Welcome to JOURNAL OF SICHUAN UNIVERSITY (MEDICAL SCIENCE EDITION)
Volume 51 Issue 6
Nov.  2020
Turn off MathJax
Article Contents
CHEN Hong-li, CUI Bo-miao, KANG Ying-zhu, et al. Expression Level of Protein Kinase D in Oral Squamous Cell Carcinoma with Diverse Differentiation[J]. JOURNAL OF SICHUAN UNIVERSITY (MEDICAL SCIENCE EDITION), 2020, 51(6): 755-759. doi: 10.12182/20201160505
Citation: CHEN Hong-li, CUI Bo-miao, KANG Ying-zhu, et al. Expression Level of Protein Kinase D in Oral Squamous Cell Carcinoma with Diverse Differentiation[J]. JOURNAL OF SICHUAN UNIVERSITY (MEDICAL SCIENCE EDITION), 2020, 51(6): 755-759. doi: 10.12182/20201160505

Expression Level of Protein Kinase D in Oral Squamous Cell Carcinoma with Diverse Differentiation

doi: 10.12182/20201160505
More Information
  • Corresponding author: E-mail: cj123@163.com
  • Received Date: 2019-11-14
  • Rev Recd Date: 2020-05-22
  • Publish Date: 2020-11-20
  •   Objective  This study aimed to investigate the expression level of protein kinase D (PKD) in oral squamous cell carcinoma (OSCC) and its relationship with differentiation of OSCC.  Methods  Sample was collected from 10 healthy control subjects and 40 OSCC confirmed by histopathological diagnosis, and the immunohistochemical staining was adopted to detect the expression of PKDs in OSCC tissues. The proportion of stained cell and staining intensity were evaluated to get a score, which used to analyze the difference among PKD1, PKD2 and PKD3 in various differentiation OSCC tissues. The correlations between the staining score of PKDs and differentiation of OSCC were further analyzed.  Results  PKD1 and PKD3 were high expression in OSCC tissues. There were statistical significance among the staining score of PKD1, PKD2 and PKD3 in various differentiation OSCC tissues (P<0.001). In addition, there was a significantly negative correlation between the staining score of PKD1 and PKD2 with the differentiation of OSCC (r=−0.574, −0.341, P<0.001).  Conclusion  In OSCC tissues with different degree of differentiation, there might be some differences among PKDs which play a major role. The expression of PKD1 and PKD2 was correlated with the differentiation of OSCC, the poor differentiation of OSCC, the higher expression of PKD1 and PKD2.
  • loading
  • [1]
    桂心伟, 姚小武, 陈仕生, 等. NF-κB在口腔鳞状细胞癌及癌旁组织中的表达意义. 口腔疾病防治,2019,27(6): 360–363.
    [2]
    TANG D, TAO D, FANG Y, et al. TNF-alpha promotes invasion and metastasis via NF-Kappa B pathway in oral squamous cell carcinoma. Med Sci Monit Basic Res,2017,23: 141–149. doi: 10.12659/MSMBR.903910
    [3]
    WANG P, LIU J, SONG Y, et al. Screening of immunosuppressive factors for biomarkers of breast cancer malignancy phenotypes and subtype-specific targeted therapy. Peer J,2019,7: e7197[2019-09-21].https://doi.org/10.7717/peerj.7197. doi: 10.7717/peerj.7197
    [4]
    WANG X, BAI Y, HAN Y, et al. Downregulation of GBAS regulates oral squamous cell carcinoma proliferation and apoptosis via the p53 signaling pathway. Onco Targets Ther,2019,12: 3729–3742. doi: 10.2147/OTT.S207930
    [5]
    ASHE S, YADAV S. Maintenance of rhodopsin levels in drosophila photoreceptor and phototransduction requires protein kinase D. Fly(Austin),2018,12(3/4): 164–173.
    [6]
