Prof. D. James Morré received his doctorate in Biochemistry from the California Institute of Technology in 1963 after which he joined the Faculty of Purdue University. He is currently the Dow Distinguished Professor of Medicinal Chemistry in the Department of Medicinal Chemistry and Molecular Pharmacology. In collaboration with Professor Dorothy Morré he was a major contributor to the base intellectual property upon which NOX Technologies, Inc. was founded. Professor Morré has had considerable expertise in cancer research and research administration. In 2006 Professor Morré was placed in the 95th percentile of (extramural) NIH grants over the last 25 years based on Columbia University study of NIH records.
His interest in cancer research emerged from early focus on a mechanism for control of cell growth involving a cell-surface plasma membrane hydroquinone (NADH) oxidase with protein disulfide-thiol interchange activity (ECTO-NOX or ENOX proteins). The constitutive (CNOX or ENOX1) form of the activity is ubiquitous and is sensitive to stimulation by growth factors and linked to transmembrane signaling.
tNOX or ENOX2 is specific for cancer cells. It is distinguished from CNOX and from other common oxidoreductases activities by differential susceptibility to cytostatic and cytotoxic drugs, all of which have anticancer activity. Inhibited by these same drugs is a protein disulfide-thiol interchange activity also catalyzed by the tNOX protein. The latter bears a direct relationship to the unregulated growth that typifies growth of cancer cells in that when the activity is inhibited, growth also is inhibited. The function of the ECTO-NOX proteins is in the enlargement phase of the cell cycle. When cells divide, they must reach some minimal size in order to divide again. tNOX inhibitors block cancer cell enlargement and the resultant small cells fail to divide. After several days, such growth-inhibited cells undergo apoptotic cell death.
As ectoproteins of the cell surface, ENOX proteins are shed into culture media and into the circulation. The circulating form of the tNOX protein has the same response characteristics to inhibitors and antitumor agents as does the cell-surface form and together with the cell surface form exhibits characteristics of a universal oncoprotein suitable for development of molecular diagnostic and therapeutic reagents.
Underway at NOX Technologies, Inc. is a major translational effort to bring the diagnostic potential of the tNOX target into clinical utility. Prof. Morré’s continued input is critical to the continued advance of the ENOX program. He is not only highly qualified to provide scientific oversight to the project but also highly committed to ensuring the Company’s continued success.
D. James Morré Dow Distinguished Professor of Medicinal Chemistry Department of Medicinal Chemistry and Molecular Pharmacology Purdue University Room 136A Hansen Life Sciences Research Building 201 South University Street West Lafayette, IN 47907-2064 Phone: (765) 494-1388 FAX: (765) 494-4007 Email: morre@pharmacy.purdue.edu
SELECTED PUBLICATIONS OF PROF. D. JAMES MORRÉ
Encio, I., D. J. Morré, R. Villar, M. J. Gil and V. Martinez-Merion. 2005. Benzo[b]thiophenesulphonamide 1,1-dioxide derivatives inhibit tNOX activity in a redox state dependent manner. Br. J. Cancer 92: 690-695.
De Luca, T., D. M. Morré, H. Zhao and D. J. Morré. 2005. NAD+/NADH and/or CoQ/CoQH2 ratios from plasma membrane electron transport may determine ceramide and sphingosine-1-phosphate levels accompanying G1 arrest and apoptosis. BioFactors 25: 43-60.
Yagiz, K., D. J. Morré and D. M. Morré. 2006. Transgenic mouse line overexpressing the cancer-specific tNOX protein has an enhanced growth and acquired drug-response phenotype. J. Nutr. Biochem. 17:750-759
Jiang, Z., D. M. Morré and D. J. Morré. 2006. A role for copper in biological time-keeping. J. Inorg. Biochem. 100: 2140-2149.
Hicks-Berger, C., I. Sokolchik, C. Kim and D. J. Morré. 2006. A plasma membrane-associated AAA-ATPase from Glcine max. BioFactors 28: 135-149.
Morré, D. J.. P.-J. Chueh, Kader Yagiz, Andrew Balicki, Chinpal Kim and D. M. Morré. 2007. ECTO-NOX target for the anticancer isoflavene phenoxodiol. Oncol. Res. 16: 299-312.
Morré, D. J., S. Heald, J. Coleman, J. Orczyk, Z. Zhang and D. M. Morré. 2007. Structural observations of time dependent oscillatory behavior of copper (II) chloride solutions measured via extended X-ray absorption fine structure. J. Inorg. Biochem. 101: 715-726.
Yagiz, K., L.-Y. Wu, C.P. Kuntz, D. J. Morré and D. M. Morré. 2007. Mouse embryonic fibroblast cells from transgenic mice overexpressing tNOX express an altered growth and drug response phenotype. J. Cell. Biochem. 101: 295-306.
Tang, X., Z. Tian, P.-J. Chueh, S. Chen, D. M. Morré and D. J. Morré. 2007. Alternative splicing as the basis for specific localization of tNOX, a unique hydroquinone (NADH) oxidase, to the cancer cell surface. Biochemistry 46: 12,337-12,346.
Morré, D. J. and H. H. Mollenhauer. 2007. Microscopic morphology and the origins of the membrane maturation model of Golgi apparatus function. Int. Rev. Cytol. 262: 191-218.