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Overland Park Sheraton Floor Plan LOCATION OF EVENTS
| Content Provider | Semantic Scholar |
|---|---|
| Author | Shivashankar, K. N. Kumar, S. Ganesh Jefferson, Wendy N. Williams, Carmen Braun Chennathukuzhi, Vargheese M. Welti, Ruth Peterson, Brian Kobayashi, Yass |
| Copyright Year | 2015 |
| Abstract | HSV-1 infects sensory neurons in humans and establishes lifelong latent infections, which can reactivate by stress stimuli. Among the first proteins to be expressed when HSV-1 infects a cell is infected cell protein 0 (ICP0). ICP0 is an E3 ubiquitin ligase that stimulates viral gene expression and enhances viral replication. ICP0 facilitates viral gene expression by impairing the antiviral effects of the cellular factor, interferon (IFN)-β. The mechanism(s) by which ICP0 impairs IFN-β restriction on HSV-1 replication remain largely unknown. Consequently, the purpose of the present study was to determine which domain(s) in ICP0 contribute to HSV-1 resistance to the antiviral effects of IFN-β. To identify one or more domains, a series of ICP0 truncation mutants was used to perform plaque reduction and gene expression assays in untreated cells and cells pretreated with IFN-β. We determined that the first 388 N-terminal amino acids of ICP0 confer significant resistance of HSV-1 to IFN-β while efficiently stimulating viral gene expression; specifically, amino acids from 312 to 388 are crucial for mediating this resistance. We hypothesize that this N-terminal domain of ICP0 plays a role in counteracting the IFN-β-induced restriction on viral replication through ICP0-host protein interactions. Overall, we conclude that the N-terminal half of ICP0 enables HSV-1 to resist an established IFN-β response with residues from 312 to 388 being required for this function. Sunday, January 17, 2016 Dopaminergic Cell Toxicity of a Derivative of Parkinsonian Toxin, 4-methyl-phenylpyridinium (MPP+) Lickteig, Bryan and Dr. Kandatege Wimalasena Department of Chemistry, Wichita State University Parkinson’s disease (PD) is a neurodegenerative disease that has been studied for several decades with no definitive answer to its origin. It has been hypothesized that genetics, environmental factors, and mitochondrial mutations are linked to PD, but the etiology of PD has not been fully understood. 1-Methyl-4-phenylpyridinium (MPP+) has been 6 PLATFORM PRESENTATION ABSTRACTS used as a model for PD due to the finding that it causes PD symptoms in humans and other primates. MPP + inhibits the mitochondrial complex I and increase oxidative stress of dopaminergic neurons. Our lab previously characterized 3-Amino-2-phenylpropene (APP), as an irreversible inhibitor of vesicular monoamine transporter-2 (VMAT2) and also reported that it is toxic to the dopaminergic cells. Since the synaptic accumulation of MPP+ is proposed to be a detoxification mechanism, it was hypothesized that the conjugate of MPP+ and APP, N-(2-phenypropene)-4phenylpyridinium (MPP-APP), would be more toxic to dopaminergic cells. To test this hypothesis, the dopaminergic toxicity of MPP-APP was determined using MN9D cells. The results showed that MPP-APP is more toxic to MN9D cells than either the MPP+ or APP themselves. MPP-APP accumulates in cells through simple diffusion and similar to MPP+ it increase the ROS production specifically in dopaminergic cells. Experiments with fluorescence dye DAPI shows that the cell death is due to the ROS induced apoptotic pathway and antioxidants protects cells from the toxicity. These studies will not only help to understand the mechanism of the specific dopaminergic toxicity of MPP+ and similar toxins, but also lead to the development of preventive strategies for PD. New MR Activatable Nanoprobe for the Multiparametric Imaging and Treatment of Prostate Cancer Kallu, Jyothi, Jessica Jewell, Tuhina Banerjee, and Santimukul Santra* Department of Chemistry, Biology and Kansas Polymer Research Center, Pittsburg State University, Pittsburg, KS 66762. Email: jyothi.kallu@gus.pittstate.edu An innovative activatable MRI probe is designed for the image-guided prostate cancer (PCa) diagnosis and monitoring of the treatment. This MRI probe is formulated in such a way that the T1 magnetic relaxation (spin-spin) will be activated only after internalization into cancer cells and a bright contrast is expected. In addition, combination therapy approach using doxorubicin and PARP-1 inhibitor, Olaparib, will be used for the effective treatment of prostate cancers. The PSMA receptor over-expressed PCa cells will be selectively targeted by conjugating A10 PSMA aptamer in order to reduce any off-target side effects. We will be using a robust Gd-DTPA encapsulating iron oxide nanoparticles as an activatable T1 MRI contrast agent, which will be activated and provide bright contrast once inside the tumor (1-3). This activatable MRI probe will be used to carry doxorubicin and Olaparib specifically to the PCa cells by conjugating A10 PSMA aptamer on the nanoprobe’s surface, minimizing off-target delivery. Towards this end, GdDTPA-encapsulating iron oxide nanoparticle (IONP) will be formulated. We hypothesized that the T1 relaxation of GdDTPA is quenched upon encapsulation into the superparamagnetic IONPs. The T1 MR activation will be detected using bench-top magnetic relaxometer (0.47T, Bruker) in response to the oxidative stress and acidic pH inside the tumor microenvironment of prostate cancer. References: 1) Santra, S. et. al., Small 2009, 5, 1862-1868. 