    BORGES S, PEREZ E A, THOMPSON E A, et al. Effective targeting of estrogen receptor-negative breast cancers with the protein kinase D inhibitor CRT006610111306. Mol Cancer Ther,2015,14(6): 1306–1316. doi: 10.1158/1535-7163.MCT-14-0945
    [7]
    余宇, 卢婉鹭, 陈娇, 等. 蛋白激酶D1沉默可降低人涎腺腺样囊性癌细胞ACC-2对紫杉醇的敏感度. 肿瘤防治研究,2016,43(6): 448–452. doi: 10.3971/j.issn.1000-8578.2016.06.003
    [8]
    XU X H, JIN T. The novel functions of the PLC/PKC/PKD signaling axis in G protein-coupled receptor-mediated chemotaxis of neutrophils. J Immunol Res,2015,2015: 817604[2019-12-13]. https://doi.org/10.1155/2015/817604. doi: 10.1155/2015/817604
    [9]
    WANG Q J. PKD at the crossroads of DAG and PKC signaling. Trends Pharmacol Sci,2006,27(6): 317–323. doi: 10.1016/j.tips.2006.04.003
    [10]
    BORGES S, DÖPPLER H, PEREZ E A, et al. Pharmacologic reversion of epigenetic silencing of the PRKD1 promoter blocks breast tumor cell invasion and metastasis. Breast Cancer Res,2013,15(2): R66[2019-12-13]. https://doi.org/10.1186/bcr3460. doi: 10.1186/bcr3460
    [11]
    EISELER T, DÖPPLER H, YAN I K, et al. Protein kinase D1 regulates matrix metalloproteinase expression and inhibits breast cancer cell invasion. Breast Cancer Res,2009,11(1): R13[2019-12-13]. https://doi.org/10.1186/bcr2232. doi: 10.1186/bcr2232
    [12]
    DURAND N, BORGES S, STORZ P. Functional and therapeutic significance of protein kinase D enzymes in invasive breast cancer. Cell Mol Life Sci,2015,72(22): 4369–4382. doi: 10.1007/s00018-015-2011-2
    [13]
    SOLOMON B, YOUNG R J, RISCHIN D. Head and neck squamous cell carcinoma: genomics and emerging biomarkers for immunomodulatory cancer treatments. Semin Cancer Biol,2018,52: 228–240. doi: 10.1016/j.semcancer.2018.01.008
    [14]
    CHI A C, DAY T A, NEVILLE B W. Oral cavity and oropharyngeal squamous cell carcinoma—an update. CA Cancer J Clin,2015,65(5): 401–421. doi: 10.3322/caac.21293
    [15]
    RYKX A, DEKIMPE L, MIKHALAP S, et al. Protein kinase D: a family affair. FEBS Lett,2003,546(1): 81–86. doi: 10.1016/S0014-5793(03)00487-3
    [16]
    ISHIKAWA E, KOSAKO H, YASUDA T, et al. Protein kinase D regulates positive selection of CD4+ thymocytes through phosphorylation of SHP-1. Nat Commun, 2016, 7: 12756[2019-12-13]. https://doi.org/10.1038/ncomms12756.
    [17]
    OLAYIOYE M A, BARISIC S, HAUSSER A. Multi-level control of actin dynamics by protein kinase D. Cell Signal,2013,25(9): 1739–1747. doi: 10.1016/j.cellsig.2013.04.010
    [18]
    DöPPLER H, BASTEA L I, BORGES S, et al. Protein kinase D isoforms differentially modulate cofilin-driven directed cell migration. PLoS One, 2014, 9(5): e98090[2019-09-21]. https://doi.org/10.1371/journal.pone.0098090.
    [19]
    STARUSCHENKO A. To cleave or not to cleave: role of ADAM17 in cell proliferation in PKD. Am J Physiol Renal,2014,307(6): F658–F659. doi: 10.1152/ajprenal.00341.2014
    [20]
    EISLER S A, CURADO F, LINK G, et al. A Rho signaling network links microtubules to PKD controlled carrier transport to focal adhesions. eLife, 2018, 7: e35907[2019-09-21]. https://doi.org/10.7554/eLife.35907.001.
    [21]
    DURAND N, BORGES S, STORZ P. Protein kinase D enzymes as regulators of EMT and cancer cell invasion. J Clin Med,2016,5(2): 20[2019-09-21]. https://doi.org/10.3390/jcm5020020. doi: 10.3390/jcm5020020
    [22]
