RIPK4 is downregulated in poorly differentiated tongue cancer and is associated with migration/invasion and cisplatin-induced apoptosis

International Journal of Biological Markers

Volumn 29, Issue 2, 2014, Pages

  Wang, Xinhua ^a   Zhu, Wenyuan ^a   Zhou, Yi ^a   Xu, Wanlian ^c   Wang, Huiming ^a,b  

^a ZHEJIANG UNIVERSITY   (China)

^b ZHEJIANG UNIVERSITY   (China)

^c Third Hospital of Hangzhou   (China)

Author keywords

Cancer; Differentiation; Oral squamous cell carcinomas; Receptor interacting kinase protein 4; Tongue

Indexed keywords

CASPASE 8; CISPLATIN; FLUORESCEIN ISOTHIOCYANATE; MATRIGEL; RECEPTOR INTERACTING PROTEIN SERINE THREONINE KINASE; RECEPTOR INTERACTING PROTEIN SERINE THREONINE KINASE 4; SHORT HAIRPIN RNA; UNCLASSIFIED DRUG; ANKRD3 PROTEIN, HUMAN; ANTINEOPLASTIC AGENT; PROTEIN SERINE THREONINE KINASE;

ADULT; AGED; APOPTOSIS; ARTICLE; CELL CYCLE PHASE; CELL CYCLE PROGRESSION; CELL DIFFERENTIATION; CELL GROWTH ASSAY; CELL INVASION; CELL MIGRATION; CELL PROLIFERATION ASSAY; CHEMILUMINESCENCE IMMUNOASSAY; CHEMOSENSITIVITY; CONFOCAL LASER MICROSCOPY; CONTROLLED STUDY; DISEASE ASSOCIATION; FEMALE; FLOW CYTOMETRY; HUMAN; HUMAN CELL; HUMAN TISSUE; IMMUNOCYTOCHEMISTRY; IMMUNOHISTOCHEMISTRY; MAJOR CLINICAL STUDY; MALE; MRNA EXPRESSION ASSAY; PROTEIN EXPRESSION; REAL TIME POLYMERASE CHAIN REACTION; RECEPTOR DOWN REGULATION; RECEPTOR UPREGULATION; SCRATCH WOUND HEALING ASSAY; TONGUE CARCINOMA; ULTRAVIOLET SPECTROSCOPY; WESTERN BLOTTING; CELL MOTION; DOWN REGULATION; DRUG EFFECTS; ENZYMOLOGY; GENETIC TRANSFECTION; GENETICS; HEAD AND NECK TUMOR; METABOLISM; PATHOLOGY; SQUAMOUS CELL CARCINOMA; TONGUE TUMOR;

AGED; ANTINEOPLASTIC AGENTS; APOPTOSIS; CARCINOMA, SQUAMOUS CELL; CELL DIFFERENTIATION; CELL MOVEMENT; CISPLATIN; DOWN-REGULATION; FEMALE; HEAD AND NECK NEOPLASMS; HUMANS; MALE; PROTEIN-SERINE-THREONINE KINASES; TONGUE NEOPLASMS; TRANSFECTION;

EID: 84903385930     PISSN: 03936155     EISSN: 17246008     Source Type: Journal    
DOI: 10.5301/jbm.5000073     Document Type: Article

References (21)

