Expression of genes encoding for enzymes associated with O-GlcNAcylation in endometrial carcinomas: Clinicopathologic correlations

Ginekologia Polska

Volumn 83, Issue 1, 2012, Pages 22-26

  Krześlak, Anna ^a   Wójcik Krowiranda, Katarzyna ^b   Forma, Ewa ^a   Bieńkiewicz, Andrzej ^b   Bryś, Magdalena ^a  

^a UNIVERSITY OF LODZ   (Poland)

^b MEDICAL UNIVERSITY OF LODZ   (Poland)

Author keywords

Endometrial carcinoma; MGEA5; O GlcNAcylation; OGT

Indexed keywords

EID: 84857126294     PISSN: 00170011     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (22)

1. Hart G, Slawson C, Ramirez-Correa G, Lagerlof O. Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease. Annu Rev Biochem. 2011, 80, 825-858.
2. Hanover J, Krause M, Love D. The hexosamine signaling pathway: O-GlcNAc cycling in feast or famine. Biochim Biophys Acta. 2010, 1800, 80-95.
3. Slawson C, Hart G. O-GlcNAc signalling: implications for cancer cell biology. Nat Rev Cancer. 2011, 11:678-684.
4. Caldwell S, Jackson S, Shahriari K, [et al.]. Nutrient sensor O-GlcNAc transferase regulates breast cancer tumorigenesis through targeting of the oncogenic transcription factor FoxM1. Oncogene. 2010, 29, 2831-2842.
5. Gu Y, Mi W, Ge Y, [et al.]. GlcNAcylation plays an essentials role in breast cancer metastasis. Cancer Res. 2010, 70, 6344-6351.
6. Mi W, Gu Y, Han C, [et al.]. O-GlcNacylation is a novel regulator of lung and colon cancer malignancy. Biochim Biophys Acta. 2011, 1812, 514-519.
7. Shi Y, Tomic J, Wen F [et al.]. Aberrant O-GlcNAcylation characterizes chronic lymphocytic leukemia. Leukemia. 2010, 24, 1588-1598.
8. Zhu Q, Zhou L, Yang Z, [et al.]. O-GlcNAcylation plays a role in tumor recurrence of hepatocellular carcinoma following liver transplantation. Med Oncol. 2011, DOI: 10.1007/s12032-011-9912-1.
9. Krześlak A, Forma E, Bernaciak M, [et al.]. Gene expression of O-GlcNAc cycling enzymes in human breast cancers. Clin Exp Med. 2011, DOI 10.1007/s10238-011-0138-5.
10. Bansal N, Yendluri V, Wenham R. The molecular biology of endometrial cancers and the implications for pathogenesis, classification, and targeted therapies. Cancer Control. 2009, 16, 8-13.
11. Engelsen I, Akslen L, Salvesen H. Biologic markers in endometrial cancer treatment. APMIS. 2009, 117, 693-707.
12. Grosman-Dziewiszek P, Dziegiel P, Zabel M, Disturbance of gene expression in endometrial cancer as therapy aim. Ginekol Pol. 2011, 82, 276-280.
13. Kamemura K, Hayes B, Comer F, Hart G. Dynamic interplay between O-glycosylation and O-phosphorylation of nucleocytoplasmic proteins: alternative glycosylation/phosphorylation of ThR-58, a known mutational hot spot of c-Myc in lymphomas, is regulated by mitogens. J Biol Chem. 2002, 277, 19229-19235.
14. Yang W, Kim J, Nam H, [et al.]. Modification of p53 with O-linked n-acetylglucosamine regulates p53 activity and stability. Nat Cell Biol. 2006, 8, 1074-1083.
15. Jeon Y, Kang S, Kang D, [et al.]. Cyclooxygenase-2 and p53 expressions in endometrial cancer. Cancer Epidemiol Biomarkers Prev. 2004, 13,1538-1542.
16. Simionescu C, Georgescu C, Mǎrgǎritescu C, [et al.]. P53 and PCNA immunoexpression in endometrial carcinomas. Rom J Morphol Embryol. 2006, 47, 137-141.
17. Ozcan S, Andrali S, Cantrell J. Modulation of transcription factor function by O-GlcNAc modification. Biochim Biophys Acta. 2010, 64, 353-364.
18. Li L, Davie J. The role of Sp1 and Sp3 in normal and cancer cell biology. Ann Anat. 2010, 192, 275-83.
19. Lim K, Chang H. Elevated O-linked N-acetylglucosamine correlated with reduced Sp1 cooperative DNA binding with its collaborating factors in vivo. Biosci Biotechnol Biochem. 2010, 74, 1668-1672.
20. Lim K, Chang H. O-GlcNAcylation of Sp1 interrupts Sp1 interaction with NF-Y. Biochem Biophys Res Commun. 2009, 382, 593-597.
21. Dauphinee S, Ma M, Too C. Role of O-linked beta-N-acetylglucosamine modification in the subcellular distribution of alpha4 phosphoprotein and Sp1 in rat lymphoma cells. J Cell Biochem. 2005, 96, 579-88.
22. Vicart A, Lefebvre T, Imbert J, [et al.]. Increased chromatin association of Sp1 in interphase cells by PP2A-mediated dephosphorylations. J Mol Biol. 2006, 364, 897-908.