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个人简介

B.S.; Chemical Engineering, University of Massachusetts at Amherst PhD; Polymer Science and Engineering, University of Massachusetts, Amherst

研究领域

Engineering at the extracellular level The extracellular matrix (ECM) provides a spectrum of biophysical and biochemical clues that influence cell and tissue response. Biophysical and biochemical clues come from the molecular composition of the ECM and come in the form of chemical, morphological, and mechanical cues. Our laboratory has focused largely on the glycosaminoglycan (GAG), or long chain sugar biopolymers, and the instructive role they play in the ECM. The GAGs themselves can be chemically modified and used to form hydrogels for tissue engineering. The modified GAGs can also be used to engineer mimetics of the proteoglycans found within the ECM. Synthesis and evaluation of proteoglycan mimetics composes a large portion of the more recent effort in the Panitch laboratory. These molecules can be designed to mimic many of the functional properties of native proteoglycans, and we have used them in vascular, dermal and cartilage applications. Our published work has shown that these mimics can inhibit dermal scarring, improve vessel healing after balloon angioplasty and suppress osteoarthritis following traumatic joint injury. Ongoing efforts include partnering to translate these therapeutics into the market place in addition to developing new ECM therapeutics. Engineering at the intracellular level Inflammation plays a critical role in tissue healing. Thus, fine-tuning the inflammatory process to promote normal tissue repair, while preventing scar formation is an on going effort in many labs throughout the world. Our laboratory has focused on the design of cell-penetrating peptide therapeutics that help regulate the inflammatory response by controlling key pathways in both inflammation and fibrosis. Our main effort has been focused on optimization and delivery of peptide inhibitors of the kinase Mitogen-Activated Protein Kinase-Activated Protein Kinase II, or MK2. Past efforts involving optimization of the peptide showed that both the cell-penetrating peptide and the kinase inhibitor sequence contribute to the specificity and activity of the peptide. With key collaborators we have shown that the peptide is effective at inhibiting surgical adhesions, intimal hyperplasia following vein-graft bypass, and the progression of idiopathic pulmonary fibrosis. Current efforts include developing methodologies to study key cellular delivery mechanisms, developing nanoparticle delivery technologies to improve efficacy, and expanding into the bioinformatics area, through collaborations with the Rundell and Kinzer-Ursem laboratories to elucidate how the MK2 signaling pathway interfaces with the AKT and TGF-β1 pathways to regulate tissue healing.

