University Directory

Suzanne K. Murphy, PhD

Professor
Dean Emeritus, Misher College of Arts and Sciences

Suzanne Murphy PhD

Department

Office

STC, Room 346

Phone

215-596-8921
Contact

Previous work in Dr. Murhy's lab has focused on understanding how medullary cells of the kidney function in an environment of severe osmotic stress. Renal medullary cells normally exist in a hypertonic environment and can tolerate acute osmotic stress at 830 mOsm. Following RNAi mediated knock down of HSP-70, she observed at least a 50% reduction in the viability of medullary cells subjected to acute osmotic stress, suggesting a role for HSP70 in osmotic stress tolerance. Further work has focused on the role of HSP-70 and other HSPs in the adaptation of medullary cells to osmotic stress.

Osmotic stress and cytoskeletal rearrangement in hematopoietic stem cells
Another earlier project in Murphy's lab focused on the effects of osmotic stress on the cytoskeletal arrangement of human hematopoietic (KG1a) cells. She found that in response to hypertonic stress KG1a cells extrude filopodia. The lab also analyzed p38MAPk and heat shock protein-27 (HSP-27) regulation of hypertonic stress induced filopodia formation in KG1a cells.

HSP involvement in cancer progression
More currently, the lab has focused on the role HSPs play in cancer progression. Cancer cells are under a constant state of stress due to aberrant metabolism, chaotic signal transduction, and exposure to chemotherapeutic agents. As a result, cancer cells become dependent on proteins such as HSPs for viability, resistance to chemotherapy, and to escape anoikis in order to metastasize. Therefore, it is no surprise clinical studies have shown increased expression of HSPs correlates with poor prognosis.

One of Murphy's current projects is focused on elucidating the role of HSPs in bestowing resistance to chemotherapeutic agents in Ras transformed lung carcinomas. Her preliminary findings have shown that cancer cells with the ability to survive exposure to the chemotherapeutic agent cisplatin have an increased expression of HSP-27 phosphorylated at serine 82. Work is in progress to determine the effects that phosphorylated HSP-27 has on impairing apoptosis in these chemoresistant cells.

Another cancer related project in Murphy's lab is focused on the role HSPs play in helping Ras transformed lung carcinomas escape anoikis, which is crucial for the ability of cancer cells to metastasize. Her preliminary findings have shown a dramatic increase in the expression of HSP-70 in these cells when grown in suspension. Work is underway to determine if the anti-apoptotic properties of HSP-70 are involved in helping lung carcinomas survive in suspension and escape anoikis.

    • B.A., Rosemont
    • PhD, Hahnemann
    • Post-Doctoral Fellowship, SmithKline and Beckman Laboratories Corp.Department of Tumor Biology
    • Post-Doctoral Fellowship, Albert Einstein Medical Center Department of Pediatrics

  • Misher College of Arts and Sciences, University of the Sciences in Philadelphia, P.A.

    • Dean, 2009-2018
    • Interim Dean, 2007-2009
    • Associate Dean, 2005-2007

    Department of Biological Sciences, University of the Sciences in Philadelphia, P.A.

    • Professor, 1999-present
    • Associate Professor, 1991-1999
    • Assistant Professor, 1985-1991
    • Graduate Faculty, 1985-present
    • Director of Undergraduate Programs, 2002-2006
    • Interim Co-Chair, 2001-2002 and 2003-200

    Department of Physical Therapy (Joint Appointments), University of the Sciences in Philadelphia, P.A.

    • Professor, 1999-2007
    • Associate Professor 1991-1992

    Weston Institute, West Chester, PA

    • Adjunct Associate Professor. 1991-1992
    • Adjunct Assistant Professor, 1989-1991

  • Academic Appointments
    Misher College of Arts and Sciences, University of the Sciences in Philadelphia, P.A.

    • Dean, 2009-2018
    • Interim Dean, 2007-2009
    • Associate Dean, 2005-2007

    Department of Biological Sciences, University of the Sciences in Philadelphia, P.A.

