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003 OCoLC;

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007 cr bn|||||||||;

008 110211s2010 ncu ob 000 0 eng d;

035 a| (Sirsi) o701552233;

035 a| (OCoLC)701552233;

040 a| EREc| EREd| EREd| UtOrBLW;

049 a| EREE;

090 a| QH603.C4;

100 1 a| Hoggard, John Elliott.?| UNAUTHORIZED;

245 10 a| Claudin-7 increases chemosensitivity to cisplatin in human NCI-H522 lung cancer cells /c| by John Elliott Hoggard.;

260 a| [Greenville, N.C.] :b| East Carolina University,c| 2010.;

300 a| 53 pages :b| digital, PDF file;

336 a| text2| rdacontent;

337 a| computer2| rdamedia;

338 a| online resource2| rdacarrier;

538 a| System requirements: Adobe Reader.;

538 a| Mode of access: World Wide Web.;

502 b| M.S.c| East Carolina Universityd| 2010.;

500 a| Presented to the faculty of the Department of Biology.;

500 a| Advisor: Yan-Hua Chen.;

500 a| Title from PDF t.p. (viewed April 1, 2011).;

520 3 a| Lung cancer is a leading cause of cancer death for both men and women worldwide. The 5-year survival rate for lung cancer is only 15%, and it accounts for approximately 1.4 million deaths every year. Recently, it has been reported that changes in expression level of claudin proteins, a family of tight junction integral membrane proteins, has been associated with several types of cancer tissues. Claudin proteins are vital components of the tight junction complex, playing a crucial role in maintaining cell polarity, adhesion, and paracellular permeability. Studies have illustrated that claudin-7 expression is lost in head, neck, invasive breast cancer, and certain types of lung cancer. The objective of this study was to investigate apoptosis in a human lung adenocarcinoma cancer cell line transfected with claudin-7. We transfected claudin-7 cDNA tagged with myc into human NCI-H522 lung cancer cells, which have no detectable expression of claudin-7 protein. H522 cells transfected with vector alone were used as a control. Flow cytometry analysis demonstrated that cells transfected with claudin-7 had a significantly higher percentage of cell apoptosis when compared to that of vector transfected cell population. The cell viability by MTT, (3-(4,5-Dimethylthiazol-2-yl)-2,5- diphenyltetrazolium bromide, a tetrazole), assay was significantly decreased and cell apoptosis by Annexin V assay was significantly increased in claudin-7 transfected cells compared to that of vector transfected cells after cisplatin treatment. Cisplatin is an anti-cancer drug clinically used to treat tumors in several tissues including lung tumors. Furthermore, we found that claudin-7 transfected cells exhibited upregulation of caspase-3, -8, and -9. Also, the phosphorylation of claudin-7 in the H522 cells was examined, and analyses revealed that claudin-7 was phosphorylated at serine 204 by protein kinase C. Comparison of phosphorylated and non- phosphorylated claudin-7 in the H522 cells showed decreased cell viability by the MTT assay suggesting that phosphorylation increases chemosensitivity to cisplatin treatment. We demonstrated that claudin-7 expression in H522 lung cancer cells increases chemosensitivity to cisplatin through increased activation of caspase pathways.;

504 a| Includes bibliographical references.;

650 0 a| Tight junctions (Cell biology)x| Research.=| ^A1042574;

650 0 a| Junctional complexes (Epithelium)x| Research.=| ^A1042533;

650 0 a| Membrane proteinsx| Research.=| ^A105037;

650 0 a| Apoptosisx| Research.=| ^A294849;

650 0 a| Cisplatinx| Research.=| ^A287094;

650 0 a| Lungsx| Cancerx| Research.=| ^A6943;

653 a| Biology;

653 a| Cellular Biology;

700 1 a| Chen, Yan-Hua.?| UNAUTHORIZED;

710 2 a| East Carolina University.b| Department of Biology.=| ^A637467;

