Genetics, Cell Biology & Anatomy

Vimla Band, Ph.D.
Professor and Vice Chair of Research
Department of Genetics, Cell Biology and Anatomy

Associate Director of Center for Breast Cancer Research
Eppley Cancer Center

All India Institute of Medical Sciences, India (Ph.D), 1985
Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA (Post-doc), 1991

Phone: (402) 559-8565 (office)
Fax:    (402) 559-7328
Email:  vband@unmc.edu

Vimla Band, Ph.D. 


Research – Overall Goals:

The major focus of the laboratory is to delineate molecular mechanisms of early steps in transformation of mammary epithelial cells with the goal of identifying novel molecular diagnostic/prognostic markers and potential therapy targets of breast cancers.

We have identified several new proteins that are involved in mammary epithelial cell transformation.  These are: i) E6TP1 (for E6 targeted protein 1) it was later renamed as Sipa1L1 (due to high homology with Sipa1). We are testing the hypothesis that Sipa1L1 functions as a negative regulator of Rap-GTPase in mammary epithelial cell-matrix and cell-cell adhesion; ii) hADA3 (alteration deficiency in activation 3), we have shown that hADA3 is a novel transcriptional co-activator of p53, retinoid receptors and estrogen receptors and thus involved in number of physiological processes; iii) hEcd, the human homologue of drosophila ecdysoneless (Ecd). Cell and knockout mouse model demonstrates that Ecd is involved in cell survival. Current research in the laboratory is to examine the role of these novel targets in epithelial cell growth, differentiation, development, and oncogenesis using both in vitro and in vivo (knock-out) models.  Furthermore, an important ongoing area of research is to examine the role of these novel proteins in breast and other carcinomas tumor progression by examining their expression and localization in human tumor tissues.

The other area of interest in the laboratory is to isolate and define stem/progenitor cells that differentiate into different cell types of the mammary gland, such as myoepithelial, luminal or basal cells. We are attempting to develop in vitro and in vivo models of different sub-types of human breast cancers to understand the biological basis of distinct tumor subtypes and exploring these as potential models for therapy.

 

Publications:
  1. Zhao X, Goswami M, Pokhriyal N, Ma H, Sturgis CD, Victor TA, Band H  and Band V. Cox-2 expression during mammary epithelial cell immortalization and breast tumor progression. Cancer Res., In Press, 2007.
     
  2. Germaniuk-kurowska A, Nag A, Zhao X, Dimri, M, Band H and Band V. Ada3 requirement for HAT recruitment to estrogen receptors and estrogen-dependent breast cancer cell proliferation.  Cancer Res., In Press, 2007.
     
  3. Zhao Y, Katzman RB, Delmolino L, Bhat I, Zhang Y, Gurumurthy CB, Reddi HV, Solomon A, Zeng M, Kung A, Ma H, Gao Q, Dimri G, Stanculescu A, Miele L, Wu  l, Griffin JD, Wazer DE, Band H and Band V. The Notch regulator MAML1 interacts with p53 and functions as a coactivator.  J. Biol. Chem.  282:11969-11981,2007.
     
  4. Nag A., Sassack M, Germaniuk-Kurowska A, Band H and Band V. Essential role of human ADA3 in p53 acetylation.  J. Biol. Chem. 282:8812-8820, 2007.
     
  5. Zhang Y, Gurumurthy CB, Kim JH, Bhat I, Gao Q, Dimri G, Lee SW, Band H and Band V.  The human ortholog of drosophila ecdysoneless protein interacts with p53 and regulates its function.  Cancer Res., 66:7167-7175, 2006.
     
  6. Zeng M, Zhang Y, Bhat I, Wazer DE, Band H, Band V. The human kallikrein 10 promoter contains a functional retinoid acid response element. Biol. Chem.  387:741-747, 2006.
     
  7. Zhang Y, Bhat I, Zeng M, Goyal  J, Wazer DE, Band V. Human Kallikrein 10, a predictive marker for breast cancer. Biol. Chem.  387:715-721, 2006.
     
  8. Dimri G, Band H and Band V.   Mammary epithelial cell transformation: insights from cell culture and mouse models.  Breast Cancer Res., 7:171-179, 2005.
     
  9. Meng G, Zhao Y, Nag A, Zeng M, Dimri G, Gao Q, Wazer DE, Kumar R, Band  H and Band V.  Human ADA3 binds to Estrogen Receptor (ER) and functions as a coactivator for ER-mediated transactivation.  J. Biol. Chem. 279:54230-54240, 2004.
     
  10. Singh L, Gao Q, Kumar A, Gotoh T, Wazer DE, Band H, Feig LA, Band V. The high-risk human papillomavirus type 16 E6 counters the GAP function of E6TP1 toward small Rap G proteins.  J. Virol., 77:1614-1620, 2003.
     
  11. Zeng M, Kumar A, Meng G, Gao Q, Dimri G, Wazer D, Band H, Band V. Human papilloma virus 16 E6 oncoprotein inhibits retinoic X receptor-mediated transactivation by targeting human ADA3 coactivator.  J. Biol. Chem 277:45611-45618, 2002.
     
  12. Kumar A, Gao Q, Singh L, Huibregtse JM, Beaudenon S, Srinivasan S, Wazer DE, Band H and Band V. Human papillomavirus E6-induced degradation of E6TP1 is mediated by E6AP ubiquitin ligase. Cancer Res., 62:3315-3321, 2002.
     
  13. Kumar A, Zhao Y, Meng G, Zeng M, Srinivasan S, Delmolino LM, Gao Q, Dimri G, Wazer D, Band H and Band V. Human papilloma virus oncoprotein E6 inactivates the transcriptional coactivator human ADA3. Mol. Cell. Biol. 22:5801-5812, 2002.
     
  14. Li B, Goyal J, Dhar S, Dimri G, Evron E, Sukumar S, Wazer DE, Band V. CpG Methylation as a Basis for Breast Tumor-specific Loss of NES1/kallikrein 10 Expression. Cancer Res. 61:8014-8021, 2001.
     
  15. Dhar S,  Bhargava R, Yunes M, Li Biao, Goyal J, Naber S, Wazer DE, Band V. Analysis of NES1/kallikrein 10 mRNA Expression by In Situ-Hybridization, a Novel Marker for Breast Cancer. Clin. Cancer Res., 7:3393-3398, 2001.
     
  16. Gao Q, Singh L, Kumar A, Srinivasan S, Wazer D.E., and Band V. HPV 16 E6 Induced Degradation of E6TP1 Correlates with it's Ability to Immortalize Human Mammary Epithelial Cells. J. Virol., 75: 4459-4466, 2001.
     
  17. Gao Q, Kumar A, Srinivasan S, Singh L, Mukai H, Ono Y, Wazer DE and Band V. PKN binds and phosphorylates human papillomavirus E6 oncoprotein. J. Biol. Chem. 275: 14824-14830, 2000.
     
  18. Gao Q, Srinivasan S, Boyer SN, Wazer DE, and Band V.  The E6 oncoproteins of high-risk papilloma viruses bind to a novel putative GAP protein, E6TP1, and target it for degradation. Mol. Cell.  Biol., 19:733-744, 1999.