    • Professor, 1999-present
    • Associate Professor, 1991-1999
    • Assistant Professor, 1985-1991
    • Graduate Faculty, 1985-present
    • Director of Undergraduate Programs, 2002-2006
    • Interim Co-Chair, 2001-2002 and 2003-200

    Department of Physical Therapy (Joint Appointments), University of the Sciences in Philadelphia, P.A.

    • Professor, 1999-2007
    • Associate Professor 1991-1992

    Weston Institute, West Chester, PA

    • Adjunct Associate Professor. 1991-1992
    • Adjunct Assistant Professor, 1989-1991

    Memberships in Professional Organizations

    • American Society for Cell Biology
    • American Association for the Advancement of Science
    • Sigma Xi
    • National Association of Advisors for the Health Professions
    • (member Board of Directors 2000-2002, Secretary 2002-2007)
    • Northeast Association of Advisors for the Health Professions
    • (member of Executive Board 1996-2000, President 2000-2001)
    • Association for Women in Science
    • Association for Women in Cancer Research
    • Honorary Alumnus Award, University of the Sciences; 2013
    • Homiller Award for Outstanding Teaching; 2002
    • Alpha Chi Award for Outstanding Science Professor; 1994
    • Alpha Lambda Delta Award for Outstanding Freshman Professor; 1993
    • Advisor Recognition Award for Outstanding Performance in the Developmental Academic Advisory Program; 1990
    • The Christian R. and Mary F. Lindback Foundation Award for Distinguished Teaching; 1988
    • Faculty Special Recognition Award; 1987

  • (* indicates undergraduate student)

    (** indicates graduate student)

