Philip Board


BoardPhilip Board gained a BSc with First Class Honours in Physiology in 1972 at the University of New England and completed a PhD at the same university in 1976. He then took a postdoctoral position in the Department of Pathology at Kansas State University where he investigated the causes of glutathione deficiency. In 1979, Philip returned to Australia and was appointed a Research Fellow in the John Curtin School of Medical Research. He was appointed Professor in 1994 and Head of the Division of Molecular Medicine in 1998.

Philip has had broad research interests including investigations of red blood cell metabolism and blood coagulation and has studied the structure and function of a range of enzymes that synthesise or utilise glutathione. Philip has supervised 18 PhD students and published 225 papers in international journals and books.

In the 1980s and 1990s Philip pioneered the biochemical genetic analysis of coagulation factor XIII deficiency. He developed novel techniques that allowed the characterisation of abnormal forms of factor XIII that cause deficiency, and made the novel observation that the A and B subunits of plasma Factor XIII are synthesised in different tissues. Philip was the first to identify specific deficiency causing mutations and undertook the first prenatal diagnosis for Factor XIII deficiency. For his early work on Factor XIII, Philip was awarded the Albert Baikie Medal by the Haematology Society of Australia. His most substantial contributions have been in the molecular and structural analysis of the glutathione transferase (GST) isoenzymes. In early studies Philip discovered the common deficiency of GSTM1 that has subsequently been associated with susceptibility to a range of diseases and responses to chemotherapy.

The Board laboratory has been responsible for the cloning and characterisation of a wide range of glutathione transferase cDNAs and their corresponding genes. The successful expression of recombinant GSTs in his laboratory in the mid-1980s opened the way for their extensive molecular analysis. Collaborations with several crystallographers including Michael Parker in Melbourne resulted in the characterisation of the crystal structure and function of members of the Alpha, Delta, Theta, Zeta and Omega classes of GSTs.

In recent years, Philip has exploited the rapidly expanding sequence databases to identify several new members of the glutathione transferase structural family. These studies identified the Zeta and Omega class GSTs that play novel roles in the metabolism of tyrosine and arsenic. In a further expansion of the GST structural family, Philip and colleagues at the JCSMR, including Angela Dulhunty, Peter Gage and Gareth Chelvanayagam, showed that the family of chloride intracellular channel proteins (CLIC proteins) are structurally related to the Omega class GSTs. This observation subsequently lead to the discovery that some members of the GST family are potent modulators of ryanodine receptor calcium release channels.