BIOCHEMISTRY AT MU
FACULTY RESEARCH
ACADEMICS
CONTACT LISTS
POSITION OPENINGS
| Email: | petrism@missouri.edu |
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| Phone: | (573) 882-9685 | |
| Fax: | (573) 882-0185 | |
| Office: | 540D Bond Life Sciences Center | |
| Mailing Address: |
Christopher S. Bond Life Sciences Center
540D Bond Life Sciences Center University of Missouri-Columbia Columbia, MO 65211 |
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| Research Areas: |
The regulation of metal nutrition and impacts on common human diseases. |
Educational Background
| B.Sc. | University of Melbourne | Melbourne, Australia | Biochemistry/Genetics | |
| PhD | University of Melbourne | Melbourne, Australia | Genetics |
Notable Honors and Service
Research Description
The micronutrient copper (Cu) is essential for several key enzymatic processes involved in energy generation, protection against reactive oxygen species, formation of blood vessels, immune function, and healthy functioning of the central nervous system. This nutrient is able to exist in two oxidation states Cu1+ and Cu2+, and participate in the generation of reactive oxygen species. A delicate balance of copper homeostasis must be maintained to provide sufficient levels of this nutrient, while preventing toxic build up.
Copper and Cancer
Recent evidence suggests that copper plays a key role in tumor growth because this metal is essential for blood vessel formation (angiogenesis). Drugs that bind copper may inhibit tumor growth by preventing angiogenesis.
Copper and Alzheimer's disease
Copper has been shown to interact with the toxic beta-amyloid peptide, and is present in high concentrations in amyloid plaques within in the brains of Alzheimer’s disease patients. Whether this copper is function in a protective or detrimental capacity is unknown.
Projects
Our lab is interested in characterizing the copper homeostasis pathways in animal and cell culture models of microbial infection, tumor growth and Alzheimer's disease, and how this essential nutrient contributes to these pathologies.
Selected Publications
Lane, C., Petris, M. J., Benmerah, A., Greenough, M. & Camakaris, J. (2004) Studies on endocytic mechanisms of the Menkes copper-translocating P-type ATPase (ATP7A; MNK). Endocytosis of the Menkes protein. Biometals 17: 87-98.
Petris, M. J. (2004) The SLC31 (Ctr) copper transporter family. Pflugers Arch 447: 752-755.
Wang, F., Dufner-Beattie, J., Kim, B. E., Petris, M. J., Andrews, G. & Eide, D. J. (2004) Zinc-stimulated endocytosis controls activity of the mouse ZIP1 and ZIP3 zinc uptake transporters. J Biol Chem 279: 24631-24639.
Wang, F., Kim, B. E., Dufner-Beattie, J., Petris, M. J., Andrews, G. & Eide, D. J. (2004) Acrodermatitis enteropathica mutations affect transport activity, localization and zinc-responsive trafficking of the mouse ZIP4 zinc transporter. Hum Mol Genet 13: 563-571.
Wang, F., Kim, B. E., Petris, M. J. & Eide, D. J. (2004) The mammalian Zip5 protein is a zinc transporter that localizes to the basolateral surface of polarized cells. J Biol Chem 279: 51433-51441.
Kim, B. E. & Petris, M. J. (2007) Phenotypic diversity of menkes disease in mottled mice is associated with defects in localization and trafficking of the ATP7A protein. J Med Genet.
Mao, X., Kim, B. E., Wang, F., Eide, D. J. & Petris, M. J. (2007) A histidine-rich cluster mediates the ubiquitination and degradation of the human zinc transporter, hZIP4, and protects against zinc cytotoxicity. J Biol Chem 282: 6992-7000.
Employment Opportunities