Immunoassay Workflow Solutions Antibody Arrays, Luminex® Assays, Elisas and Simple Plex™ Assays Table of Contents

Total Page:16

File Type:pdf, Size:1020Kb

Immunoassay Workflow Solutions Antibody Arrays, Luminex® Assays, Elisas and Simple Plex™ Assays Table of Contents Immunoassay Workflow Solutions Antibody Arrays, Luminex® Assays, ELISAs and Simple Plex™ Assays Table of Contents 4 Immunoassay Workflow Solutions 6 Immunoassay Offering by Molecule 27 Proteome Profiler® Antibody Arrays 34 Luminex® High Performance Assays 37 Luminex® Preconfigured Panels Human XL Cytokine Discovery Luminex ® High Performance Assay ✔ Broad selection choose any combination from all 45 analytes ✔ Superior accuracy tested side-by-side with other leading suppliers ✔ Flexible x Effects order any combination of analytes tri within the panel a y Sele M od ct tib io n n ✔ Easy to order A select analytes directly from r Formula the product datasheet ffe tio u n B tion a QC Tes d tin li g a alibr V C a t o r s rity y ea in a L s s A Learn more | rndsystems.com/human-xl From Screening to Validation, We Have Your Total Workflow Solution screening validation Inexpensive, Easy-to-use Screening Tool Untreated Proteome Profiler™ Antibody Arrays • Analyze up to 119 proteins simultaneously • Quickly assess complex signaling responses Treated Instrumentation: Only standard Western blotting equipment Learn more | rndsystems.com/proteomeprofiler Quantitative Multiplexing Luminex® Assays • The most accurate and flexible offering on the market • Measure up to 50 analytes simultaneously FLEXMAP 3D® Instrumentation: MAGPIX®, Luminex® 200™, FlexMAP 3D® Luminex® High Performance Assays • Rigorously validated for accuracy, precision, and reproducibility MAGPIX® • XL Discovery Cytokine Panel now available Luminex® 100/200™ Learn more | rndsystems.com/luminex Uncoated ELISAs DuoSet® ELISA Development Systems • Economical and adaptable to multiple platforms • Over 1,000 available covering 8 species Instrumentation: Dependent on the platform being utilized Learn more | rndsystems.com/elisa 4 screening validation Gold Standard Coated ELISA Kits Quantikine® ELISA Kits • Exhaustively validated for superior performance and reproducibility • The most referenced ELISAs in the literature Instrumentation: Any 96-well plate reader Learn more | rndsystems.com/elisa Automated, Highly Reproducible ELISA Platform Simple Plex™ Assays • Unprecedented reproducibility • Wide dynamic range and sensitivity • Hands-free, fast results 16×4 Cartridge 32×4 Cartridge 72×1 Cartridge Instrumentation: Ella™ Learn more | proteinsimple.com/ella 5 Immunoassay Offering by Molecule Luminex® Proteome Profiler® Luminex® Uncoated Coated Simple Plex™ Molecule High Performance Arrays Assays ELISA Kits ELISA Kits Assays Assays 4-1BB/TNFRSF9/CD137 H H M 14-3-3z H 20S Immunoproteasome H 25-OH Vitamin D H ACE/CD143 H H Acetylcholinesterase/ACHE H Activin A H H H M R ADAM8 H H ADAM9 H H ADAM10 H ADAM12 H H ADAM15 H