    XU W, QIAN J, ZENG F, et al. Protein kinase Ds promote tumor angiogenesis through mast cell recruitment and expression of angiogenic factors in prostate cancer microenvironment. J Exp Clin Canc Res,2019,38(1): 114[2019-09-21]. https://doi.org/10.1186/s13046-019-1118-y. doi: 10.1186/s13046-019-1118-y
    [23]
    SUHA S, REY O, ROZENGURT E. Neurotensin induces protein kinase C-dependent protein kinase D activation and DNA synthesis in human pancreatic carcinoma cell line PANC-1. Cancer Res,2002,62(6): 1632–1640.
    [24]
    SHABELNIK M Y, KOVALEVSKA L M, YURCHENKO M Y, et al. Differential expression of PKD1 and PKD2 in gastric cancer and analysis of PKD1 and PKD2 function in the model system. Exp Oncol,2011,33(4): 206–211.
    [25]
    KIM M, JANG H R, KIM J H, et al. Epigenetic inactivation of protein kinase D1 in gastric cancer and its role in gastric cancer cell migration and invasion. Carcinogenesis,2007,29(3): 629–637. doi: 10.1093/carcin/bgm291
    [26]
    CHEN J, DENG F, SINGH S V, et al. Protein kinase D3 (PKD3) contributes to prostate cancer cell growth and survival through a PKC/PKD3 pathway downstream of Akt and ERK 1/2. Cancer Res,2008,68(10): 3844–3853. doi: 10.1158/0008-5472.CAN-07-5156
    [27]
    TANDON M, JOHNSON J, LI Z, et al. New pyrazolopyrimidine inhibitors of protein kinase D as potent anticancer agents for prostate cancer cells. PLoS One, 2013, 8(9): e75601[2019-09-21]. https://doi.org/10.1371/journal.pone.0075601.
    [28]
    LIU Y, WANG Y, YU S, et al. The role and mechanism of CRT0066101 as an effective drug for treatment of triple-negative breast cancer. Cell Physiol Biochem,2019,52(3): 382–396. doi: 10.33594/000000027
    [29]
    LIU Y, LI J, MA Z, et al. Oncogenic functions of protein kinase D2 and D3 in regulating multiple cancer-related pathways in breast cancer. Cancer Med,2019,8(2): 729–741. doi: 10.1002/cam4.1938
    [30]
    ZOU Z, ZENG F, XU W, et al. PKD2 and PKD3 promote prostate cancer cell invasion by modulating NF-kB- and HDAC1-mediated expression and activation of uPA. J Cell Sci,2012,125(20): 4800–4811. doi: 10.1242/jcs.106542
    [31]
    HUCK B, DUSS S, HAUSSER A, et al. Elevated protein kinase D3(PKD3) expression supports proliferation of triple-negative breast cancer cells and contributes to mTORC1-S6K1 pathway activation. J Biol Chem,2014,289(6): 3138–3147. doi: 10.1074/jbc.M113.502633
    [32]
    BASTEA L I, DÖPPLER H, BALOGUN B, et al. Protein kinase D1 maintains the epithelial phenotype by inducing a DNA-bound, inactive SNAI1 transcriptional repressor complex. PLoS One,2012,7(1): e30459[2019-09-21]. https://doi.org/10.1371/journal.pone.0030459. doi: 10.1371/journal.pone.0030459
    [33]
    RYVKIN V, RASHEL M, GADDAPARA T, et al. Opposing growth regulatory roles of protein kinase D isoforms in human keratinocytes. J Biol Chem,2015,290(17): 11199–11208. doi: 10.1074/jbc.M115.643742
    [34]
    MARKLUND U, LIGHTFOOT K, CANTRELL D. Intracellular location and cell context-dependent function of protein kinase D. Immunity,2003,19(4): 491–501. doi: 10.1016/S1074-7613(03)00260-7
  • 加载中

Catalog

    通讯作者: 陈斌, bchen63@163.com
    • 1. 

      沈阳化工大学材料科学与工程学院 沈阳 110142

    1. 本站搜索
    2. 百度学术搜索
    3. 万方数据库搜索
    4. CNKI搜索

    Figures(1)  / Tables(1)

    Article views (1708) PDF downloads(22) Cited by()
    Proportional views
    Related

    /

    DownLoad:  Full-Size Img  PowerPoint
    Return
    Return