Health Sciences Library & Informatics Center
MSC09 5100
1 University of New Mexico
Albuquerque, NM 87131-0001

Find Faculty at UNM Health Sciences Center

Eric R Prossnitz, PhD

Contact Information:
1 University of New Mexico
08 4630
Albuquerque NM 87131-0001
272-5647
eprossnitz@salud.unm.edu

Department:
Cell Biology and Physiology

Education:
Doctor of Philosophy :
UC Berkeley, (1989)
Bachelor of Science :
University of Victoria, (1985)

Interests:
G protein-coupled receptors represent the largest family of signal transducing molecules. In all, there are approximately 600-1000 G protein-coupled receptor genes present in the human genome. Because they are involved in almost every aspect of human physiology, G protein-coupled receptors are the targets of nearly one half of prescription drugs on the market today. One area of interest focuses on understanding the mechanisms of activation and inactivation of this receptor family. As a model system, we utilize the N-formyl peptide chemoattractant receptor (FPR) found predominantly on leukocytes. This receptor mediates chemotactic and inflammatory responses within the immune system. Our major areas of interest focus on mechanisms of receptor processing following activation and the role of arrestins in these processes. We have demonstrated that although the phosphorylated FPR binds arrestin, this interaction is not involved in the internalization of the receptor, contrary to what is observed with many other G protein-coupled receptors. However, arrestin is required for receptor recycling back to the cell surface. In addition, activation of the FPR and numerous other GPCRs induces apoptosis in cells devoid of arrestins. We are currently investigating the mechanisms involved in these processes. Another focus of the lab is the novel G protein-coupled estrogen receptor GPR30. This is a classic 7-transmembrane GPCR that we have shown, unlike other GPCRs, resides in the endoplasmic reticulum (Science 2005, 307: 1625-1630). From this location, it binds estrogen and activates numerous cellular signaling pathways including calcium mobilization and PI3K activation. Although classical estrogen receptors (ERa) can activate many of the same cellular effectors as GPR30, the signaling pathways differ for the two receptors. In order to quantitate and localize estrogen binding, we have developed a novel fluorescent estrogen analog that localizes with both classical estrogen receptors and GPR30. Recent screening efforts have led to the identification of the first GPR30-selective agonist, G-1 (Nature Chem Biol 2006 2: 207-12). Current work is addressing the role of this newest estrogen receptor in cellular function, normal physiology and disease.

Publications:
* Revankar, C.M., Cimino, D.F., Sklar, L.A., Arterburn, J.B., Prossnitz, E.R. (2005) An Intracellular 7-Transmembrane G protein-coupled Estrogen Receptor Mediates Rapid Cell Signaling. Science 307, 1625-30.

* Bologa, C.G., Revankar, C.M., Young, S.M., Edwards, B.S., Arterburn, J.B., Kiselyov, A.S., Parker, M.A., Tkachenko, S.E., Savchuck, N.P., Sklar, L.A., Oprea, T.I., Prossnitz, E.R. (2006) Virtual and Biomolecular Screening Converge on a Selective Agonist for GPR30. Nat Chem Biol 2, 207-12.