Professional Education

  • Bachelor of Science, University of Illinois at Urbana Champaign (2007)
  • Doctor of Philosophy, University of Michigan Ann Arbor (2013)

Stanford Advisors

Research & Scholarship

Lab Affiliations


All Publications

  • Aldehyde dehydrogenase 2 in aplastic anemia, Fanconi anemia and hematopoietic stem cells MOLECULAR GENETICS AND METABOLISM Van Wassenhove, L. D., Mochly-Rosen, D., Weinberg, K. I. 2016; 119 (1-2): 28-36


    Maintenance of the hematopoietic stem cell (HSC) compartment depends on the ability to metabolize exogenously and endogenously generated toxins, and to repair cellular damage caused by such toxins. Reactive aldehydes have been demonstrated to cause specific genotoxic injury, namely DNA interstrand cross-links. Aldehyde dehydrogenase 2 (ALDH2) is a member of a 19 isoenzyme ALDH family with different substrate specificities, subcellular localization, and patterns of expression. ALDH2 is localized in mitochondria and is essential for the metabolism of acetaldehyde, thereby placing it directly downstream of ethanol metabolism. Deficiency in ALDH2 expression and function are caused by a single nucleotide substitution and resulting amino acid change, called ALDH2*2. This genetic polymorphism affects 35-45% of East Asians (about ~560 million people), and causes the well-known Asian flushing syndrome, which results in disulfiram-like reactions after ethanol consumption. Recently, the ALDH2*2 genotype has been found to be associated with marrow failure, with both an increased risk of sporadic aplastic anemia and more rapid progression of Fanconi anemia. This review discusses the unexpected interrelationship between aldehydes, ALDH2 and hematopoietic stem cell biology, and in particular its relationship to Fanconi anemia.

    View details for DOI 10.1016/j.ymgme.2016.07.004

    View details for Web of Science ID 000384631000005

    View details for PubMedID 27650066

  • RhoC GTPase Is a Potent Regulator of Glutamine Metabolism and N-Acetylaspartate Production in Inflammatory Breast Cancer Cells JOURNAL OF BIOLOGICAL CHEMISTRY Wynn, M. L., Yates, J. A., Evans, C. R., Van Wassenhove, L. D., Wu, Z. F., Bridges, S., Bao, L., Fournier, C., Ashrafzadeh, S., Merrins, M. J., Satin, L. S., Schnell, S., Burant, C. F., Merajver, S. D. 2016; 291 (26): 13715-13729


    Inflammatory breast cancer (IBC) is an extremely lethal cancer that rapidly metastasizes. Although the molecular attributes of IBC have been described, little is known about the underlying metabolic features of the disease. Using a variety of metabolic assays, including (13)C tracer experiments, we found that SUM149 cells, the primary in vitro model of IBC, exhibit metabolic abnormalities that distinguish them from other breast cancer cells, including elevated levels of N-acetylaspartate, a metabolite primarily associated with neuronal disorders and gliomas. Here we provide the first evidence of N-acetylaspartate in breast cancer. We also report that the oncogene RhoC, a driver of metastatic potential, modulates glutamine and N-acetylaspartate metabolism in IBC cells in vitro, revealing a novel role for RhoC as a regulator of tumor cell metabolism that extends beyond its well known role in cytoskeletal rearrangement.

    View details for DOI 10.1074/jbc.M115.703959

    View details for Web of Science ID 000379771100026

    View details for PubMedID 27129239

  • Signaling properties of a covalent modification cycle are altered by a downstream target PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA Ventura, A. C., Jiang, P., Van Wassenhove, L., Del Vecchio, D., Merajver, S. D., Ninfa, A. J. 2010; 107 (22): 10032-10037


    We used a model system of purified components to explore the effects of a downstream target on the signaling properties of a covalent modification cycle, an example of retroactivity. In the experimental system used, a bifunctional enzyme catalyzed the modification and demodification of its substrate protein, with both activities regulated by a small molecule stimulus. Here we examined how a downstream target for one or both forms of the substrate of the covalent modification cycle affected the steady-state output of the system, the sensitivity of the response to the stimulus, and the concentration of the stimulus required to provide the half-maximal response (S(50)). When both the modified and unmodified forms of the substrate protein were sequestered by the downstream target, the sensitivity of the response was dramatically decreased, but the S(50) was only modestly affected. Conversely, when the downstream target only sequestered the unmodified form of the substrate protein, significant effects were observed on both system sensitivity and S(50). Behaviors of the experimental systems were well approximated both by simple models allowing analytical solutions and by a detailed model based on the known interactions and enzymatic activities. Modeling and experimentation indicated that retroactivity may result in subsensitive responses, even if the covalent modification cycle displays significant ultrasensitivity in the absence of retroactivity. Thus, we provide examples of how a downstream target can alter the signaling properties of an upstream signal transduction covalent modification cycle.

    View details for DOI 10.1073/pnas.0913815107

    View details for Web of Science ID 000278246000025

    View details for PubMedID 20479260

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