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Office: C104 Chemistry Building
Phone: 970-491-7326
Fax: 970-491-7569

Deborah Roess

​Professor, Department of Biomedical Sciences
Animal Reproduction and Biotechnology Laboratory
Colorado State University


PhD, St. Louis University
BA, University of Missouri

Research Interests -- Cellular Endocrinology

I use laser-optical instrumentation to measure the lateral and rotational motions of plasma membrane components. One area of study is the molecular motions of luteinizing hormone (LH) receptors on luteal and Leydig cells. Movement of molecules, such as the LH receptor, in a membrane is affected by receptor and hormone structure, cytoskeletal components capable of physically anchoring the LH receptor in the membrane, and by interactions of the receptor with other membrane proteins. We are interested in determining how these features are involved in regulating functions of reproductive organs.

I also use single particle tracking to determine how LH receptors are distributed on single cells and biochemical methods to identify other cell membrane proteins that interact with LH receptors. Such interactions may be necessary for regulating hormone secretion by hormone-responsive cells.

Representative Publications

For a complete list of publications, please visit: DA Roess PubMed

Roess DA, Horvat RD, Munnelly H, Barisas BG. 2000. Hormone receptors are self-associated in the plasma membrane. Endocrinology 141:4518-4523.

Horvat RD, Barisas BG, Roess DA. 2001. Luteinizing hormone receptors are present in slowly diffusing complexes during receptor desensitization. Molec Endocrinol 15:534-542.

Hunzicker-Dunn ME, Barisas BG, Song J, Roess DA. 2003. Membrane organization of luteinizing hormone receptors differs between actively signaling and desensitized receptors. J Biol Chem 278:42744-42749.

Roess DA, Smith SML. 2003. Self-association and raft localization of functional luteinizing hormone receptors. Biol Reprod 69:1765-1770.

Lei Y, Hagen GM, Smith SML, Barisas BG, Roess DA. 2005. Chimeric GnRH-LH receptors and LH receptors lacking C-terminus palmitoylation sites do not localize to plasma membrane rafts. Biochem Biophys Res Comm 337:430-434.

Smith SML, Lei Y, Liu J, Cahill ME, Hagen GM, Barisas BG, Roess DA. 2006. Luteinizing hormone receptors translocate to plasma membrane microdomains following binding of human chorionic gonadotropin. Endocrinology 147:1789-1795.

Lei Y, Hagen GM, Smith SML, Liu J, Barisas G, Roess DA. 2007. Constitutively-active human LH receptors are self-associated and located in rafts. Molec Cell Endocrinol 260-262:65-72.