Michael E. Wright, Ph.D.
        Assistant Professor

Office: Lab: Phone: Lab: FAX: Email:

5-630 Bowen Science Building 5-611C Bowen Science Building (319) 384-1764 (319) 384-1765 (319) 335-7330 michael-e-wright@uiowa.edu

Research Interests

Research Mission
My laboratory focuses on defining the composition, activity, and overall cellular function of protein complexes in higher organisms. We utilize state-of-art methods in quantitative mass spectrometry to understand protein network function on a global scale in the normal and diseased state.

Aberrant Androgen Receptor Signaling in Human Prostate Cancer
We are deciphering the molecular mechanisms of aberrant androgen receptor function in the development and progression of androgen-refractory prostate cancer in men. Our long-term goal is to identify novel protein targets of prognostic and therapeutic value to life-threatening forms of androgen-refractory human prostate cancer. We predict effector proteins of aberrant androgen receptor signaling will define a conserved set of genetic modifiers of androgen-refractory prostate cancer in men. We are utilizing quantitative mass spectrometry to define genetic modifiers of aberrant androgen receptor signaling on three biochemical levels. They include: (1) characterizing androgen receptor interacting protein complexes, (2) mapping androgen-mediated phosphorylation cascades, and (3) elucidating androgen-responsive protein networks. Understanding the biochemical relationships between these pathways will also shed light onto how these pathways act individually or synergistically to influence aberrant androgen receptor signaling in hormone-refractory prostate cancer. Our studies will provide an integrated molecular framework to develop and test new hypotheses regarding how aberrant androgen receptor signaling influences the evolution and progression of prostate cancer in men.

Protein Expression Signatures in Diseased Prostate Tissues
Historically it has been difficult to secure sufficient amounts of diseased human tissue to interrogate protein expression patterns in clinically relevant samples. This has posed a serious limitation in the development of robust protein biomarkers of diagnostic, prognostic, or therapeutic value to different human diseases. We are utilizing shotgun proteomic methods via tandem mass spectrometry (MS/MS) to quantify protein expression in formalin-fixed paraffin embedded prostate tissues. Our goal is to identify and validate protein expression signatures in diseased epithelial cells of the prostate gland. We anticipate these studies will define a subset of proteins associated with non-significant and significant forms of human prostate cancer in men.

Selected Publications

coming soon