Douglas Currie Ph.D.
- Ph.D., Zoology, University of Cambridge, 1992
- B. Sc., Zoology, University of St. Andrews, 1985
A native of Scotland, Dr. Currie joined the Biology Department at USM in 2003 after postdoctoral work at the University of Washington. He is a neurobiologist who specializes on the effects of toxins, particularly arsenic, on the developing nervous system.
Dr. Currie regularly teaches Neurobiology (BIO 321, 322) and Animal Physiology (BIO 401/501, 402/502). He also occasionally teaches the plant and animal physiology course (BIO 109) within the introductory biology sequence, as well as the nonmajors course in biology (BIO 101).
Brain development is a fascinating and incredibly complex process. Billions of neurons are generated and then must differentiate, sending out axons and dendrites, and make connections with target neurons throughout the brain. As a developmental neurobiologist I am broadly interested in these events.
Work in my lab focuses on trying to understand specific aspects of brain development. In particular, we are interested in understanding how electrical activity, at very early stages of development, shapes and regulates the development of neurons in the brain. We are currently investigating one of the major molecular pathways by which this activity regulates neuron development, the nitric oxide (NO)/ cyclic guanosine monophosphate (cGMP) pathway.
We also developed a new line of research in collaboration with other members of the Center for Integrated and Applied Environmental Toxicology here at USM. The emphasis of this program is to investigate the effects of exposure to arsenic in utero on neuronal development in the brain. Arsenic contamination of ground water is a significant issue in a number of New England states.
Our research approach employs multiple techniques including immunohistochemistry, pharmacological manipulations, culturing of brain slices and neurons, dye labeling and confocal microscopy.
Szlosek, D. and Currie, D. (2016) Application and mechanism of malonic acid as a green alternative for protein-crosslinking. Green and Sustainable Chemistry 6: 110-115.