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Faculty Detail Faculty Entry   
Name ANDREW JAMES PATERSON  
Campus Address BDB 767 Zip 0012
Phone 205-975-8510
E-mail paterson@uab.edu" id="FacultyDetail1EmailAddress"><a href="mailto:paterson@uab.edu">paterson@uab.edu</a>
URL
 
 

Department Affiliations(s)
Appointment Type Department Division Rank
Center  Medicine  Comprehensive Diabetes Ctr Assistant Professor
Center  Medicine  Med - Cardiovascular Disease Assistant Professor
Primary  Medicine  Med - Endocrinology, Diabetes & Metabolism Assistant Professor
Secondary  Cell, Developmntl, & Integrative Biology  Cell, Developmntl, & Integrative Biology Assistant Professor

Biographical Sketch 
Andrew James Paterson (b. 1951, Christchurch, New Zealand), citizen of the U.S.A. He received his MSc (Chemistry) from the University of Canterbury in 1975, and a PhD (Biochemistry) from the University of Otago, New Zealand in 1981. In 1981 he joined the postdoctoral fellowship program at the NIH (NCI) for 3 years and then moved to Toronto Canada as Research Associate in Dr Jeffrey Kudlow’s laboratory. In 1989 he came to UAB as Assistant Professor joining the Department of Medicine, Division of Endocrinology, with Dr. Kudlow as division director. He continued work on growth factor regulation and how O-Glycosylation regulates cellular function.

Society Memberships
Organization Name Position Held Org Link
American Physiological Society  Member   
 

Research/Clinical Interest
Title
Role of O-Glycosylation in Gene Regulation, Cell Growth, and Differentiation.
Description
The research in our laboratory is focused on the regulation of cell function by the O-GlcNAc post-translational modification on cellular proteins. We showed that the regulation of transforming growth factor-&#945; gene expression by glucose was linked to the O-GlcNAc status of the ubiquitous transcription factor, Sp1. Thus, glucose-specific O-GlcNAc modification of Sp1 regulated not only TGF-&#945;, 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, I&#954;B, 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. Also, these enzymes have an additional function in that they are able to co-associate to regulate gene transcription. In particular, we showed in cell culture that nuclear hormone receptors could be suppressed or activated depending on the O-GlcNAc status of transcription factors, and that mammary tissue development was retarded in a transgenic mouse model through the suppression of estrogen receptor-dependent transcription. We have shown physiological function of modifying O-GlcNAc in other tissues, including, brain, eye and muscle, linking the phenotypes to various degenerative diseases.

Postdoc Positions Available
Date Posted Position Title
No records
 

Selected Publications 
Publication PUBMEDID
  22908225 
  21178104 
Ho, S.-R., Wang, K., Whisenhunt, T.R., Huang, P., Zhu, X., Kudlow, J.E., and Paterson, A.J. O-GlcNAcylation enhances FOXO4 transcriptional regulation in response to stress. FEBS Lett 584, 49-54, 2010.  19932102 
Wang, K., Ho, S.R., Mao, W., Huang, P., Zhang, F., Schwiebert, E.M., Kudlow, J.E., and Paterson, A.J. Increased O-GlcNAc causes disrupted lens fiber cell differentiation and cataracts. Biochem Biophys Res Commun 387, 70-76, 2009.  19577582 
Zhang, F., Paterson, A.J., Huang, P., Wang, K., and Kudlow, J.E. Metabolic control of proteasome function. Physiology (Bethesda, Md) 22, 373-379, 2007.  18073410 
Zhang, F., Hu, Y., Huang, P., Toleman, C.A., Paterson, A.J., and Kudlow, J.E. Proteasome function is regulated by cyclic AMP-dependent protein kinase through phosphorylation of Rpt6. J Biol Chem 282, 22460-22471, 2007.  17565987 
Whisenhunt, T.R., Yang, X., Bowe, D.B., Paterson, A.J., Van Tine, B.A., and Kudlow, J.E. Disrupting the enzyme complex regulating O-GlcNAcylation blocks signaling and development. Glycobiology 16, 551-563, 2006.  16505006 
Toleman, C., Paterson, A.J., and Kudlow, J.E. Location and characterization of the O-GlcNAcase active site. Biochim Biophys Acta 1760, 829-839, 2006.  16517082 
Bowe, D.B., Sadlonova, A., Toleman, C.A., Novak, Z., Hu, Y., Huang, P., Mukherjee, S., Whitsett, T., Frost, A.R., Paterson, A.J., and Kudlow, J.E. O-GlcNAc Integrates the Proteasome and Transcriptome To Regulate Nuclear Hormone Receptors. Mol Cell Biol 26, 8539-8550, 2006.  16966374 
Toleman, C., Paterson, A.J., Whisenhunt, T.R., and Kudlow, J.E. Characterization of the histone acetyltransferase (HAT) domain of a bifunctional protein with activable O-GlcNAcase and HAT activities. J Biol Chem 279, 53665-53673, 2004.  15485860 
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Keywords
Transcription factors, gene regulation, proteasome, glycosylation, O-GlcNAc, development, transgenic mice

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