H ADAMTS1 H M H ADAMTS4 H ADAMTS5 H ADAMTS13 H H H H Adiponectin/Acrp30 H M H M H H M R H M R H Afamin H Aggrecan H H Agrin R AgRP/ART H H H Akt, Phospho (S473) Pan Specific H M R Akt1 H H M R Akt1, Phospho (S473) H M Akt2 H Akt3 H Albumin H ALCAM/CD166 H M Aldehyde Dehydrogenase 1-A1/ H ALDH1A1 Aldosterone MS ALK-1 H M a1-Acid Glycoprotein H H a1B-Glycoprotein H a1-Microglobulin H a2-Macroglobulin H a-Defensin 1 H a-Fetoprotein/AFP H H M H M a-N-acetylglucosaminidase/ H NAGLU a-Synuclein H H AMICA/JAML H Aminoacylase/ACY1 H Aminopeptidase N/CD13 H H Amphiregulin H M H M H H AMPK a1 H M R AMPK a1, Phospho (T183) H Amyloid b H Amyloid b aa 1–42 H Angiogenin H M H H H H KEY Human H Mouse M Rat R Canine C Primate Pr Porcine P Multi-Species MS Viral V Bovine B C. botulinum Cb Cotton Rabbit CR Equine E Guinea Pig G Rabbit Rb *In Development 6 Learn more | rndsystems.com/immunoassays Luminex® Proteome Profiler® Luminex® Uncoated Coated Simple Plex™ Molecule High Performance Arrays Assays ELISA Kits ELISA Kits Assays Molecule Offering by Immunoassay Assays Angiopoietin-1 H M H H H H Angiopoietin-2 H M H M H H M R H Angiopoietin-3 M M Angiopoietin-4 H Angiopoietin-like 4 H Angiopoietin-like Protein 3/ H H M ANGPTL3 Angiopoietin-like Protein 4/ H H ANGPTL4 Angiopoietin-like Protein 6/ H H ANGPTL6 Annexin A2 H Annexin V H Apolipoprotein A-I/ApoA1 H H H Apolipoprotein B/ApoB H Apolipoprotein E/ApoE H APP H H H APRIL/TNFSF13 H H Artemin H H M ASC H ATF4 H Atrial Natriuretic Peptide/ANP H Attractin H H Axl H M H M H Axl, Phospho H B7-1/CD80 H M B7-H1/PD-L1 H H B7-H3 H H BACE-1 H H Bad H BAFF R/TNFRSF13C M BAFF/BLyS/TNFSF13B H M H H M H M H Bax H Bax-a H Bcl-2 H M H Bcl-10 H Bcl-x H M Bcl-xL H M BCMA/TNFRSF17 H H M H BDNF H H H M H H BDNF, Pro H b2-Microglobulin H H bIG-H3 H M b-Catenin H H Betacellulin/BTC H M b-NGF H M H R H Bikunin H BLC/BCA-1/CXCL13 H BMP-2 H H H M R H BMP-4 H H H H BMP-5 H BMP-6 H BMP-7 H H H KEY Human H Mouse M Rat R Canine C Primate Pr Porcine P Multi-Species MS Viral V Bovine B C. botulinum Cb Cotton Rabbit CR Equine E Guinea Pig G Rabbit Rb *In Development Learn more | rndsystems.com/immunoassays 7 Luminex® Proteome Profiler® Luminex® Uncoated Coated Simple Plex™ Molecule High Performance Arrays Assays ELISA Kits ELISA Kits Assays Assays BMP-9 H H M H BMP-10 H H M BoNT-A Cb BTLA H Butyrylcholinesterase/BCHE H H C1q R1/CD93 M H M CA15-3/MUC-1 H CA125/MUC16 H H H H Cadherin-11 H H Cadherin-13 H Cadherin-17 M Calbindin D H H H cAMP M R MS Carbonic Anhydrase IX/CA9 H H H H CARD6 H Cardiotrophin-1/CT-1 M Caspase-1 H H Caspase-3 H Caspase-3, Cleaved (Asp175) M H M Caspase-8 H Catalase H M Cathepsin A H Cathepsin B H H H Cathepsin B, Pro H Cathepsin D H Cathepsin E H Cathepsin L H H Cathepsin S H H H Cathepsin S, Pro H Cathepsin V H H Cathepsin X/Z/P H CBL H CCL1/I-309/TCA-3 H H M CCL2/JE/MCP-1 H M H H M R C H CCL3/MIP-1a H M H H M C H M H CCL4/MIP-1b H M H H M C H M H CCL5/RANTES H M H H M R H CCL6/C10 M CCL7/MCP-3/MARC