    • A.Chakraborty**, S.K. Murphy and N. Coleman. “The Role of NMDA Receptors in Neural Stem Cell Proliferation and Differentiation.” Stem Cells & Development, 26: 798-807 (2017).
    • P.F. Wilkinson**, F.X. Farrell, D.W. Morel, W.R. Law and S.K. Murphy. “Adenosine Signaling Increases Proinflammatory and Profibrotic Mediators Through Activation of a Functional Adenosine 2B Receptor in Renal Fibroblasts.” Annals of Clinical & Laboratory Science, 46: 247-253 (2016).
    • Jack Carter and Suzanne K. Murphy. “Heat Shock Transcription Factor-1 and Heat Shock Protein60 Are Important for Lung Carcinoma Anoikis Resistance.” Proceedings of the American Association for Cancer Research (2014).
    • Patrick Flynn, Jessica Byerly**, Tracy Berner*, Suzanne K. Murphy. “Caspase 8 Cleavage Is Inhibited Downstream of P38 MAPK in Cisplatin Resistant Cells” Molecular Biology of the Cell." 22, 1904 (2011).
    • H. Tyagi, J. Byerly**, J. Carter*, S. Merchant*, M.R. Kasschau and S.K. Murphy. “Osmotic Stress Response of Kidney Cells Following the RNAi Mediated Knock-down of Hsp70.” Molecular Biology of the Cell. 21, 2395 (2010).
    • Jack Carter*, Priyanka Patel**, Mahasweta Dutt**, Himani Tyagi, Jessica Byerly**, Margaret Kasschau,and Suzanne K Murphy. ”Hypertonic Stress Induced Filopodia Formation Is Regulated by P38MAPk and Hsp27 in Human Acute Myelogenous Leukemic Cell Line Kg1a.” Molecular Biology of the Cell. 21, 1134 (2010).
    • P. Patel**, H. Tyagi, J. Carter*, M. Dutt**, M. R. Kasschau and S. K. Murphy. “Filopodia Formation on Exposure to Hypertonic Stress Is Regulated by Hsp27 and P38 MAPK in Acute Myelogenous Leukemic Cell Line Kg1a.” Molecular Biology of the Cell. 20,1117 (2009).
    • P. Patel, H. Tyagi, A. Khanna, M. Kasschau and S. Murphy. “Role of P38MAPK and Heat Shock Proteins, HSP27 and HSP70, in Osmotic Stress in Renal Vs. Blood Cells: A Comparative Study.” Molecular Biology of the Cell,19, 0361 (2008).
    • P. Patel, M. Dutt, M.R. Kasschau and S.K. Murphy. “Effect of P38MAPK on Filopodial Formation in KGla Human Hemotopoietic Cell Line.” Molecular Biology of the Cell, 18, 169 (2007).
    • "Formation in a Human Hematopoietic Cell Line under Hypertonic Stress.” Molecular Biology of the Cell, 17, 2361 (2006).
    • A. Khanna, M.R. Kasschau and S.K. Murphy. “Cytoskeletal Reorganization in a Kidney Cell Line (LLC-PK1) under Hypertonic Stress.” Molecular Biology of the Cell, 17, 2361 (2006).
    • P. Patel, H. Tyagi, A. Khanna, M. Kasschau and S. Murphy. “Role of P38MAPK and Heat Shock Proteins, HSP27 and HSP70, in Osmotic Stress in Renal Vs. Blood Cells: A Comparative Study.” Molecular Biology of the Cell (2008).
    • M.D. Dutt, M.R. Kasschau and S.K. Murphy. “Filopodia Formation in the KG1a Human Hematopoietic Cell Lineand Earthworm Coelomocytes Under Hypertonic Osmotic Stress.” Molecular Biology of the Cell, submitted (2005).
    • C. E. O’Brien and S.K. Murphy. “Interaction Between PKC and HSP 70 in Fibroblasts Overexpressing Cellular Ras.” Molecular Biology of the Cell, submitted (2005).
    • C. O’Brien*, D. Lakic* and S.K. Murphy. “HSP70 Levels Are Elevated in Fibroblasts Overexpressing Cellular Ras Protein.” Molecular Biology of the Cell, 15:361a (2004).
    • M. Braun*, W. Ding* and S.K. Murphy. “Regulatory Interactions of PIP2-PLC, PC-PLD and PKC in Cultured Mouse Fibroblasts.” Molecular Biology of the Cell, 14:147a (2003).
    • S.K. Murphy, R. Kareem*, Y.Lai* and J. Worobiej*. “Effects of Overexpression of Cellular Ras Vs. Mutated Ras.” Molecular Biology of the Cell. 11:242a (2000).
    • W.Ding*, Y. Kwok* and S.K. Murphy. “Reciprocal Regulations of PI-PLC and PC-PLC/PLD in Ras Transformed Fibroblasts.” Molecular Biology of the Cell. 9:117a (1998).
    • S.A. Morine*, S.K. Murphy and M.R. Kasschau. "Cytoskeletal Changes in Coelomocytes from the Earthworm, Lumbricus Terrestris, Stimulated to Adhere to Immobilized Protein Matrices." Molecular Biology of the Cell, 8:270a, (1997).
    • T.T. Ho*, T.M. Allen* and S.K. Murphy. "Ras P21 Regulates Phospholipase D Through the CAMP Cascade." Molecular Biology of the Cell, 8:142a, (1997).
    • T. Ho* and S.K. Murphy. "Regulation of Phospholipase C and D by RAS P21 and Protein Kinase C." Molecular Biology of the Cell, 7:343a (1996).
    • S.K. Murphy, S. Robb-Gaspers* and A.M. Haines*. "Protein Kinase C Regulates the Activity of Phospholipase C and Phospholipase D in Ras-expressing and Non-ras-expressing NIH3T3 Cells." Proceedings of the American Association for Cancer Research, 36:53 (1995).

  • Heat shock proteins (HSP) are an evolutionarily conserved group of proteins that play a vital role in maintaining cell viability in response to stress. Their ability to catalyze the proper folding of misfolded proteins and impair apoptosis help protect cells from a variety of stressors. For this reason, Dr. Murphy's lab is interested in how these ubiquitously expressed HSPs can have both beneficial and detrimental effects by promoting normal physiological processes as well as disease states such as cancer.