近期论文

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A. Panitch, M. J. Fournier, T. L. Mason and D. A. Tirrell. Design and Assembly of Artificial Protein-Based Materials. Journal of Biological Chemistry. 18, 1994: 283. A. Panitch, K. Matsuki, E. Cantor, S. J. Cooper, E. D. T. Atkins, M. J. Fournier, T. L. Mason and D. A. Tirrell. Poly(L-alanylglycine): ‘Multigram-Scale Biosynthesis, Chrystallization, and Structural Analysis of Chain-Folded Lamella’. Macromolecules. 30, 1997: 42-49. A. Panitch, T. Yamaoka, M. J. Fournier, T. L. Mason, D. A. Tirrell. Design and Biosynthesis of Elastin-Like Artificial Extracellular Matrix Proteins Containing Periodically Spaced Fibronectin CS5 Domains. Macromolecules. 32, 1999: 1701-1704. T. Tamura, T. Yamaoka, S. Kunki, A. Panitch and D. A. Tirrell. Effects of Temperature and Pressure on the Aggregational Properties of an Engineered Elastin Model Peptide in Aqueous Solution. Biomacromolecules. 1(4) 2000: 552-5. S. Sakiyama-Elbert, A. Panitch and J. A. Hubbell. Development of Growth Factor Fusion Proteins for Cell-Triggered Drug Delivery. FASEB J. 15(7), 2001: 1300-1302. B.L. Seal*, T. Otero*, and A. Panitch. Polymeric Biomaterials for Tissue and Organ Regeneration. Materials Science and Engineering R: Reports. 43(4-5), 2001: 147-230. S. Halstenberg, A. Panitch, S. Rizzi, H. Hall, and J.A. Hubbell. Biologically Engineered Protein-graft-Poly(Ethylene Glycol) Hydrogels: A Cell-Adhesive and Plasmin-Degradable Biosynthetic Material for Tissue Repair, Biomacromolecules, 3(4), 2002: 710-723. Flynn CR, Komalavilas P, Tessier D, Thresher J, Niederkofler E, Nelson RW, Panitch A, Joshi L, Brophy CM. Transduction of biologically active motifs of the small heat shock related protein, HSP20, leads to relaxation of vascular smooth muscle. Faseb J, 17(10), 2003: 1358-60. Tessier D, Komalavilas P, Panitch A, Joshi L, Brophy CM. The small heat shock protein, HSP20, is dynamically associated with the actin cross-linking protein, actinin. J Surg Res, 111(1), 2003: 152-157. B Seal* and A. Panitch. Physical Polymer Matrices Based on Affinity Interactions Between Peptides and Polysaccharides. Biomacromolecules, 4(6), 2003: 1572-1582 BA Koeneman*, K Lee, A Singh, J He, GB Raupp, A Panitch, David G. Capco. An Ex Vivo Method for Evaluating the Biocompatibility of Neural Electrodes in Rat Brain Slice Cultures. Journal of Neuroscience Methods, 137(2) 2004: 257-263. Tessier DJ, Komalavilas P, Liu B, Kent CK, Thresher, JS, Dreiza*, CM, Panitch A, Joshi L, Furnish, E, Stone W, Fowl R, Brophy CM. Transduction of peptide analogs of the small heat shock-related protein HSP20 inhibits intimal hyperplasia. Journal of Vascular Surgery, 40(1), 2004: 206-214. C Dreiza*, C Brophy, P Komalavilas, M Pallero, J Murphy-Ullrich, E Furnish, L Joshi, M von Rechenberg, J Ho, B Richardson, N Xu, Y Zhen, J M Peltier, A Panitch. Transducible Heat Shock Protein 20 (HSP20) Phosphopeptide Alters Cytoskeletal Dynamics. FASEB J 19(2) 2005: 261-3. L. B. Lopes, C. M. Brophy, E. Furnish, C. R. Flynn, O. Sparks, P. Komalavilas, L. Joshi, A. Panitch, V. L. B. Bentley, Comparative Study of the Skin Penetration of Protein Transduction Domains and a Conjugated Protein. Pharmaceutical Research, 22(5) 2005: 750-7. B. Seal* and A. Panitch, Physical Matrices Stabilized by Enzymatically Sensitive Covalent Crosslinks, Acta Biomaterialia, 2(3) 2006: 241-251. B. Seal* and A. Panitch, Viscoelastic Behavior of Environmentally Sensitive Biomimetic Polymer Matrices, Macromolecules, 39(6), 2006: 2268-2274. E Horn, M Beaumont*, A Harvey*, M Preul and A Panitch, 2007, Influence of Cross-Linked Hyaluronan Hydrogels on Neurite Outgrowth and Recovery from Spinal Cord Injury. Journal of Neurosurgery-Spine, 6(2), 2007: 133-40 P. Stice, A. Gilletti, A. Panitch, J. Muthuswamy, Thin microelectrodes reduce GFAp expression in the implant site in rodent somatosensory cortex. Journal of Neuroscience Methods, Journal of Neurological Engineering, 4, 2007: 42-53. S. Padalkar, Y. Zhao, K. Stuart*, A. Panitch, J. Rickus, L. Stanciu Preparation of Biomolecule Gel Matrices for Electron Microscopy Ultramicroscopy, 108(4), 2007: 309-313. L. B. Lopes, E. Furnish, P. Komalavilas, B. L. Seal*, A. Panitch, M. V. L. B. Bentley, C. M. Brophy, Enhanced skin penetration of P20 phosphopeptide using protein transduction domains. European Journal of Pharmaceutics and Biopharmaceutics, 68 (2), 2008: 441-445. K. Stuart* and A. Panitch, Influence of Chondroitin Sulfate on Collagen Gel Structure and Mechanical Properties at Physiologically Relevant Levels, Biopolymers 89(10), 2008: 841-851. K.J. Jeong*, K. Butterfield* and A. Panitch, A novel assay to probe heparin-peptide interactions using peptide stabilized gold nanoparticles, Langmuir, 24(16), 2008: 8794-8800. J.E. Paderi* and A. Panitch, Design of a Synthetic Collagen-Binding Peptidoglycan that Modulates Collagen Fibrillogenesis, Biomacromolecules, 9(9), 2008: 2562-2566. L.B. Lopes, E.J. Furnish, P. Komalavilas, C. R. Flynn, P. Ashby, A. Hansen, D.P. Ly, G. P. Yang, M. T. Longaker, A. Panitch, C. M. Brophy, Cell Permeant Peptide Analogues of the Small Heat Shock Protein, HSP20, Reduce TGF-β1-Induced CTGF Expression in Keloid Fibroblasts. Investigative Dermatology, 129(3), 2009: 590-598. doi: 10.1038/jid.2008.264 R. Sistiabudi, J. Paderi*, A. Panitch and A. Ivanisevic, Modification of Native Collagen with Cell-Adhesive Peptide to Promote RPE Cell Attachment on Bruch’s Membrane. Biotechnology and Bioengineering, 102(6), 2008: 1723-1729.

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