H M H H H CCL8/MCP-2 H M H M H CCL9/10/MIP-1g M CCL11/Eotaxin H M H H M H M CCL12/MCP-5 M M M CCL13/MCP-4 H H H CCL14/HCC-1/HCC-3 H CCL14a/HCC-1 H CCL15/MIP-1d H H CCL16/HCC-4 H H CCL17/TARC H H M H CCL18/PARC H H H CCL19/MIP-3b H M H H M CCL20/MIP-3a H M H H M R H M H KEY Human H Mouse M Rat R Canine C Primate Pr Porcine P Multi-Species MS Viral V Bovine B C. botulinum Cb Cotton Rabbit CR Equine E Guinea Pig G Rabbit Rb *In Development 8 Learn more | rndsystems.com/immunoassays Luminex® Proteome Profiler® Luminex® Uncoated Coated Simple Plex™ Molecule High Performance Arrays Assays ELISA Kits ELISA Kits Assays Molecule Offering by Immunoassay Assays CCL21/6Ckine H M H M M CCL22/MDC H M H H M H M H CCL23/MPIF-1/Ckb8-1 H CCL24/Eotaxin-2/MPIF-2 H H M H CCL25/TECK H H M CCL26/Eotaxin-3 H H H CCL27/CTACK H H M H CCL28 H M H H M CD3e H CD5 H CD6 H CD8 H CD9 H CD14 H M H H H M H M H CD21/ Complement receptor H H type 2/CR2 CD23/Fce RII H H M H CD25/IL-2 Ra H H M H H CD27 Ligand/TNFSF7 M CD27/TNFRSF7 H H H M H CD28 H H CD30 Ligand/TNFSF8 M CD30/TNFRSF8 H H H M CD31/PECAM-1 H H CD36/SR-B3 H M CD38 H CD40 Ligand/TNFSF5 H H H H M H CD40/TNFRSF5 H H H H M H CD43 H CD44 H H CD44 s H CD47 H CD48/SLAMF2 H CD59 H CD97 H H CD99 H CD117/c-kit H H H CD117/c-kit, Phospho H CD163 H H H M H H CD200 H CD300a/LMIR1 H CDCP1 H CEACAM-1 H H H CEACAM-5/CD66e H H H H* CEACAM-6/CD66c H cGMP MS Chemerin H M H H M H M Chitinase 3-like 1 M H M H M H M H Chk2 (T68), Phospho H Chordin M Chorionic Gonadotropin b Chain H (HCG b) KEY Human H Mouse M Rat R Canine C Primate Pr Porcine P Multi-Species MS Viral V Bovine B C. botulinum Cb Cotton Rabbit CR Equine E Guinea Pig G Rabbit Rb *In Development Learn more | rndsystems.com/immunoassays 9 Luminex® Proteome Profiler® Luminex® Uncoated Coated Simple Plex™ Molecule High Performance Arrays Assays ELISA Kits ELISA Kits Assays Assays Chromogranin A H H cIAP-1 H cIAP-2 H Cited-2 H Claspin H M CLEC-1 H CLEC-2 H Clusterin H H M H M CNTF R H R H Coagulation Factor III H (Tissue Factor)/CD142 Coagulation Factor XIV/Protein C H COCO H Collagen I a1 H H Collagen II, Pro H Collagen IV a1/COL4A1 H Common g Chain/IL-2 Rg H COMP/Thrombospondin-5 H H H Complement Component C2 H Complement Component C3a H Complement Component C5/C5a H M H H M Complement Component C9 H Complement Factor D/Adipsin H M H M H H M H Complement Factor H H Contactin-1 H Contactin-2/TAG1 H Corin H H Corticosterone MS Cortisol MS COX-2 H H M C-Peptide H C-Reactive Protein/CRP H H M H H M H Creatinine MS CREB H CREB (S133), Phospho H M R c-Rel H CRELD2 H Cripto H H CRISP-1 M CRTAM H H CTGF/CCN2 H CTLA-4 M CTRP3/C1qTNF3/CORS26 H CTRP9/C1qTNF9 H CX3CL1/Fractalkine H H H M R H M H CXCL1/GROa/KC/CINC-1 H M H H M R H M R CXCL2/GROb/MIP-2/CINC-3 H M R H H M R M R CXCL3/GROg/CINC-2/DCIP-1 R R R CXCL4/PF4 H H M H M CXCL5/ENA-78 H H H H H CXCL6/GCP-2 H H H CXCL7/NAP-2 H H KEY Human H Mouse M Rat R Canine C Primate Pr Porcine P Multi-Species MS Viral V Bovine B C.
