Nancy Wangechi KaruriAssistant Professor
- B.E. from University of New South Wales, Australia (Chemical Eng., 1999)
- Ph.D. from University of Wisconsin-Madison (Chemical Eng., 2005)
We address two critical needs in the study of chronic wounds; the need for a proteolytically stable fibronectin and the need for an extracellular matrix on which the tissue can be repaired. These needs are addressed by the following goals:
(1) Design a soluble bioactive and proteolytically stable polymer conjugate of fibronectin.
(2) Design biologically functional extracellular matrix mimics that are based on composites of polymer hydrogels and fibronectin functional domains.
We use cell and molecular biology techniques as well engineering analytical skills to address these goals. These studies will contribute to the design of novel therapeutic approaches to hard to heal wounds."
"In a significant proportion of the population in the United States, a small break in the skin can lead to loss of limb or life due to of impaired wound healing. In hard to heal or chronic wounds, fibronectin, an integral part of the cellular scaffold or extracellular matrix in the wound bed is degraded. Chronic wounds do not heal because cells involved in tissue repair, need specific cues in fibronectin to attach, migrate, proliferate and assemble a tissue extracellular matrix.
We in our laboratory envision the chronic skin wound as presenting two main problems: (i) Fibronectin degradation and (ii) the lack of an extracellular matrix on which the tissue can be rebuilt. We have focused on solving these two main problems by two main thrusts:
(a)Developing polymer conjugates of fibronectin that are biologically active and proteolytically stable
(b)Synthesizing biologically functional extracellular matrix mimics that are based on composites of hydrogels and fibronectin functional domains."
- The effect of fibronectin on the kinetics of fibrin matrix assembly.
- Synthesis of artificial scaffolds with fibronectin domains.
- Stabilizing fibronectin against protease degradation.
- ASCB Travel award for Raj Desai (Undergraduate), American Society for Cell Biology 2013
- Visiting Professor Research Award, American Society for Cell Biology 2013
- Minorities Affairs Committee Travel Awards, American Society for Cell Biology 2011
- Educational and Research Initiative Fund (ERIF) Award, Illinois Institute of Technology 2010
- Minorities Affairs Committee Travel Awards, American Society for Cell Biology 2009
- Carl Storm Underrepresented Minority Fellowship, Gordon Research Conferences 2006
- T32 National Institutes of Health Training Grant, 2006
- Roland Ragatz Teaching Assistant Award, University of Wisconsin-Madison, 2002, 2003
- Graduate Engineering Research Scholars Fellowship, University of Wisconsin-Madison, 2000
- Australian Research Council Scholarship, University of New South Wales, Australia, 1999
Selected Publications1. Zhang, C, Desai, R, Karuri, NW, “Lysine PEGylation of fibronectin – Effect of PEG molecular weight on secondary structure, proteolytic stability, gelatin binding, cell adhesion and cell spreading”, under review, 2014.
2. Ramanathan, A, Karuri, NW, “Fibronectin increases the rate of fibrin clot polymerization and alters matrix morphology”, Biochemical and Biophysical Research Communications, 2014, 2014 10;443(2):395-399.
3. Ramanathan, A, Karuri, NW, “Fibronectin Increases the Rate of Fibrin Clot Polymerization and Alters Matrix Morphology”, Proceedings of the American Institute of Chemical Engineers, 2013, San Francisco, 2013.
4. Zhang, C, Hekmatfar, S, Karuri, NW, “A comparative study of polyethylene glycol hydrogels derivatized with the RGD peptide and the cell-binding domain of fibronectin”, Journal of Biomedical Materials Research Part A, 2013
5. Zhang, C, Hekmatfar, S, Ramanathan, A, Karuri, NW, “PEGylated human plasma fibronectin is proteolytically stable, supports cell adhesion, cell migration, focal adhesion formation and fibronectin fibrillogenesis”, Biotechnology Progress, 2013.
6. Kshatriya, PP, Karuri, SW, Chiang, C, Karuri, NW, "A combinatorial approach for directing the amount of fibronectin fibrils assembled by cells that uses surfaces derivatized with mixtures of fibronectin and cell binding domains", Biotechnology Progress, 2012, 28(3):862-871.
7. Chiang, C, Karuri, SW, Kshatriya, PP, Schwartz, J, Schwarzbauer, J. E., Karuri, N. W., "A new surface derivatization strategy for combinatorial analysis of cell response to mixtures of protein domains", Langmuir, 2012, 28: 548-556.Karuri, NW, Lin, Z, Rye, H, Schwarzbauer, JE, “Probing the conformation of the fibronectin III1-2 domain by fluorescence resonance energy transfer”, Journal of Biological Chemistry, 2009, 284: 3445 - 3452.
8. Karuri, NW, Porri, TJ, Albrecht, R, Murphy, CJ, Nealey, PF, “Structural organization of the cytoskeleton in SV40 human corneal epithelial cells cultured on nano- and microscale grooves”, Scanning, 2008, 30: 1-9.
9. Karuri, NW, Albrecht, R, Murphy, CJ, Nealey, PF, “Nano- and microscale holes modulate cell-substrate adhesion, cytoskeletal organization and –β1 integrin localization in SV-40 Human Corneal Epithelial Cells”, IEEE Transactions on Nanobioscience, 2006, 5: 273-280.
10. Karuri, NW, Nealey, PF, Murphy, CJ, Albrecht, RM, “Structural organization of the cytoskeleton in SV40 human corneal epithelial cells cultured on nano- and microscale topography”, Microscopy and Microanalysis, 2005, 11: 182-183.
11. Karuri, NW, Liliensiek, S, Teixeira, AI, Abrams, G, Campbell, S, Nealey, PF, Murphy, CJ, “Biological length scale topography enhances cell substrate adhesion of human corneal epithelial cells”, Journal of Cell Science, 2004, 117: 3153-3164.