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Edmond Fischer
Edmond Fischer

Emeritus Professor of Biochemistry

efischer[at]uw.edu

Honors

1992 Nobel Prize in Physiology or Medicine, with fellow Biochemistry Professor Edwin Krebs

1952 Werner Medal, Swiss Chemical Society
1956-1959 Lederle Medical Faculty Award
1963-1964 Guggenheim Foundation Award
1963-1964 Special Fellowship Award, NIGMS, NIH
1968 Prix Jaubert, University of Geneva
1972 American Academy of Arts and Sciences
1973 National Academy of Sciences
1988 Senior Passano Foundation Award, Baltimore
1991 Steven C. Beering Award
1993 Spanish Royal Academy of Sciences, Foreign Associate
1994 Venice Academy of Sciences, Arts and Letters, Italy
1994 Honorary Member, Japanese Biochemical Society
1998 Royal Academy of Medicine and Surgery, Cadiz, Spain
1998 Honorary Member, Faculty of Medicine of Cadiz, Spain
1998 Bert and Kugie Vallee Visiting Professor, Harvard Univ
1998 Honorary Member, Pediatria Extrahospitalaria de Cadiz
2000 Korean Academy of Science and Technology, Seoul, Korea
2004 European Academy of Sciences
2004 Honorary Professor, Jilin University, Changchun, China
2004 Honorary Director, "Edmond H. Fischer Signal Transduction Laboratory", Jilin University, Changchun, China
2004 Honorary Professor, Hunan Normal University, Changsha
2005 Lifetime Achievement Award, Miami Winter Symposium
2007 Honorary Citizen, City of New Orleans
2008 Washington State Academy of Sciences
2009 Medal of the International Union of Biochemistry and Molecular Biology
2010 Foreign Member, The Royal Society

Research

This group has been mainly concerned with the regulation of cellular processes by protein phosphorylation, particularly tyrosine phosphorylation. Tyrosine phosphorylation has been implicated in cell growth, proliferation, differentiation and transformation initiated by tyrosine kinases of cellular or viral origin, or linked to hormones and growth factor receptors. Of major interest has been the structure and function of protein tyrosine phosphatases (PTPs) required to catalyze the reverse reaction. Several members of this diverse family of enzymes have been isolated in homogeneous form from various tissues, cloned from various libraries and expressed in different cell types. They represent both transmembrane receptor forms and intracellular enzymes; they are homologous in terms of their catalytic domains but vary greatly in the structure and function of their non-catalytic segments. Special attention is being paid to a family of intracellular PTPs having two SH2 (src-homology 2 domains). Efforts are being made to determine their involvement in signal transduction, sytoskeletal reorganization and cell cycle regulation. Depending on the form of enzyme involved, PTP can act synergistically or antagonistically with the tyrosine kinases in either promoting or preventing neoplastic transformation.

Selected Publications

Purification and Characterization of a Protein Tyrosine Phosphatase Containing SH2 Domains,” Z. Zhao, P. Bouchard, C.D. Diltz, S-H Shen and E.H. Fischer, J. Biol. Chem, 268, 2816 (1993).

“Suppression of v-fms-induced transformation by overexpression of a truncated T-cell protein tyrosine phosphatase,” Zander, N.F., Cool, D.E., Diltz, C.D., Rohrschneider, L.R., Krebs, E.G. and Fischer, E.H. Oncogene, 8, 1175 (1993).

“Multiple Forms of the Human Tyrosine Phosphatase RPTP alpha”, G. Daum, S. Regenass, J. Sap, J. Schlessinger and E.H. Fischer, J. Biol. Chem., 269, 10524 (1994).

“Phorbol ester-induced expression, phosphorylation and translocation of protein-tyrosine-phosphatase 1C in HL-60 cells,” Z. Zhao, S-H Shen and E.H. Fischer, Proc. Natl. Acad. Sci. USA, 91, 5007 (1994).

“Identification and Purification of a Chicken Brain Neuroglia-associated Protein,” F.F. Solca, D.I. Lurie, C.D. Diltz, R.S. Johnson, S. Kuman, E.W. Rubel and E.H. Fischer, J. Biol. Chem., 269, 27559 (1994).