Leukaemia Foundation

Andrew Boyd
Staff
Collaborators
Student Projects
Key Recent Publications
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Lab Head: Prof Andrew Boyd

The Leukaemia Foundation laboratory is exploring the biology of leukaemia and other cancers through studies of leukaemia-associated proteins. A major project is to understand the function of Eph and ephrin membrane proteins in cancer. When Eph and ephrin proteins on adjacent cell bind together they initiate bi-directional signals which affect the cytoskeleton and adhesion proteins resulting in de-adhesion and contact repulsion. Recent studies have highlighted the role of these processes in the normal events of embryonic development. Members of these protein families are highly expressed in many human cancers where, by actively promoting de-adhesion of cells, they contribute to tumour spread and invasion. We are exploring how these proteins function in a number of cancers through work in animal models and through in vitro studies. In pre-clinical models we have shown that both antibodies which target Eph proteins and soluble forms of their ephrin ligands can be used to target tumours and inhibit tumour growth. These are being developed as potential therapeutics for leukaemia and other human cancers.

We are also studying an adhesion protein called Fat. This protein is abnormally expressed in some forms of T cell leukaemia and we have recently shown that these abnormal forms inhibit the normal Fat protein, resulting in abnormal cell movement and altered tissue morphology. By understanding the function of the truncated Fat protein we hope to determine how it contributes to leukaemia and related cancers and to devise therapies which attack the cancer cells through the targeting of the Fat proteins.

Leukaemic-associated Proteins

Staff

Labhead:	Professor Andrew Boyd (leukaemia genes)
Post-doctoral scientists:	Dr Nirmitha Herath (Eph receptors in cancer) Dr Jason Lickliter (Bcl2 in cancer) Dr Mark Spanevello (Eph/ephrin expression in disease) Dr Brett Stringer (Gene regulation) Dr Trina Yeadon (CD44 in cancer)
Research Assistants:	Ke Chen Joanne Cox Bryan Day Bridget Douglas Michelle Down Jenny McCarron Jenny Reeder Melissa Scott Fiona Smith
Post Graduate Students:	Mark Coulthard Shannon Duffy Eugene Lau Con Stylianou Michael Ting

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Collaborators

Dr Martin Lackmann, Dept of Biochemistry, Monash University
Prof Gordon Burns, Dept of Biochemistry, University of Newcastle
Professor Perry Bartlett, Brain Research Institute, University of Queensland
Dr Dimitar Nikolov, Memorial Sloan Kettering Institute, New York
Dr Bing Wang, Case Western Reserve University, Cleveland, Ohio

Student Projects

Inquiries are welcome for graduates in science, medicine or other health-related areas to undertake projects leading to BSc(Hons), MMedSc, MSc, PhD or MD in any of the above areas.

Key Recent Publications

Day, B, To, C, Himanen, J-P, Smith, FM, Nikolov, DB, BOYD, AW, Lackmann, M. Three distinct molecular surfaces in ephrin-A5 are essential for a functional interaction with EphA3. J.Biol.Chem. 280:26526-26532; 2005. [pubmed abstract]

Down, LM, Power, M, Smith, SI, Ralston, K, Spanevello, M, Burns, GF, BOYD, AW. Cloning and expression of the large zebrafish protocadherin gene, Fat. Gene Expr. Patterns 5:483-90;2005. [pubmed abstract]

Vearing, C, Lee, FT, Wimmer-Kleikamp, S, Spirkoska, V, To, C, Styllianou, C, Spanevello, M, Brechbiel, M, BOYD, AW, Scott, A, Lackmann, M. Concurrent binding of anti-EphA3 antibody and ephrin A5 amplifies EphA3 signalling and downstream responses: potential as EphA3-specific tumour targeting reagents. Cancer Res. 65:6745-54; 2005. [pubmed abstract]

Himanen J, Chumley MJ, Lackmann M, Li C, Barton WA, Jeffrey PD, Vearing, C, Geleick, D, Feldheim DA, BOYD AW, Henkemeyer M, Nikolov D. Repelling Class Discrimination: EphrinA5 Binds the EphB2 Receptor and Activates EphB2 receptor signaling. Nature Neurosci. 7:501-9; 2004. [pubmed abstract]

Smith FM, M Lackmann, C Vearing, H Treutlein, J Himanen, K Chen, D Nikolov & BOYD AW. Dissecting the EphA3/Ephrin-A5 interactions using a novel functional mutagenesis screen. J Biol Chem 279:9522-31; 2004. [pubmed abstract]

BOYD, AW, Lackmann, M. Signals from Eph and ephrin proteins: A developmental toolkit. Science's STKE (2001), [on-line]

Coulthard MG, Lickliter JD, Subanesan N, Chen K, Lowry AJ, Webb GC, Koblar S, Bottema CDK, Boyd, AW Characterization of the EphA1 receptor tyrosine kinase: expression in epithelial tissues. Growth Factors 18:303-317;2001. [pubmed abstract]

Kullander, K, Mather, NK, Diella, F, Dottori, M, Boyd, AW & Klein, R Kinase-dependent and kinase-independent functions of EphA4 in major axon tract formation in vivo. Neuron 29:73-84; 2001. [pubmed abstract]

Davis, ID, Maher, DW, Cebon, JS, Green, MD, Fox, RM, McKendrick, JJ, Rybak, ME & Boyd AW Phase I and pharmacokinetic study of subcutaneously administered recombinant human interleukin-4(rhu-IL-4) in patients with advanced cancer. Growth Factors 17:287-300;2000. [pubmed abstract]

Smith, SI, Down, M, Boyd, AW & Li, CL. Expression of the Wilm’s Tumor Supressor Gene, WT1, reduces the tumorigenicity of the leukemic cell line M1 in C.B-17 scid/scid mice. Cancer Res 60:808-814; 2000. [pubmed abstract]

Oates, AC, Lackmann,M, Power, M, Brennan, C, Down M, Do, C, Evans,B, Holder, N & Boyd, AW An early developmental role for Eph-ephrin interaction during vertebrate gastrulation. Mech. Dev. 83:77-94;1999. [pubmed abstract]

Dottori, M, Down, M, Hüettmann, A, Fitzpatrick, DR & Boyd, AW Cloning and characterization of the EphA3 gene promoter: DNA methylation regulates expression in hemopoietic tumor cells. Blood 94:2477-2486;1999. [pubmed abstract]

Dottori, M, Hartley, L, Galea, M, Paxinos, G, Polizzotto,M, Kilpatrick, T, Bartlett, PB, Murphy, M, Köntgen, F & BOYD, AW. EphA4 (Sek1) receptor tyrosine kinase is required for the development of the corticospinal tract. Proc. Natl. Acad. Sci. USA 95:13248-53; 1998. [pubmed abstract]

Lackmann,M, Oates, A, Dottori, M, Power, M, Smith, FM, Do, C, Kravets, L, & BOYD, AW Distinct subdomains of the EphA3 receptor mediate ligand binding and receptor dimerisation. J. Biol. Chem. 273:20228-37; 1998 [pubmed abstract]