Bruce D. Hammock, Ph.D.

Distinguished Professor of Entomology and Cancer Research Center, and Director, NIEHS-UCDavis Superfund Basic Research Program, Department of Entomology, College of Agricultural and Environmental Sciences

University of California, Davis
90 Briggs Hall
Davis, CA
E-mail:  bdhammock@ucdavis.edu

Recognized by the international scientific community for novel and remarkable contributions to his field, Dr. Hammock’s research has delved into basic questions of biology and biochemistry that have practical implications for improving both human and environmental health.  His wide ranging peer-reviewed publications attest to his ability to impact a variety of fields relevant to the environment, agriculture and food chemistry.  His research is currently focused on three areas: finding improved pest control agents; determining the human health effects of pesticides, food additives and drugs specifically regulation of xenobiotic metabolism; and developing rapid analytical methods for detecting environmental contaminants.  Among his many academic honors are election to the National Academy of Sciences, and selection as the 2001 UC Davis Faculty Research Lecturer, 2003 UC Davis Distinguished Professor, the 1999 Sterling B. Hendrics Memorial Lecturer, and the 1995 Alexander von Humboldt Awardee.

Viswanathan S, Hammock BD, Newman JW, Meerarani P, Toborek M, Hennig B.  Involvement of CYP 2C9 in Mediating the Proinflammatory Effects of Linoleic Acid in Vascular Endothelial Cells.  J Am Coll Nutr 22(6): 502-510, 2003.  Linoleic acid was shown to induce cytochrome P450 2C9 expression, a fatty acid epoxygenase, resulting in oxidative stress and activation of inflammatory pathways in endothelial cells. Blockade of this enzyme prevented the inflammatory response. Linoleic acid metabolites only produced this response at high concentrations, suggesting that a by-product of this enzymatic reaction, possibly super oxide, was responsible for the inflammatory response. These results suggest dietary intake can influence inflammatory status, and may have implications in gastro-intestinal inflammation observed in association with autism.

Newman JW, Morisseau C, Harris TR, Hammock BD.  The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity.  PNAS 100:1558-1563, 2003. The soluble epoxide hydrolase is an important enzyme involved in the regulation of lipid mediators of blood pressure, inflammation, and steroidogenesis. We recently discovered that this enzyme has a second catalytic site, which can remove phosphate from novel lipid substrates.  The biological function of this metabolic process is unknown but may represent a previously unreported intercellular mechanism of signal transduction.

Yu Z, Davis BB, Morisseau C, Hammock BD, Olson JL, Kroetz DL, Weiss RH.  Vascular localization of soluble epoxide hydrolase in the human kidney.  Am J Physiol-Renal Physiol 286:F720-F726, 2004. Previous animal studies indicate that soluble epoxide hydrolase plays an important role in the regulation of renal eicosanoid levels and systemic blood pressure. We found that soluble epoxide hydrolase is present in the human kidney, being preferentially expressed in the renal vasculature, and support an essential role for this enzyme in renal hemodynamic regulation and its potential utility as a target for therapeutic intervention.

Gomez GA, Morisseau C, Hammock BD, Christianson DW. Structure of human epoxide hydrolase reveals mechanistic inferences on bifunctional catalysis in epoxide and phosphate ester hydrolysis.  Biochem  43:4716-4723, 2004. The X-ray crystal structure of human soluble epoxide hydrolase (sEH) was determined at 2.6 A resolution, revealing a domain-swapped quaternary structure. Key features of the two active sites of the epoxide hydrolase were revealed.

Stok JE, Huang H, Jones PD, Wheelock CE, Morisseau C, Hammock BD.  Identification, expression and purification of a pyrethroid hydrolyzing carboxylesterase from mouse liver microsomes.  J Biol Chem 279:29863-29869, 2004. Carboxylesterases are enzymes that catalyze the hydrolysis of a wide range of ester-containing endogenous and xenobiotic compounds. Although the use of pyrethroids is increasing, the specific enzymes involved in the hydrolysis of these insecticides have yet to be identified. Two pyrethroid-hydrolyzing carboxylesterases were cloned and characterized from mouse liver. Both these enzymes could be used as preliminary tools in establishing the relative toxicity of new pyrethroids.

Principal Investigator: Hydrolytic enzymes in the metabolism, NIEHS, Merit Award, 7/03-6/08, $300,961 annual.  Investigate aspects of the biochemistry, regulation and role of hydrolytic enzymes in the metabolism of epoxide containing toxins and natural products; investigate aspects of the biochemistry, regulation, and role of hydrolytic enzymes in the metabolism of ester containing toxins (Merit Award).

Program Director: Biomarkers of exposure to hazardous substances, National Institute of Environmental Health Sciences Superfund Research Program, NIEHS, 4/00-3/05, $850,000 annual (9 research projects and 5 research/service cores).  The goals of this program project are to determine the fate and transport of hazardous materials in ground water, surface water and air as they move from toxic waste sites; develop sensitive systems for evaluating the exposure and effects of these materials on populations and explore new technologies for thermal and bioremediation of toxic waste

Co-Principal Investigator: Development and implementation of immunoassays for human and environmental monitoring, National Institute of Environmental Health Sciences Superfund Research Program, Project 3, NIEHS, 4/00-3/05, $65,200 annual.  To develop immunoassays for the rapid analysis of environmental contaminants, as biomarkers of exposure to hazardous materials, and develop new immunochemical technologies for use in the environmental field.

Principal Investigator: Role of a/b-hydrolase fold enzymes in the regulation of juvenile hormone U.S. Department of Agriculture/CSREES, 9/03-8/06, $60,300 annual direct.  Development of tools to study the physiology of juvenile hormone epoxide hydrolase and juvenile hormone esterase and use these enzymes in the development of baculoviruses which should have enhanced speed of kill of the most destructive family of pest caterpillars.  This proposal probes fundamental aspects of insect development with the work leading to the development of both classical and recombinant pesticides with high selectivity for target species.

Principal Investigator: Identification and development of biological markers of human exposure to the insecticide permethrin, U.S. Army Medical Research Acquisition Activity, 9/01-10/05, $80,000 annual direct.  Develop analytical technologies to identify and develop laboratory based and field portable methods for the detection and quantitation of human exposure to permethrin.

Director, NIEHS Superfund Basic Research Program Project
Director, NIH Post-doctoral Training Program, Biotechnology

University of California Davis, Distinguished Professor
The University of Queensland, AU, Honorary Professor in the School of Molecular and Microbial Sciences