclear pores promote lethal prostate cancer by increasing POM121-driven E2F1, MYC, and AR nuclear import[J]. Cell, 2018,174(5):174-1215.e1220.DOI: 10.1016/j.cell.2018.07.015.
[3]	Qiao W, Han Y, Jin W, et al. Overexpression and biological function of TMEM48 in non-small cell lung carcinoma[J]. Tumour Biol, 2016,37(2):2575-2586. DOI: 10.1007/s13277-015-4014-x. doi: 10.1007/s13277-015-4014-x pmid: 26392108
[4]	Zhu M, Jiang B, Yan D, et al. Knockdown of TMEM45A overcomes multidrug resistance and epithelial-mesenchymal transition in human colorectal cancer cells through inhibition of TGF-beta signaling pathway[J]. Clin Exp Pharmacol Physiol, 2019,47(3):503-516. DOI: 10.1111/1440-1681.13220. doi: 10.1111/1440-1681.13220 pmid: 31788833
[5]	Guo J, Chen L, Luo N, et al. Inhibition of TMEM45A suppresses proliferation, induces cell cycle arrest and reduces cell invasion in human ovarian cancer cells[J]. Oncol Rep, 2015,33(6):3124-3130. DOI: 10.3892/or.2015.3902. doi: 10.3892/or.2015.3902 pmid: 25872785
[6]	Sun W, Qiu G, Zou Y, et al. Knockdown of TMEM45A inhibits the proliferation, migration and invasion of glioma cells[J]. Int J Clin Exp Pathol, 2015,8(10):12657-12667. pmid: 26722455
[7]	Luo F, Yang K, Wang YZ, et al. TMEM45B is a novel predictive biomarker for prostate cancer progression and metastasis[J]. Neoplasma, 2018,65(5):815-821. DOI: 10.4149/neo_2018_170822N551. doi: 10.4149/neo_2018_170822N551 pmid: 30249106
[8]	Zhao LC, Shen BY, Deng XX, et al. TMEM45B promotes proliferation, invasion and migration and inhibits apoptosis in pancreatic can-cer cells[J]. Mol Biosyst, 2016,12(6):1860-1870. DOI: 10.1039/c6mb00203j. doi: 10.1039/c6mb00203j pmid: 27108650
[9]	Hu R, Hu F, Xie X, et al. TMEM45B, up-regulated in human lung cancer, enhances tumorigenicity of lung cancer cells[J]. Tumour Biol, 2016,37(9):12181-12191. DOI: 10.1007/s13277-016-5063-5. doi: 10.1007/s13277-016-5063-5 pmid: 27225290
[10]	Molina-Pinelo S, Gutiérrez G, Pastor MD, et al. MicroRNA-dependent regulation of transcription in non-small cell lung cancer[J]. PLoS One, 2014,9(3):e90524. DOI: 10.1371/journal.pone.0090524. doi: 10.1371/journal.pone.0090524 pmid: 24625834
[11]	Li Y, Guo W, Liu S, et al. Silencing transmembrane protein 45B (TNEM45B) inhibits proliferation, invasion, and tumorigenesis in osteosarcoma cells[J]. Oncol Res, 2017,25(6):1021-1026. DOI: 10.3727/096504016x14821477992177. doi: 10.3727/096504016X14821477992177 pmid: 28244852
[12]	Shen K, Yu W, Yu Y, et al. Knockdown of TMEM45B inhibits cell proliferation and invasion in gastric cancer[J]. Biomed Pharmaco-ther, 2018,104:576-581. DOI: 10.1016/j.biopha.2018.05.016.
[13]	Zhang Q, Chen X, Zhang X, et al. Knockdown of TMEM14A expression by RNAi inhibits the proliferation and invasion of human ovarian cancer cells[J]. Biosci Rep, 2016,36(1):e00298. DOI: 10.1042/bsr20150258. doi: 10.1042/BSR20150258 pmid: 26896463
[14]	Salim H, Zong D, Hååg P, et al. DKK1 is a potential novel mediator of cisplatin-refractoriness in non-small cell lung cancer cell lines[J]. BMC Cancer, 2015,15:628. DOI: 10.1186/s12885-015-1635-9. doi: 10.1186/s12885-015-1635-9 pmid: 26353782
[15]	Cheng Z, Guo J, Chen L, et al. Overexpression of TMEM158 contributes to ovarian carcinogenesis[J]. J Exp Clin Cancer Res, 2015,34:75. DOI: 10.1186/s13046-015-0193-y. doi: 10.1186/s13046-015-0193-y pmid: 26239324
[16]	Liu L, Zhang J, Li S, et al. Silencing of TMEM158 inhibits tumorigenesis and multidrug resistance in colorectal can-cer[J]. Nutr Cancer, 2019: 1-10. DOI: 10.1080/01635581.2019.1650192. doi: 10.1080/01635581.2020.1783330 pmid: 32586130
[17]	Fu Y, Yao N, Ding D, et al. TMEM158 promotes pancreatic cancer aggressiveness by activation of TGFbeta1 and PI3K/AKT signaling pathway[J]. J Cell Physiol, 2020,235(3):2761-2775. DOI: 10.1002/jcp.29181. doi: 10.1002/jcp.29181 pmid: 31531884