2) Santra, S. et al., ACS Nano, 2012, 6, 7281-7294. 3) Kaittanis C, Santra, S. et. al., Nat. Commune. 2014, 5, 3384-3395. The Effects of Peptides derived from Beta2 Glycoprotein I on Endothelial and Placental Tissue in Models of Preeclampsia Nieto, Noel F. and Sherry Fleming Division of Biology, Kansas State University, Manhattan KS 66503 Preeclampsia, a hypertensive disorder that affects nearly 10% of pregnant women, is the leading cause of maternal death and medically-induced preterm births in the US. Preeclampsia symptoms include high blood pressure, elevated protein in the mother’s urine, and low birth weight. Although the exact cause remains unknown, evidence indicates that complement dysregulation caused by placental hypoxia plays a vital role in the development of preeclampsia. To simulate preeclampsia, a frequent model of placental ischemia and induced hypertension is the reduced uteroplacental perfusion pressure (RUPP) rat model. Beta2-glycoprotein I (β2-GPI) elicits an immune response during hypertension and mediates fetal loss and growth restrictions in other pregnancy conditions. We tested the hypothesis that β2-GPI binds hypoxic endothelial cells and peptides derived from mouse β2-GPI block binding in vitro and in preeclampsic rats. Rat endothelial cells, IEC-18, were incubated in either hypoxic or normoxic conditions for two hours prior to receiving one of four different peptide treatments during a 30 min reperfusion period. The treated cells were stained for β2-GP1 with immunohistochemistry. The results strongly indicate that hypoxic conditions induced β2-GPI binding to rat endothelial cells and peptides 296c-s and RD-p9 reduced binding compared to the control peptide or the untreated sample. Importantly, RD-p9 appeared to have a greater effect on the reduction of rat endothelial binding. Future experiments will examine IgM, C3, and β2-GPI deposited on rat placenta from rats treated with β2-GPI peptides prior to Sham or RUPP surgery to simulate preeclamptic conditions. 7 POSTER PRESENTATIONS 1. Guo, Y., R. Marquez, X. Wu, A. Smith, L. Lan, and X. Liang Departments of Molecular Biosciences and Radiation Oncology, University of Kansas Cancer Center, KU Lawrence, KS: Long non-coding RNA lincRNA-p21 and radiation response of cancer 2. Haller, R. and S. H. Leung Department of Chemistry, Washburn University, Topeka, KS 66621: Progress toward the synthesis of dipyrroyl-α,β-unsaturated ketones 3. Han, S., X. Wu, Y.Guo, J. Zhang, X. Gu, R. T Marquez, J. Aube, D. A. Dixon and L. Xu Department of Molecular Biosciences, University of Kansas; The University of North Carolina; 3 Department of Cancer Biology, University of Kansas Medical Centre Research Institute: Id1 is the oncogenic downstream target of RNA binding protein HuR in gastric cancer 4. Harmon, G., C. Barnard, J. Yeomans and P. Harries Pittsburg State University, Department of Biology: The Effect of SOS3 Knockout on Salt Tolerance in Physcomitrella patens 5. Heckert, B., T. Banerjee, R. Alnasser and S. Santra* Department of Chemistry, Pittsburg State University, Pittsburg, KS 66762; Email: blazeheckert@gus.pittstate.edu: Designer Polymeric Nanotheranostics for the Detection and Treatment of Lung Cancer 6. Karanicolas, J., K. Khar, J. Niu, W. Lea, A. Ranjan, M. Fisher, and T. Iwakuma Center for Computational Biology and 2 Department of Molecular Biosciences, University of Kansas, Lawrence, KS, 3 Department of Biochemistry and Molecular Biology and 4 Department of Cancer Biology, University of Kansas Medical Center, Kansas City, KS: Chemical Tools to Modulate p53 Folding in Cells 7. Sharma, N. and M. Markiewicz Department of Microbiology, Molecular Genetics, & Immunology, University of Kansas Medical Center, KS, USA: Constitutive Expression of the NKG2D Ligand RAE1ε Within Pancreatic Islets Ameliorates Autoimmune Diabetes Development in Non-Obese Diabetic Mice 8. Tharp, J. and A. Herbig Department of Biology Washburn University: Determination of Intracellular Magnesium in Bacillus subtilis 9. Troupe, R., T. Marriage* and B. Olson* Department of Biology, Langston University; Division of Biology, Kansas State University*: Cell wall modification genes and the promotion of multicellularity 10. Velazhahan,V., A. Khosla, and K. Schrick Division of Biology, Kansas State University: Investigating the mechanism underlying the inhibitory role of dietary flavonoids in human cancers 11. Winkley, K. and K. Michel Kansas State University, Division of Biology: Efficacy of fungal biopesticides in vector control can be enhanced by genetic manipulation of mosquitoes. 12. Woody, K., J. Kallu, D. Thompson, T. Banerjee, N. N. Gerasimchuk and S. Santra* *Department of Chemistry, Biology and Kansas Polymer Research Center, Pittsburg State University, Pittsburg, KS 66762. Depart |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | http://www.k-inbre.org/2016symposium/2016%20Symposium%20program.webpage.pdf |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
