Ph. D., University of Denver; 1994

   

Office:     411 Life Sciences Building

Phone:   1-419-372-9156

Email:     tcsteve@bgsu.edu

   

Research:

Protein Biochemistry; Molecular Neuroendocrinology; Cell Biology; Protein Trafficking

   

 

   

Research Interests:

My research interests focus on examining the cellular and molecular mechanisms of how copper, an essential element, is regulated and transported into vesicles for incorporation into enzymes that function in the secretory pathway of neuroendocrine cells. Copper is required for the normal function of several important enzymes and excess copper is highly toxic. Therefore, copper homeostasis is carefully regulated. Wilson's Disease and Menkes Disease, two disorders characterized by disturbances in copper homeostasis, are caused by mutations in P-type copper transporter ATPases. Currently, I am analyzing the expression, biosynthesis, subcellular distribution and trafficking of the Menkes ATPase using rat/mouse pituitary to determine how the endogenous Menkes ATPase functions in cells that synthesize copper requiring enzymes.

Selected Publications:

Steveson, T.C., G.D. Ciccotosto, X.M. Ma, G.P. Mueller, R.E. Mains and B.A. Eipper. 2003. Menkes protein contributes to the function of Peptidylglycine a-Amidating Monooxygenase. Endocrinology, 144:188-200.

Alam, M.R., T.C. Steveson, R.C. Johnson, N. Bäck, B. Abraham, R.E. Mains, and B.A. Eipper. 2001. Signaling mediated by the cytosolic domain of Peptidylglycine a–Amidating Monooxygenase. Mol. Biol. Cell, 12:629-644.

Oyarce, A.M., T.C. Steveson, L. Jin and B.A. Eipper. 2001. DBM signal/anchor sequence alters trafficking of Peptidylglycine a-Hydroxylating Monooxygenase. J. Biol. Chem., 276:33265-33272.

Steveson, T.C., G.C. Zhao, H.T. Keutmann, R.E. Mains and B.A. Eipper. 2001. Access of a membrane protein to secretory granules is facilitated by phosphorylation. J. Biol. Chem., 276:40326-40337.

Steveson, T.C., H.T. Keutmann, R.E. Mains and B.A. Eipper. 1999. Phosphorylation of cytosolic domain Ser937 affects both biosynthetic and endocytic trafficking of Peptidylglycine a-Amidating Monooxygenase. J. Biol. Chem., 274:21128-21138.

Steveson, T.C. and R.M. Dores. 1996. POMC-related products in the intermediate pituitary of the amphibian, Bufo marinus: Differential subcellular processing in the Golgi and secretory granules. Peptides, 17:425-434.

Dores, R.M., K.E. Gieseker and T.C. Steveson. 1994. The posttranslational modification of ß-endorphin in the intermediate pituitary of the toad, Bufo marinus, includes processing at a monobasic cleavage site. Peptides, 15:1497-1504.

Dores, R.M., H. Wasinger, D. Vaudry, T. Steveson and A. Lancha. 1993. The melanotropes of the lizard, Anolis carolinensis, lack N-acetylating mechanisms for both a-MSH and ß-endorphin. Neuroendocrinol., 59:603-609.

Dores, R.M., T. Truong and T.C. Steveson. 1992. Detection and partial characterization of proopiomelanocortin-related end-products from the pars intermedia of the toad, Bombina orientalis. Gen. Comp. Endocrinol., 87:197-207.

Dores, R.M., T.C. Steveson and K. Lopez. 1991. Differential mechanisms for the N-acetylation of a-MSH and ß-endorphin in the intermediate pituitary of the frog, Xenopus laevis. Neuroendocrinology, 53:54-62.

Dores, R.M., L.K. McDonald, T.C. Steveson and C.A. Sei. 1990. The molecular evolution of neuropeptides: prospects for the 90's. Brain Behav. Evol., 36:80-99.

Steveson, T.C., C.L. Jennett and R.M. Dores. 1990. Detection of N-acetylated forms of ß-endorphin and non-acetylated a-MSH in the intermediate pituitary of the toad, Bufo marinus. Peptides, 11:797-803.

Dores, R.M., T.C. Steveson and J. Joss. 1988. The isolation of multiple forms of ß-endorphin from the intermediate pituitary of the Australian lungfish, Neoceratodus forsteri. Peptides, 9:801-808.