Recommended publications
  • Agrin Differentially Regulates the Rates of Axonal and Dendritic Elongation in Cultured Hippocampal Neurons
    The Journal of Neuroscience, September 1, 2001, 21(17):6802–6809 Agrin Differentially Regulates the Rates of Axonal and Dendritic Elongation in Cultured Hippocampal Neurons Kristina B. Mantych and Adriana Ferreira Institute for Neuroscience and Department of Cell and Molecular Biology, Northwestern University Medical School, Chicago, Illinois 60611 In the present study, we examined the role of agrin in axonal elongation and branching were paralleled by changes in the and dendritic elongation in central neurons. Dissociated hip- composition of the cytoskeleton. In the presence of agrin, there pocampal neurons were grown in the presence of either recom- was an upregulation of the expression of microtubule- binant agrin or antisense oligonucleotides designed to block associated proteins MAP1B, MAP2, and tau. In contrast, a agrin expression. Our results indicate that agrin differentially downregulation of the expression of these MAPs was detected regulates axonal and dendritic growth. Recombinant agrin de- in agrin-depleted cells. Taken collectively, these results suggest creased the rate of elongation of main axons but induced the an important role for agrin as a trigger of the transcription of formation of axonal branches. On the other hand, agrin induced neuro-specific genes involved in neurite elongation and branch- both dendritic elongation and dendritic branching. Conversely, ing in central neurons. cultured hippocampal neurons depleted of agrin extended longer, nonbranched axons and shorter dendrites when com- Key words: agrin; neurite outgrowth; microtubule-associated pared with controls. These changes in the rates of neurite proteins; CREB; antisense oligonucleotides; axons and dendrites Agrin, an extracellular matrix protein, is synthesized by motor Conversely, neurons depleted of agrin elongated longer axons neurons and transported to their terminals where it is released when compared with control ones (Ferreira 1999; Serpinskaya et (Magill-Solc and McMahan, 1988; Martinou et al., 1991; Ruegg et al., 1999).
    [Show full text]
  • Localization and Alternative Splicing of Agrin
    The Journal of Neuroscience, March 1994, 14(3): 1141-l 152 Localization and Alternative Splicing of Agrin mRNA in Adult Rat Brain: Transcripts Encoding lsoforms that Aggregate Acetylcholine Receptors Are Not Restricted to Cholinergic Regions Lawrence T. O’Connor, Julie C. Lauterborn, Christine M. Gall, and Martin A. Smith Department of Anatomy and Neurobiology, University of California at Irvine, Irvine, California 92717 Agrin is a protein implicated in the formation and mainte- that direct their organization. In comparison, much more is nance of the neuromuscular junction. In addition to motor known about the neuromuscularjunction. Like other chemical neurons, agrin mRNA has been detected in the brains of synapses,the neuromuscularjunction is characterized by spe- embryonic rat and chick and adult marine ray, suggesting cializations that adapt it for its role in synaptic transmission. that this molecule may also be involved in the formation of In particular, the postsynaptic apparatus is associatedwith a synapses between neurons. As a step toward understanding high concentration of acetylcholine receptors (AChR). The ac- agrin’s role in the CNS, we utilized Northern blot and in situ cumulation of AChR is an early event in development of the hybridization techniques to analyze the regional distribution neuromuscularjunction and has been shown to be the result of and cellular localization of agrin mRNA in the spinal cord inductive interactions between motor neuronsand musclefibers and brain of adult rats. The results of these studies indicate they innervate (reviewed in Hall and Sanes, 1993). Current ev- that the agrin mRNA is expressed predominantly by neurons idence suggeststhat agrin, a synaptic basal lamina protein, me- broadly distributed throughout the adult CNS.
