Localization of enolase in the subfractions of a breast cancer cell line

Zeitschrift fur Naturforschung - Section C Journal of Biosciences

Volumn 64, Issue 9-10, 2009, Pages 754-758

  Seweryn, Ewa ^a   Pietkiewicz, Jadwiga ^a   Bednarz Misa, Iwona S ^a   Ceremuga, Ireneusz ^a   Saczko, Jolanta ^a   Kulbacka, Julita ^a   Gamian, Andrzej ^a  

^a WROCLAW MEDICAL UNIVERSITY   (Poland)

Author keywords

MCF 7 breast cancer cells; Plasminogen; Enolase

Indexed keywords

EID: 70449562668     PISSN: 09395075     EISSN: None     Source Type: Journal    
DOI: 10.1515/znc-2009-9-1023     Document Type: Article

References (22)

1. Altenberg B. and Greulich K. O. (2004), Genes of glycolysis are ubiquitously overexpressed in 24 cancer classes. Genomics 84, 1014-1020.
2. Altenberg B., Gemuend C., and Greulich K. O. (2006), Ubiquitous cancer genes: multipurpose molecules for protein micro-arrays. Proteomics 6, 67-71.
3. Andronicos N. M., Ranson M., Bognacki J., and Baker M. S. (1997), The human ENO1 gene product (recombinant human alpha-enolase) displays characteristics required for a plasminogen binding protein. Biochim. Biophys. Acta 1337, 27-39.
4. Bergmann S., Wild D., Diekmann O., Frank R., Bracht D., Chatwal G. S., and Hammerschmidt S. (2003), Identification of a novel plasmin(ogen)-binding motif in surface displayed alpha-enolase of Streptococcus pneumoniae. Mol. Microbiol. 49, 411-423.
5. Ehinger S., Schubert W. D., Bergmann S., Hammerschmidt S., and Heinz D. (2004), Plasmin(ogen)-binding α-enolase from Streptococcus pneumoniae: crystal structure and evaluation of plasmin(ogen)-binding sites. J. Mol. Biol. 343, 997-1005.
6. Feo S., Arcuri D., Piddini E., Passantino R., and Giallongo A. (2000), ENO 1 gene product binds to the c-myc promoter and acts as a transcriptional repressor: Relationship with Myc promoter-binding protein 1 (MBP-1). FEBS Lett. 473, 47-52.
7. Fox D. and Smulian A. G. (2001), Plasminogen-binding activity of enolase in the opportunistic pathogen Pneumocystis carinii. Med. Mycol. 39, 495-507.
8. Johnstone S. A., Waisman D. M., and Rattner J. B. (1992), Enolase is present at the centrosome of HeLa cells. Exp. Cell Res. 202, 458-463.
9. Laemmli K. (1970), Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
10. Liliom K., Wagner G., Kovacs J., Comin B., Cascante M., Orosz F., and Ovadi J. (1999), Combined enhancement of microtubule assembly and glucose metabolism in neuronal systems in vitro: decreased sensitivity to copper toxicity. Biochem. Biophys. Res. Commun. 264, 605-610.
11. Liu K. J. and Shih N. Y. (2007), The role of enolase in tissue invasion and metastasis of pathogens and tumor cells. J. Cancer Mol. 3, 45-48.
12. Lopez-Alemany R., Longstaff C., Hawley S., Mirshahi M., Fabregas P., Jardi M., Merton E., Miles L. A., and Felez J. (2003), Inhibition of cell surface mediated plasminogen activation by a monoclonal antibody against α-enolase. Am. J. Hematol. 72, 234-242.
13. Malorni L., Cacace G., Cuccurullo M., Pocsfalvi G., Chambery A., Farina A., Di Marco A., Parente A., and Malorni A. (2006), Proteomic analysis of MCF-7 breast cancer cell line exposed to mitogenic concentration of 17β-estradiol. Proteomics 6, 5973-5982.
14. Mazzola J. L. and Sirover M. A. (2003), Subcellular localization of human glyceraldehydes-3-phosphate dehydrogenase is independent of its glycolytic function. Biochim. Biophys. Acta 1622, 50-56.
15. Pancholi V. (2001), Multifunctional α-enolase: its role in diseases. Cell. Mol. Life Sci. 58, 902-920.
16. Redlitz A., Fowler B. J., Plow E. F., and Miles L. A. (1995), The role of an enolase-related molecule in plasmin(ogen)-binding to cells. Eur. J. Biochem. 227, 407-415.
17. Sedoris K. C., Thomas S. D., and Miller D. M. (2007), c-Myc promoter binding protein regulates the cellular response to an altered glucose concentration. Biochemistry 46, 8659-8668.
18. Seweryn E., Pietkiewicz J., Szamborska A., and Gamian A. (2007), Enolase on the surface of prokaryotic and eukaryotic cells is a receptor for human plasminogen. Postepy Hig. Med. Dosw. 61, 672-682 (online).
19. Seweryn E., Bednarz-Misa I. S., Danielewicz R., Saczko J., Kulbacka J., Dawiskiba T., and Pietkiewicz J. (2008), Distribution of β-enolase in normal and tumor rat cells. Folia Histochem. Cytobiol. 46, 519-524.
20. Tanaka M., Taniguchi T., Ohkubo T., and Nakashima K. (1998), c DNA cloning and characterization of neuron-specific enolase from chicken. Biochim. Biophys. Acta 1395, 28-33.
21. Walsh J. K., Keith T. J., and Knull H. R. (1989), Glycolytic enzyme interactions with tubulin and microtubules. Biochim. Biophys. Acta 999, 64-70.
22. Witkowska D., Pietkiewicz J., Szostko B., Danielewicz R., Maslowski L., and Gamian A. (2005), Antibodies against human muscle enolase recognize a 45-kDa bacterial cell wall outer membrane enolase-like protein. FEMS Immunol. Med. Microbiol. 45, 53-62.