Bio

Professional Education


  • Doctor of Philosophy, Loyola University Of Chicago (2010)
  • B.S., Illinois State University, Chemistry and Biochem/Mol Bio (2004)

Stanford Advisors


Publications

Journal Articles


  • A low-carb diet kills tumor cells with a mutant p53 tumor suppressor gene: The Atkins diet suppresses tumor growth Comment on: Rodriguez OC, et al. Cell Cycle 2012; 11:4436-46; PMID:23151455; http://dx.doi.org/10.4161/cc.22778 CELL CYCLE Lagory, E. L., Giaccia, A. J. 2013; 12 (5): 718-719

    View details for DOI 10.4161/cc.22778

    View details for Web of Science ID 000315522200008

  • VHL loss in renal cell carcinoma leads to up-regulation of CUB domain-containing protein 1 to stimulate PKC delta-driven migration PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA Razorenova, O. V., Finger, E. C., Colavitti, R., Chernikova, S. B., Boiko, A. D., Chan, C. K., Krieg, A., Bedogni, B., LaGory, E., Weissman, I. L., Broome-Powell, M., Giaccia, A. J. 2011; 108 (5): 1931-1936

    Abstract

    A common genetic mutation found in clear cell renal cell carcinoma (CC-RCC) is the loss of the von Hippel-Lindau (VHL) gene, which results in stabilization of hypoxia-inducible factors (HIFs), and contributes to cancer progression and metastasis. CUB-domain-containing protein 1 (CDCP1) was shown to promote metastasis in scirrhous and lung adenocarcinomas as well as in prostate cancer. In this study, we established a molecular mechanism linking VHL loss to induction of the CDCP1 gene through the HIF-1/2 pathway in renal cancer. Also, we report that Fyn, which forms a complex with CDCP1 and mediates its signaling to PKC?, is a HIF-1 target gene. Mechanistically, we found that CDCP1 specifically regulates phosphorylation of PKC?, but not of focal adhesion kinase or Crk-associated substrate. Signal transduction from CDCP1 to PKC? leads to its activation, increasing migration of CC-RCC. Furthermore, patient survival can be stratified by CDCP1 expression at the cell surface of the tumor. Taken together, our data indicates that CDCP1 protein might serve as a therapeutic target for CC-RCC.

    View details for DOI 10.1073/pnas.1011777108

    View details for Web of Science ID 000286804700036

    View details for PubMedID 21233420

  • The Protein Kinase C delta Catalytic Fragment Is Critical for Maintenance of the G(2)/M DNA Damage Checkpoint JOURNAL OF BIOLOGICAL CHEMISTRY Lagory, E. L., Sitailo, L. A., Denning, M. F. 2010; 285 (3): 1879-1887

    Abstract

    Protein kinase Cdelta (PKCdelta) is an essential component of the intrinsic apoptotic program. Following DNA damage, such as exposure to UV radiation, PKCdelta is cleaved in a caspase-dependent manner, generating a constitutively active catalytic fragment (PKCdelta-cat), which is necessary and sufficient for keratinocyte apoptosis. We found that in addition to inducing apoptosis, expression of PKCdelta-cat caused a pronounced G(2)/M cell cycle arrest in both primary human keratinocytes and immortalized HaCaT cells. Consistent with a G(2)/M arrest, PKCdelta-cat induced phosphorylation of Cdk1 (Tyr(15)), a critical event in the G(2)/M checkpoint. Treatment with the ATM/ATR inhibitor caffeine was unable to prevent PKCdelta-cat-induced G(2)/M arrest, suggesting that PKCdelta-cat is functioning downstream of ATM/ATR in the G(2)/M checkpoint. To better understand the role of PKCdelta and PKCdelta-cat in the cell cycle response to DNA damage, we exposed wild-type and PKCdelta null mouse embryonic fibroblasts (MEFs) to UV radiation. Wild-type MEFs underwent a pronounced G(2)/M arrest, Cdk1 phosphorylation, and induction of apoptosis following UV exposure, whereas PKCdelta null MEFs were resistant to these effects. Expression of PKCdelta-green fluorescent protein, but not caspase-resistant or kinase-inactive PKCdelta, was able to restore G(2)/M checkpoint integrity in PKCdelta null MEFs. The function of PKCdelta in the DNA damage-induced G(2)/M cell cycle checkpoint may be a critical component of its tumor suppressor function.

    View details for DOI 10.1074/jbc.M109.055392

    View details for Web of Science ID 000273429100034

    View details for PubMedID 19917613

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