    [Show full text]
  • Genomics of Mature and Immature Olfactory Sensory Neurons Melissa D
    University of Kentucky UKnowledge Physiology Faculty Publications Physiology 8-15-2012 Genomics of Mature and Immature Olfactory Sensory Neurons Melissa D. Nickell University of Kentucky, [email protected] Patrick Breheny University of Kentucky, [email protected] Arnold J. Stromberg University of Kentucky, [email protected] Timothy S. McClintock University of Kentucky, [email protected] Right click to open a feedback form in a new tab to let us know how this document benefits oy u. Follow this and additional works at: https://uknowledge.uky.edu/physiology_facpub Part of the Genomics Commons, and the Physiology Commons Repository Citation Nickell, Melissa D.; Breheny, Patrick; Stromberg, Arnold J.; and McClintock, Timothy S., "Genomics of Mature and Immature Olfactory Sensory Neurons" (2012). Physiology Faculty Publications. 66. https://uknowledge.uky.edu/physiology_facpub/66 This Article is brought to you for free and open access by the Physiology at UKnowledge. It has been accepted for inclusion in Physiology Faculty Publications by an authorized administrator of UKnowledge. For more information, please contact [email protected]. Genomics of Mature and Immature Olfactory Sensory Neurons Notes/Citation Information Published in Journal of Comparative Neurology, v. 520, issue 12, p. 2608-2629. Copyright © 2012 Wiley Periodicals, Inc. This is the peer reviewed version of the following article: Nickell, M. D., Breheny, P., Stromberg, A. J., and McClintock, T. S. (2012). Genomics of mature and immature olfactory sensory neurons. Journal of Comparative Neurology, 520: 2608–2629, which has been published in final form at http://dx.doi.org/ 10.1002/cne.23052. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving.
    [Show full text]
  • Agrin Controls Synaptic Differentiation in Hippocampal Neurons
    The Journal of Neuroscience, December 15, 2000, 20(24):9086–9095 Agrin Controls Synaptic Differentiation in Hippocampal Neurons Christian M. Bo¨ se,1 Dike Qiu,1 Andrea Bergamaschi,3 Biagio Gravante,3 Mario Bossi,2 Antonello Villa,2 Fabio Rupp,1 and Antonio Malgaroli3 1Department of Neuroscience, The Johns Hopkins University, School of Medicine, Baltimore, Maryland 21205, 2Microscopy and Image Analysis, University of Milan School of Medicine, and 3Department of Biological and Technological Research, Scientific Institute San Raffaele, 20123 Milano, Italy Agrin controls the formation of the neuromuscular junction. agrin and could not be detected in cultures from agrin-deficient Whether it regulates the differentiation of other types of synapses animals. Interestingly, the few synapses formed in reduced agrin remains unclear. Therefore, we have studied the role of agrin in conditions displayed diminished vesicular turnover, despite a cultured hippocampal neurons. Synaptogenesis was severely normal appearance at the EM level. Thus, our results demon- compromised when agrin expression or function was sup- strate the necessity of agrin for synaptogenesis in hippocampal pressed by antisense oligonucleotides and specific antibodies. neurons. The effects of antisense oligonucleotides were found to be highly Key words: agrin; synaptogenesis; synapses; primary hip- specific because they were reversed by adding recombinant pocampal neurons; agrin antibodies; antisense oligonucleotides The fidelity of neural transmission depends on interactions of a can be detected in CNS neurons, where the temporal pattern of large number of presynaptic and postsynaptic molecules. Despite expression of agrin parallels synaptogenesis (Hoch et al., 1993; the importance of these processes for neural communication, the O’Connor et al., 1994; Stone and Nikolics, 1995; N.
