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  • Cancer Investig br Dumont JA and Bitonti

    2022-04-28

    Cancer Investig 26, 13–21.
    [66] Dumont JA and Bitonti AJ (1994). Modulation of human melanoma cell metastasis and adhesion may involve integrin phosphorylation mediated through protein kinase C. Biochem Biophys Res Commun 204, 264–272.
    [67] Gopalakrishna R and Barsky SH (1988). Tumor promoter-induced membrane-bound protein kinase C regulates hematogenous metastasis. Proc Natl Acad Sci U S A 85, 612–616. 
    [68] Miwa N, Furuse M, Tsukita S, Niikawa N, Nakamura Y, and Furukawa Y (2001). Involvement of claudin-1 in the β-catenin/Tcf signaling pathway and its frequent upregulation in human colorectal cancers. Oncol Res 12, 469–476.
    [69] Awadelkarim KD, Callens C, Rosse C, Susini A, Vacher S, Rouleau E, Lidereau R, and Bieche I (2012). Quantification of PKC family genes in sporadic breast cancer by qRT-PCR: evidence that PKCiota/lambda overexpression is an independent prognostic factor. Int J Cancer 131, 2852–2862. [70] Lonne GK, Cornmark L, Zahirovic IO, Landberg G, Jirstrom K, and Larsson C (2010). PKCalpha Malonyl Coenzyme A is a marker for breast cancer aggressiveness. Mol Cancer 9, 76.
    [71] Pal D, Outram SP, and Basu A (2013). Upregulation of PKCeta by PKCepsilon and PDK1 involves two distinct mechanisms and promotes breast cancer cell survival. Biochim Biophys Acta 1830, 4040–4045.
    [74] Yano K, Imaeda T, and Niimi T (2008). Transcriptional activation of the human claudin-18 gene promoter through two AP-1 motifs in PMA-stimulated MKN45 gastric cancer cells. Am J Physiol Gastrointest Liver Physiol 294, G336–G343.
    [78] Dukes JD, Fish L, Richardson JD, Blaikley E, Burns S, Caunt CJ, Chalmers AD, and Whitley P (2011). Functional ESCRT machinery is required for constitutive recycling of claudin-1 and maintenance of polarity in vertebrate epithelial cells. Mol Biol Cell 22, 3192–3205.
    [80] Assender JW, Gee JM, Lewis I, Ellis IO, Robertson JF, and Nicholson RI (2007). Protein kinase C isoform expression as a predictor of disease outcome on endocrine therapy in breast cancer. J Clin Pathol 60, 1216–1221.
    [82] Parsons M, Keppler MD, Kline A, Messent A, Humphries MJ, Gilchrist R, Hart IR, Quittau-Prevostel C, Hughes WE, and Parker PJ, et al (2002). Site-directed perturbation of protein kinase C–integrin interaction blocks carcinoma cell chemotaxis. Mol Cell Biol 22, 5897–5911.
    [83] Pan Q, Bao LW, Kleer CG, Sabel MS, Griffith KA, Malonyl Coenzyme A Teknos TN, and Merajver SD (2005). Protein kinase C epsilon is a predictive biomarker of aggressive breast cancer and a validated target for RNA interference anticancer therapy. Cancer Res 65, 8366–8371.
    [84] Platet N, Prevostel C, Derocq D, Joubert D, Rochefort H, and Garcia M (1998). Breast cancer cell invasiveness: correlation with protein kinase C activity and differential regulation by phorbol ester in estrogen receptor-positive and -negative cells. Int J Cancer 75, 750–756.
    [85] Sjo A, Magnusson KE, and Peterson KH (2010). Protein kinase C activation has distinct effects on the localization, phosphorylation and detergent solubility of the claudin protein family in tight and leaky epithelial cells. J Membr Biol 236, 181–189. Pancreatology 19 (2019) 88e96
    Contents lists available at ScienceDirect
    Pancreatology
    Claudin 7 as a possible novel molecular target for the treatment of pancreatic cancer
    Norimitsu Okui a, Yuko Kamata b, Yukiko Sagawa b, Akiko Kuhara b, Kazumi Hayashi c, Tadashi Uwagawa a, Sadamu Homma b, *, Katsuhiko Yanaga a a Department of Surgery, The Jikei University School of Medicine, Tokyo, Japan
    b Division of Oncology, Research Center for Medical Sciences, The Jikei University School of Medicine, Tokyo, Japan
    c Division of Clinical Oncology and Hematology, Department of Internal Medicine, The Jikei University School of Medicine, Tokyo, Japan
    Article history:
    Received in revised form
    Available online 2 November 2018
    Keywords:
    Cell proliferation
    Claudin 7
    Gene expression
    Pancreatic cancer
    Cell cycle
    Background/objectives: Pancreatic cancer consists of various subpopulations of cells, some of which have aggressive proliferative properties. The molecules responsible for the aggressive proliferation of pancreatic cancer may become molecular targets for the therapies against pancreatic cancer. Methods: From a human pancreatic cancer cell line, MIA PaCa-2, MIA PaCa-2-A cells with an epithelial morphology and MIA PaCa-2-R cells with a non-epithelial morphology were clonogenically isolated by the limiting dilution method. Gene expression of these subpopulations was analyzed by DNA microarray. Gene knockdown was performed using siRNA.
    Results: Although the MIA PaCa-2-A and MIA PaCa-2-R cells displayed the same DNA short tandem repeat (STR) pattern identical to that of the parental MIA PaCa-2 cells, the MIA PaCa-2-A cells were more proliferative than the MIA PaCa-2-R cells both in culture and in tumor xenografts generated in immu-nodeficient mice. Furthermore, the MIA PaCa-2-A cells were more resistant to gemcitabine than the MIA PaCa-2-R cells. DNA microarray analysis revealed a high expression of claudin (CLDN) 7 in the MIA PaCa-2-A cells, as opposed to a low expression in the MIA PaCa-2-R cells. The knockdown of CLDN7 in the MIA PaCa-2-A cells induced a marked inhibition of proliferation. The MIA PaCa-2-A cells in which CLDN7 was knocked down exhibited a decreased expression of phosphorylated extracellular signal-regulated kinase (p-Erk)1/2 and G1 cell cycle arrest.