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Dr John E Hunt
School of Medical Sciences
University of New South Wales
Sydney, NSW 2052
Email: J.Hunt@unsw.edu.au
Tel: +61-2-9385-1580
Fax: +61-2-9385-1389

Our research interests centre on the biology of the mast cell proteases. Mast cells are highly granulated effector cells of the immune system that may be recruited during an inflammatory response. Following activation they secrete a variety of preformed mediators including histamine, proteoglycans, and a range of serine proteases. These proteases comprise two major families, chymases and tryptases, and represent the major protein component of mast cell granules. Much of what is known about the biology of these gene families comes from our studies in the mouse. We previously cloned the genes and cDNAs of four mouse mast cell proteases (mMCPs), and examined their substrate specificity, in vivo function, and factors that controlled their expression. We also used these protease genes as markers to follow the development and fate of mast cells following an inflammatory response. Recently we have focused on the biology of human tryptases. Although mast cells produce many pro-inflammatory molecules there has been an increasing appreciation of the role of mast cell tryptases in various inflammatory diseases. This has resulted in the use of tryptase inhibitors to successfully treat patients with asthma and inflammatory bowel disease We have discovered and cloned a number of new human tryptases, including delta tryptase. We are currently studying its substrate specificity, in vivo function, and association with various inflammatory diseases.
Prof. Ahsan Husain, University of Alabama, USA
Ass Prof. H. Patrick McNeil, Prince of Wales Hospital, NSW, Australia,
Prof K. Frank Austen, Harvard Medical School, USA.
Wang H-W, McNeil HP, Husain A, Liu K, Tedla N, Thomas PS, Raftery M, King GC, Cai ZY, Hunt JE. d-tryptase is expressed in multiple human tissues and a recombinant form has proteolytic activity. J.Immunol.2002;169:5145-5152

Hunt JE, Stevens RL, Austen KF, Zhang J, Xia Z, and Ghildyal N. Natural Disruption of the Mouse Mast Cell Protease 7 (mMCP-7) gene in the C57BL/6 Mouse. J. Biol. Chem. 1996, 271(5):2851-2855.

Hunt JE, Friend DS, Gurish MF, Feyfant E, Sali A, Huang C, Ghildyal N, Stechshulte S, Austen KF and Stevens RL. Mouse Mast Cell Protease 9, a Novel Member of the Chromosome 14 Family of Serine Proteases that is Selectively Expressed in Uterine Mast Cells. J. Biol Chem. 1997, 272: 29158-29166.

Huang C, Li L, Krilis SA, Chanasyk K, Tang Y, Li Z, Hunt JE, and Stevens RL. Human Tryptases alpha and beta are functionally distinct, due in part to a single amino acid difference in one of the surface loops that forms the substrate binding cleft. J. Biol Chem. 1999, 274: 19670-19676.

Friend DS, Gurish MF, Hunt JE, Austen KF, and Stevens RL. Senescent Jejunal Mast Cells and Eosinophils Preferentially Translocate to the Spleen and Draining Lymph Nodes, Respectively, During the Recovery Phase of Helminth Infection. J. Immunology. 2000 165. 344-352.

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