Andrew James Paterson, PhD

Paterson-andrewAssistant Professor

Dept. of Medicine

Divison of Endocrinology, Diabetes and Metabolism

Contact Information:

Office Address: BDB 767
Phone: 205-975-8510
E-mail: This email address is being protected from spambots. You need JavaScript enabled to view it.
Websites: Division of Endocrinology Faculty Page

Education:

University of Canterbury, Christchurch, New Zealand

BSc, 1973

University of Canterbury, Christchurch, New Zealand

MSc, 1976

University of Otago, Dunedin, New Zealand

PhD, 1981

Post-Graduate Training:

National Institutes of Health, Bethesda, MD

Postdoctoral Fellow, Laboratory of Tumor Immunology, 1982-5

University of Toronto, Canada

Postdoctoral Fellow, Molecular Biology of Growth Factors, 1985-7

Research Interests

Role of O-Glycosylation in Gene Regulation, Cell Growth, and Differentiation.

Research Interest Description

The research in our laboratory is focused on the regulation of cell function by the O-GlcNAc post-translational modification on cellular proteins. Through our specific studies on the regulation of transforming growth factor-α gene expression by glucose, we were able to show that O-GlcNAcylation was involved in transcriptional regulation of genes in general. Thus, glucose-specific O-GlcNAc modification of Sp1 regulated not only TGF-α, but also a multitude of other cytoplasmic and nuclear proteins, including the proteasome, a major protein complex whose function is to get rid of unwanted cellular proteins. Our data showed that increased cellular O-GlcNAc levels reduced proteasome activity, and since some of the important cellular regulatory proteins, such as Sp1, p53, IκB, and the cyclins, are targets of the proteasome, they too can be regulated by glucose. For example, in times of low nutrition (less O-GlcNAc modification), the active proteasome degrades proteins involved in cell propagation (such as Sp1), and processes muscle proteins that are then used as an energy source. Much of our studies have involved the two principle enzymes that regulate the O-GlcNAcylation process; O-GlcNAc transferase (OGT), the enzyme that adds the O-GlcNAc moiety to proteins, and the O-GlcNAcase that removes the modification. By expressing a spliced-variant O-GlcNAcase in transgenic mice, we have demonstrated physiological function by modifying O-GlcNAc in tissues, including, brain, eye and muscle, linking the phenotypes to degenerative diseases.

Publications

DRC Membership Category:

Senior Scientist