[18]	Yang J, Chen J, Del Carmen Vitery M, et al. PAC, an evolutiona-rily conserved membrane protein, is a proton-activated chloride channel[J]. Science, 2019,364(6438):395-399. DOI: 10.1126/science.aav9739. doi: 10.1126/science.aav9739 pmid: 31023925
[19]	Zhao J, Zhu D, Zhang X, et al. TMEM206 promotes the malignancy of colorectal cancer cells by interacting with AKT and extracellular signal-regulated kinase signaling pathways[J]. J Cell Physiol, 2019,234(7):10888-10898. DOI: 10.1002/jcp.27751. doi: 10.1002/jcp.27751 pmid: 30417481
[20]	Kaliaperumal J, Padarthi P, Elangovan N, et al. Anti-tumorigenic effect of nano formulated peptide pACC1 by diminishing de novo lipogenisis in DMBA induced mammary carcinoma rat model[J]. Biomed Pharmacother, 2014,68(6):763-773. DOI: 10.1016/j.biopha.2014.07.016. doi: 10.1016/j.biopha.2014.07.016
[21]	Doolan P, Clynes M, Kennedy S, et al. TMEM25, REPS2 and Meis 1: favourable prognostic and predictive biomarkers for breast cancer[J]. Tumour Biol, 2009,30(4):200-209. DOI: 10.1159/000239795. doi: 10.1159/000239795 pmid: 19776672
[22]	Hrašovec S, Hauptman N, Glǎvac D, et al. TMEM25 is a candidate biomarker methylated and down-regulated in colorectal cancer [J]. Dis Markers, 2013,34(2):93-104. DOI: 10.3233/dma-120948. doi: 10.3233/DMA-120948
[23]	Zhou X, Popescu NC, Klein G, et al. The interferon-alpha responsive gene TMEM7 suppresses cell proliferation and is downregulated in human hepatocellular carcinoma[J]. Cancer Genet Cytogenet, 2007,177(1):6-15. DOI: 10.1016/j.cancergencyto.2007.04.007. doi: 10.1016/j.cancergencyto.2007.04.007 pmid: 17693185
[24]	Wrzesiński T, Szelag M, Cieślikowski WA, et al. Expression of pre-selected TMEMs with predicted ER localization as potential classi-fiers of ccRCC tumors [J]. BMC Cancer, 2015,15:518. DOI: 10.1186/s12885-015-1530-4. doi: 10.1186/s12885-015-1530-4 pmid: 26169495
[25]	Dang S, Feng S, Tien J, et al. Cryo-EM structures of the TMEM16A calcium-activated chloride channel[J]. Nature, 2017,552(7685):426-429. DOI: 10.1038/nature25024. doi: 10.1038/nature25024 pmid: 29236684
[26]	Ji Q, Guo S, Wang X, et al. Recent advances in TMEM16A: structure, function, and disease[J]. J Cell Physiol, 2019,234(6):7856-7873. DOI: 10.1002/jcp.27865. doi: 10.1002/jcp.27865 pmid: 30515811
[27]	Finegersh A, Kulich S, Guo T, et al. DNA methylation regulates TMEM16A/ANO1 expression through multiple CpG islands in head and neck squamous cell carcinoma[J]. Sci Rep, 2017,7(1):15173. DOI: 10.1038/s41598-017-15634-9. doi: 10.1038/s41598-017-15634-9 pmid: 29123240
[28]	Wang H, Zou L, Ma K, et al. Cell-specific mechanisms of TMEM16A Ca(2+)-activated chloride channel in cancer[J]. Mol Cancer, 2017,16(1):152. DOI: 10.1186/s12943-017-0720-x. doi: 10.1186/s12943-017-0720-x pmid: 28893247
[29]	Crottès D, Jan LY. The multifaceted role of TMEM16A in cancer[J]. Cell Calcium, 2019,82:102050. DOI: 10.1016/j.ceca.2019.06.004. doi: 10.1016/j.ceca.2019.06.004 pmid: 31279157
[30]	Wu H, Wang H, Guan S, et al. Cell-specific regulation of proliferation by Ano1/TMEM16A in breast cancer with different ER, PR, and HER2 status[J]. Oncotarget, 2017,8(49):84996-85013. DOI: 10.18632/oncotarget.18662. doi: 10.18632/oncotarget.18662 pmid: 29156699
[31]	Zhang X, Zhang Y, Miao Y, et al. TMEM17 depresses invasion and metastasis in lung cancer cells via ERK signaling pathway[J]. Oncotarget, 2017,8(41):70685-70694. DOI: 10.18632/oncotarget.19977. doi: 10.18632/oncotarget.19977 pmid: 29050311
[32]	Zhao Y, Song K, Zhang Y, et al. TMEM17 promotes malignant progression of breast cancer via AKT/GSK3β signaling[J]. Cancer Manag Res, 2018,10:2419-2428. DOI: 10.2147/cmar.S168723. doi: 10.2147/CMAR.S168723 pmid: 30122991
