Institute for Medicine and Engineering

The mission of the Institute for Medicine and Engineering (IME) is to stimulate fundamental research at the interface between biomedicine and engineering/physical/computational sciences leading to innovative applications in biomedical research and clinical practice. The IME was created in 1996 by the Schools of Medicine (SOM) and Engineering and Applied Science (SEAS) to pursue opportunities for collaborative research. The IME has been successful in obtaining over $80 million in extramural grants, and funded programs. These include a research center in Cell Studies of Pulmonary Artery Hypertension, and a Penn Center for Molecular Discovery.

Membership: The Institute houses 11 core faculty, 6 from the School of Medicine and 5 from SEAS, who were recruited to form the basis for the IME; however, the Institute extends beyond the core group to include 106 members from various schools including School of Medicine, SEAS and Arts and Sciences faculty. The Institute interacts with 24 other Centers or departments.

Multi-disciplinary Research: The IME mission to foster research at the interface of medicine and engineering is met (i) through 8 central investigators who span these disciplines in both schools, (ii) through the core facilities, pilot grant programs, research training, and educational events involving its very wide membership (of 106). The research conducted by central investigators is quite broad, ranging from cell and molecular biology to tissue engineering, biophysics and nanobiology/medicine. Having established a strong basic research foundation the Institute is now expanding translational programs in medicine and engineering.

Strategic Importance: The IME relates directly to 3 major themes of the SOM Research Strategic Plan: Cancer, Neurosciences and Cardiovascular Biology. The University Strategic Plan identifies the link between engineering and medicine as one of the key drivers of success and recommends "fostering advances in engineering, computing, chemistry, mathematics and behavioral sciences that can be applied to life sciences." Because of the multi-disciplinary nature of the Institute, it is well positioned to take advantage of the new NIH roadmap. Because of its unique interface with SEAS, the IME is a strong force in faculty retention by providing unique directions and connections for research among faculty.





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  • Publication
    α6ß4 integrin regulates keratinocyte chemotaxis through differential GTPase activation and antagonism of α3ß1 integrin
    (2003-09-01) Russell, Alan J; Fincher, Edgar F; Millman, Linda; Smith, Robyn; Vela, Veronica; Waterman, Elizabeth A.; Dey, Clara N; Weaver, Valerie M.; Weaver, Valerie M.; Marinkovich, Matthew P
    Growth factor-induced cell migration and proliferation are essential for epithelial wound repair. Cell migration during wound repair also depends upon expression of laminin-5, a ligand for α6ß4 integrin. We investigated the role of α6ß4 integrin in laminin-5-dependent keratinocyte migration by re-expressing normal or attachment-defective ß4 integrin in ß4 integrin null keratinocytes. We found that expression of ß4 integrin in either a ligand bound or ligand unbound state was necessary and sufficient for EGF-induced cell migration. In a ligand bound state, ß4 integrin supported EGF-induced cell migration though sustained activation of Rac1. In the absence of α6ß4 integrin ligation, Rac1 activation became tempered and EGF chemotaxis proceeded through an alternate mechanism that depended upon α3ß1 integrin and was characterized by cell scattering. α3ß1 integrin also relocalated from cell-cell contacts to sites of basal clustering where it displayed increased conformational activation. The aberrant distribution and activation of α3ß1 integrin in attachment-defective ß4 cells could be reversed by the activation of Rac1. Conversely, in WT ß4 cells the normal cell-cell localization of α3ß1 integrin became aberrant after the inhibition of Rac1. These studies indicate that the extracellular domain of ß4 integrin, through its ability to bind ligand, functions to integrate the divergent effects of growth factors on the cytoskeleton and adhesion receptors so that coordinated keratinocyte migration can be achieved.