1. Jemal A, Siegel R, Xu J, Ward E. Cancer statistics, 2010. CA Cancer J Clin. 2010; 60(5): 277-300.
2. de Camargo Cancela M, Voti L, Guerra-Yi M, Chapuis F, Mazuir M, Curado MP. Oral cavity cancer in developed and in developing countries: population-based incidence. Head Neck. 2010; 32(3): 357-367.
3. Weinberg MA, Estefan DJ. Assessing oral malignancies. Am Fam Physician. 2002; 65(7): 1379-1384.
4. Bello IO, Soini Y, Salo T. Prognostic evaluation of oral tongue cancer: means, markers and perspectives (I). Oral Oncol. 2010; 46(9): 630-635.
5. Bhr C, Rohwer A, Stempka L, Rincke G, Marks F, Gschwendt M. DIK, a novel protein kinase that interacts with protein kinase Cdelta. Cloning, characterization, and gene analysis. J Biol Chem. 2000; 275(46): 36350-36357.
6. Chen L, Haider K, Ponda M, Cariappa A, Rowitch D, Pillai S. Protein kinase C-associated kinase (PKK), a novel membrane-associated, ankyrin repeat-containing protein kinase. J Biol Chem. 2001; 276(24): 21737-21744.
7. Meylan E, Martinon F, Thome M, Gschwendt M, Tschopp J. RIP4 (DIK/PKK), a novel member of the RIP kinase family, activates NF-kappa B and is processed during apoptosis. EMBO Rep. 2002; 3(12): 1201-1208.
8. Muto A, Ruland J, McAllister-Lucas LM, et al. Protein kinase C-associated kinase (PKK) mediates Bcl10-independent NFkappa B activation induced by phorbol ester. J Biol Chem. 2002; 277(35): 31871-31876.
9. Moran ST, Haider K, Ow Y, Milton P, Chen L, Pillai S. Protein kinase C-associated kinase can activate NFkappaB in both a kinase-dependent and a kinase-independent manner. J Biol Chem. 2003; 278(24): 21526-21533.
10. Holland P, Willis C, Kanaly S, et al. RIP4 is an ankyrin repeat-containing kinase essential for keratinocyte differentiation. Curr Biol. 2002; 12(16): 1424-1428.
11. Rountree RB, Willis CR, Dinh H, et al. RIP4 regulates epidermal differentiation and cutaneous inflammation. J Invest Dermatol. 2010; 130(1): 102-112.
12. Adams S, Munz B. RIP4 is a target of multiple signal transduction pathways in keratinocytes: implications for epidermal differentiation and cutaneous wound repair. Exp Cell Res. 2010; 316(1): 126-137.
13. Adams S, Pankow S, Werner S, Munz B. Regulation of NFkappaB activity and keratinocyte differentiation by the RIP4 protein: implications for cutaneous wound repair. J Invest Dermatol. 2007; 127(3): 538-544.
14. Wolff AC, Hammond ME, Schwartz JN, et al. American Society of Clinical Oncology/College of American Pathologists. American Society of Clinical Oncology/College of American Pathologists guideline recommendations for human epidermal growth factor receptor 2 testing in breast cancer. Arch Pathol Lab Med. 2007; 131(1): 18-43.
15. Dun ZN, Zhang XL, An JY, Zheng LB, Barrett R, Xie SR. Specific shRNA targeting of FAK influenced collagen metabolism in rat hepatic stellate cells. World J Gastroenterol. 2010; 16(32): 4100-4106.
16. Assadi M, Lamerz J, Jarutat T, et al. Multiple protein analysis of FFPE tissue samples with reverse-phase protein arrays. Mol Cell Proteomics. 2013.
17. Navolanic PM, Steelman LS, McCubrey JA. EGFR family signaling and its association with breast cancer development and resistance to chemotherapy (Review). [Review]. Int J Oncol. 2003; 22(2): 237-252.
18. Ross JS, Fletcher JA, Bloom KJ, et al. Targeted therapy in breast cancer: the HER-2/neu gene and protein. Mol Cell Proteomics. 2004; 3(4): 379-398.
19. Thomas GJ, Speight PM. Cell adhesion molecules and oral cancer. Crit Rev Oral Biol Med. 2001; 12(6): 479-498.
20. Alnemri ES, Livingston DJ, Nicholson DW, et al. Human ICE/CED-3 protease nomenclature. Cell. 1996; 87 (2):171.
21. Meylan E, Tschopp J. The RIP kinases: crucial integrators of cellular stress. Trends Biochem Sci. 2005; 30(3): 151-159.