Entity

Time filter

Source Type

Sheridan, IL, United States

Serrano M.C.,Chemistry of Life Processes Institute | Ameer G.A.,CSIC - Institute of Materials Science | Ameer G.A.,Northwestern University
Macromolecular Bioscience | Year: 2012

Shape-memory polymers (SMP) are versatile stimuli-responsive materials that can switch, upon stimulation, from a temporary to a permanent shape. This advanced functionality makes SMP suitable and promising materials for diverse technological applications, including the fabrication of smart biomedical devices. In this paper, advances in the design of SMP are discussed, with emphasis on materials investigated for medical applications. Future directions necessary to bring SMP closer to their clinical application are also highlighted. © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. Source


Uzarski J.S.,Northwestern University | Xia Y.,Salk Institute for Biological Studies | Belmonte J.C.I.,Salk Institute for Biological Studies | Wertheim J.A.,Northwestern University | Wertheim J.A.,Chemistry of Life Processes Institute
Current Opinion in Nephrology and Hypertension | Year: 2014

The severe shortage of suitable donor kidneys limits organ transplantation to a small fraction of patients suffering from end-stage renal failure. Engineering autologous kidney grafts on-demand would potentially alleviate this shortage, thereby reducing healthcare costs, improving quality of life, and increasing longevity for patients suffering from renal failure. RECENT FINDINGS: Over the past 2 years, several studies have demonstrated that structurally intact extracellular matrix (ECM) scaffolds can be derived from human or animal kidneys through decellularization, a process in which detergent or enzyme solutions are perfused through the renal vasculature to remove the native cells. The future clinical paradigm would be to repopulate these decellularized kidney matrices with patient-derived renal stem cells to regenerate a functional kidney graft. Recent research aiming toward this goal has focused on the optimization of decellularization protocols, design of bioreactor systems to seed cells into appropriate compartments of the renal ECM to nurture their growth to restore kidney function, and differentiation of pluripotent stem cells (PSCs) into renal progenitor lineages. SUMMARY: New research efforts utilizing bio-mimetic perfusion bioreactor systems to repopulate decellularized kidney scaffolds, coupled with the differentiation of PSCs into renal progenitor cell populations, indicate substantial progress toward the ultimate goal of building a functional kidney graft on-demand. © 2014 Wolters Kluwer Health | Lippincott Williams & Wilkins. Source


Savaryn J.P.,Chemistry of Life Processes Institute | Catherman A.D.,Chemistry of Life Processes Institute | Thomas P.M.,Chemistry of Life Processes Institute | Abecassis M.M.,Comprehensive Transplant Center | And 2 more authors.
Genome Medicine | Year: 2013

Proteomic technology has advanced steadily since the development of 'soft-ionization' techniques for mass-spectrometry-based molecular identification more than two decades ago. Now, the large-scale analysis of proteins (proteomics) is a mainstay of biological research and clinical translation, with researchers seeking molecular diagnostics, as well as protein-based markers for personalized medicine. Proteomic strategies using the protease trypsin (known as bottom-up proteomics) were the first to be developed and optimized and form the dominant approach at present. However, researchers are now beginning to understand the limitations of bottom-up techniques, namely the inability to characterize and quantify intact protein molecules from a complex mixture of digested peptides. To overcome these limitations, several laboratories are taking a whole-protein-based approach, in which intact protein molecules are the analytical targets for characterization and quantification. We discuss these top-down techniques and how they have been applied to clinical research and are likely to be applied in the near future. Given the recent improvements in mass-spectrometry-based proteomics and stronger cooperation between researchers, clinicians and statisticians, both peptide-based (bottom-up) strategies and whole-protein-based (top-down) strategies are set to complement each other and help researchers and clinicians better understand and detect complex disease phenotypes. © 2013 BioMed Central Ltd. Source


Trippier P.C.,Northwestern University | Trippier P.C.,Texas Tech University | Zhao K.T.,Northwestern University | Fox S.G.,Chemistry of Life Processes Institute | And 7 more authors.
ACS Chemical Neuroscience | Year: 2014

(Chemical Equation Presented) Amyotrophic lateral sclerosis (ALS) is a progressive and ultimately fatal neurodegenerative disease. Pyrazolone containing small molecules have shown significant disease attenuating efficacy in cellular and murine models of ALS. Pyrazolone based affinity probes were synthesized to identify high affi nity binding partners and ascertain a potential biological mode of action. Probes were confirmed to be neuroprotective in PC12-SOD1G93A cells. PC12-SOD1G93A cell lysates were used for protein pull-down, affinity purification, and subsequent proteomic analysis using LC-MS/MS. Proteomics identified the 26S proteasome regulatory subunit 4 (PSMC1), 26S proteasome regulatory subunit 6B (PSMC4), and T-complex protein 1 (TCP-1) as putative protein targets. Coincubation with appropriate competitors confirmed the authenticity of the proteomics results. Activation of the proteasome by pyrazolones was demonstrated in the absence of exogenous proteasome inhibitor and by restoration of cellular protein degradation of a fluorogenic proteasome substrate in PC12-SOD1G93A cells. Importantly, supplementary studies indicated that these molecules do not induce a heat shock response. We propose that pyrazolones represent a rare class of molecules that enhance proteasomal activation in the absence of a heat shock response and may have therapeutic potential in ALS. © 2014 American Chemical Society. Source


Marvin R.G.,Chemistry of Life Processes Institute | Wolford J.L.,Northwestern University | Kidd M.J.,University of Michigan | Murphy S.,University of Washington | And 7 more authors.
Chemistry and Biology | Year: 2012

Dynamic fluxes in the concentration of ions and small molecules are fundamental features of cell signaling, differentiation, and development. Similar roles for fluxes in transition metal concentrations are less well established. Here, we show that massive zinc fluxes are essential in the infection cycle of an intracellular eukaryotic parasite. Using single-cell quantitative imaging, we show that growth of the blood-stage Plasmodium falciparum parasite requires acquisition of 30 million zinc atoms per erythrocyte before host cell rupture, corresponding to a 400% increase in total zinc concentration. Zinc accumulates in a freely available form in parasitophorous compartments outside the food vacuole, including mitochondria. Restriction of zinc availability via small molecule treatment causes a drop in mitochondrial membrane potential and severely inhibits parasite growth. Thus, extraordinary zinc acquisition and trafficking are essential for parasite development. © 2012 Elsevier Ltd All rights reserved. Source

Discover hidden collaborations