856 40 z| Access via ScholarShipu| http://hdl.handle.net/10342/3146;

949 o| jgml;

994 a| C0b| ERE;

596 a| 1 4;

998 a| 2399308;

999 a| CLICK ON WEB ADDRESSw| ASISc| 1i| 2399308-1001l| JNETm| JOYNERr| Ys| Yt| JNE3ETDu| 2/14/2011x| ETDz| JERESOURCE;

999 a| CLICK ON WEB ADDRESSw| ASISc| 1i| 2399308-2001l| HSLELECm| HSLr| Ys| Yt| HEETDu| 2/14/2011x| ETDz| HERESOURCE;

Claudin-7 increases chemosensitivity to cisplatin in human NCI-H522 lung cancer cells / by John Elliott Hoggard.

Author/creator	Hoggard, John Elliott
Other author	Chen, Yan-Hua.
Other author	East Carolina University. Department of Biology.
Format	Theses and dissertations
Publication Info	[Greenville, N.C.] : East Carolina University, 2010.
Description	53 pages : digital, PDF file
Supplemental Content	Access via ScholarShip
Subjects	Tight junctions (Cell biology)--Research. Junctional complexes (Epithelium)--Research. Membrane proteins--Research. Apoptosis--Research. Cisplatin--Research. Lungs--Cancer. --Research.

Summary	Lung cancer is a leading cause of cancer death for both men and women worldwide. The 5-year survival rate for lung cancer is only 15%, and it accounts for approximately 1.4 million deaths every year. Recently, it has been reported that changes in expression level of claudin proteins, a family of tight junction integral membrane proteins, has been associated with several types of cancer tissues. Claudin proteins are vital components of the tight junction complex, playing a crucial role in maintaining cell polarity, adhesion, and paracellular permeability. Studies have illustrated that claudin-7 expression is lost in head, neck, invasive breast cancer, and certain types of lung cancer. The objective of this study was to investigate apoptosis in a human lung adenocarcinoma cancer cell line transfected with claudin-7. We transfected claudin-7 cDNA tagged with myc into human NCI-H522 lung cancer cells, which have no detectable expression of claudin-7 protein. H522 cells transfected with vector alone were used as a control. Flow cytometry analysis demonstrated that cells transfected with claudin-7 had a significantly higher percentage of cell apoptosis when compared to that of vector transfected cell population. The cell viability by MTT, (3-(4,5-Dimethylthiazol-2-yl)-2,5- diphenyltetrazolium bromide, a tetrazole), assay was significantly decreased and cell apoptosis by Annexin V assay was significantly increased in claudin-7 transfected cells compared to that of vector transfected cells after cisplatin treatment. Cisplatin is an anti-cancer drug clinically used to treat tumors in several tissues including lung tumors. Furthermore, we found that claudin-7 transfected cells exhibited upregulation of caspase-3, -8, and -9. Also, the phosphorylation of claudin-7 in the H522 cells was examined, and analyses revealed that claudin-7 was phosphorylated at serine 204 by protein kinase C. Comparison of phosphorylated and non- phosphorylated claudin-7 in the H522 cells showed decreased cell viability by the MTT assay suggesting that phosphorylation increases chemosensitivity to cisplatin treatment. We demonstrated that claudin-7 expression in H522 lung cancer cells increases chemosensitivity to cisplatin through increased activation of caspase pathways.
General note	Presented to the faculty of the Department of Biology.
General note	Advisor: Yan-Hua Chen.
General note	Title from PDF t.p. (viewed April 1, 2011).
Dissertation note	M.S. East Carolina University 2010.
Bibliography note	Includes bibliographical references.
Technical details	System requirements: Adobe Reader.
Technical details	Mode of access: World Wide Web.

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Claudin-7 increases chemosensitivity to cisplatin in human NCI-H522 lung cancer cells / by John Elliott Hoggard.

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