[33]	Shan Y, Ding H, Lu J, et al. Pleural MAC30 as a prognostic mar-ker in NSCLC with malignant pleural effusion[J]. Oncotarget, 2017,8(68):112809-112815. DOI: 10.18632/oncotarget.22631. doi: 10.18632/oncotarget.22631 pmid: 29348867
[34]	Qu T, Zhao Y, Chen Y, et al. Down-regulated MAC30 expression inhibits breast cancer cell invasion an31934012d EMT by suppre-ssing Wnt/beta-catenin and PI3K/Akt signaling pathways[J]. Int J Clin Exp Pathol, 2019,12(5):1888-1896. pmid: 31934012
[35]	Kabe Y, Nakane T, Koike I, et al. Haem-dependent dimerization of PGRMC1/Sigma-2 receptor facilitates cancer proliferation and chemoresistance[J]. Nat Commun, 2016,7:11030. DOI: 10.1038/ncomms11030. doi: 10.1038/ncomms11030 pmid: 26988023
[36]	Song GQ, Zhao Y. MAC30 knockdown involved in the activation of the Hippo signaling pathway in breast cancer cells[J]. Biol Chem, 2018,399(11):1305-1311. DOI: 10.1515/hsz-2018-0250. doi: 10.1515/hsz-2018-0250 pmid: 29990302
[37]	Longhitano L, Castracani CC, Tibullo D, et al. Sigma-1 and Sigma-2 receptor ligands induce apoptosis and autophagy but have opposite effect on cell proliferation in uveal melanoma[J]. Oncotarget, 2017,8(53):91099-91111. DOI: 10.18632/oncotarget.19556. doi: 10.18632/oncotarget.19556 pmid: 29207628
[38]	Liu CC, Yu CF, Wang SC, et al. Sigma-2 receptor/TMEM97 agonist PB221 as an alternative drug for brain tumor[J]. BMC Cancer, 2019,19(1):473. DOI: 10.1186/s12885-019-5700-7. doi: 10.1186/s12885-019-5700-7 pmid: 31109310
[39]	Huang YS, Lu HL, Zhang LJ, et al. Sigma-2 receptor ligands and their perspectives in cancer diagnosis and therapy[J]. Med Res Rev, 2014,34(3):532-566. DOI: 10.1002/med.21297. doi: 10.1002/med.21297 pmid: 23922215
[40]	Ge YX, Wang CH, Hu FY, et al. New advances of TMEM88 in cancer initiation and progression, with special emphasis on Wnt signaling pathway[J]. J Cell Physiol, 2018,233(1):79-87. DOI: 10.1002/jcp.25853. doi: 10.1002/jcp.25853 pmid: 28181235
[41]	Yu X, Zhang X, Zhang Y, et al. Cytosolic TMEM88 promotes triple-negative breast cancer by interacting with Dvl[J]. Oncotarget, 2015,6(28):25034-25045. DOI: 10.18632/oncotarget.4379. doi: 10.18632/oncotarget.4379 pmid: 26325443
[42]	de Leon M, Cardenas H, Vieth E, et al. Transmembrane protein 88 (TMEM88) promoter hypomethylation is associated with platinum resistance in ovarian cancer[J]. Gynecol Oncol, 2016,142(3):539-547. DOI: 10.1016/j.ygyno.2016.06.017. doi: 10.1016/j.ygyno.2016.06.017 pmid: 27374141
[43]	Zhang X, Wan JX, Ke ZP, et al. TMEM88, CCL14 and CLEC3B as prognostic biomarkers for prognosis and palindromia of human hepatocellular carcinoma[J]. Tumour Biol, 2017,39(7):1010428317708900. DOI: 10.1177/1010428317708900. doi: 10.1177/1010428317708900 pmid: 28718365
[44]	Liu Z, An H, Song P, et al. Potential targets of TMEM176A in the growth of glioblastoma cells[J]. Onco Targets Ther, 2018,11:7763-7775. DOI: 10.2147/ott.S179725. doi: 10.2147/OTT.S179725 pmid: 30464524
[45]	Li H, Zhang M, Linghu E, et al. Epigenetic silencing of TMEM176A activates ERK signaling in human hepatocellular carcinoma[J]. Clin Epigenetics, 2018,10(1):137. DOI: 10.1186/s13148-018-0570-4. doi: 10.1186/s13148-018-0570-4 pmid: 30400968
[46]	Cuajungco MP, Podevin W, Valluri VK, et al. Abnormal accumulation of human transmembrane (TMEM)-176A and 176B proteins is associated with cancer pathology[J]. Acta Histochem, 2012,114(7):705-712. DOI: 10.1016/j.acthis.2011.12.006. doi: 10.1016/j.acthis.2011.12.006
[47]	Segovia M, Russo S, Jeldres M, et al. Targeting TMEM176B enhances antitumor immunity and augments the efficacy of immune checkpoint blockers by unleashing inflammasome activation[J]. Cancer Cell, 2019, 35(5):767-781.DOI: 10.1016/j.ccell.2019.04.003. doi: 10.1016/j.ccell.2019.04.003 pmid: 31085177