    [Show full text]
  • Agrin Promotes Synaptic Differentiation by Counteracting an Inhibitory Effect of Neurotransmitter
    Agrin promotes synaptic differentiation by counteracting an inhibitory effect of neurotransmitter Thomas Misgeld*, Terrance T. Kummer*, Jeff W. Lichtman, and Joshua R. Sanes† Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138; and Department of Anatomy and Neurobiology, Washington University Medical School, St Louis, MO 63110 Contributed by Joshua R. Sanes, June 9, 2005 Synaptic organizing molecules and neurotransmission regulate bryos than in controls (10), suggesting that ACh could actually synapse development. Here, we use the skeletal neuromuscular antagonize postsynaptic differentiation. junction to assess the interdependence of effects evoked by an Here, using agrnϪ/Ϫ and chatϪ/Ϫ mice that we previously essential synaptic organizing protein, agrin, and the neuromuscu- generated and characterized, we reassess agrin’s role and ask lar transmitter, acetylcholine (ACh). Mice lacking agrin fail to whether ACh is the nerve-derived factor that antagonizes syn- maintain neuromuscular junctions, whereas neuromuscular syn- aptic differentiation. Using double-mutant mice, we show that apses differentiate extensively in the absence of ACh. We now synapses do form in the absence of agrin provided that ACh is demonstrate that agrin’s action in vivo depends critically on cho- also absent. We then provide evidence from cultured muscle linergic neurotransmission. Using double-mutant mice, we show cells that ACh destabilizes nascent postsynaptic sites, and that that synapses do form in the absence of agrin provided that ACh one critical physiological role of agrin is to counteract this is also absent. We provide evidence that ACh destabilizes nascent ‘‘antisynaptogenic’’ influence. postsynaptic sites, and that one major physiological role of agrin Methods is to counteract this ‘‘antisynaptogenic’’ influence.
    [Show full text]
  • Specific Proteolytic Cleavage of Agrin Regulates Maturation of the Neuromuscular Junction
    3944 Research Article Specific proteolytic cleavage of agrin regulates maturation of the neuromuscular junction Marc F. Bolliger1,*, Andreas Zurlinden1,2,*, Daniel Lüscher1,*, Lukas Bütikofer1, Olga Shakhova1, Maura Francolini3, Serguei V. Kozlov1, Paolo Cinelli1, Alexander Stephan1, Andreas D. Kistler1, Thomas Rülicke4,‡, Pawel Pelczar4, Birgit Ledermann4, Guido Fumagalli5, Sergio M. Gloor1, Beat Kunz1 and Peter Sonderegger1,§ 1Department of Biochemistry, University of Zurich, 8057 Zurich, Switzerland 2Neurotune AG, 8952 Schlieren, Switzerland 3Department of Medical Pharmacology, University of Milan, 20129 Milan, Italy 4Institute of Laboratory Animal Science, University of Zurich, 8091 Zurich, Switzerland 5Department of Medicine and Public Health, University of Verona, 37134 Verona, Italy *These authors contributed equally to this work ‡Present address: Vetmeduni Vienna, 1210 Vienna, Austria §Author for correspondence ([email protected]) Accepted 5 August 2010 Journal of Cell Science 123, 3944-3955 © 2010. Published by The Company of Biologists Ltd doi:10.1242/jcs.072090 Summary During the initial stage of neuromuscular junction (NMJ) formation, nerve-derived agrin cooperates with muscle-autonomous mechanisms in the organization and stabilization of a plaque-like postsynaptic specialization at the site of nerve–muscle contact. Subsequent NMJ maturation to the characteristic pretzel-like appearance requires extensive structural reorganization. We found that the progress of plaque-to-pretzel maturation is regulated by agrin.
    [Show full text]
  • Hud and the Survival Motor Neuron Protein Interact in Motoneurons and Are Essential for Motoneuron Development, Function, and Mrna Regulation
    The Journal of Neuroscience, November 29, 2017 • 37(48):11559–11571 • 11559 Neurobiology of Disease HuD and the Survival Motor Neuron Protein Interact in Motoneurons and Are Essential for Motoneuron Development, Function, and mRNA Regulation Thi Hao le,1 Phan Q. Duy,1* Min An,1 Jared Talbot,2,3 Chitra C. Iyer,2 Marc Wolman,4 and Christine E. Beattie1 1Wexner Medical Center Department of Neuroscience, 2Department of Biochemistry and Pharmacology, and 3Department of Molecular Genetics and Center for Muscle Health and Neuromuscular Disorders, Ohio State University, Columbus, Ohio 43210, and 4Department of Zoology, University of Wisconsin, Madison, Wisconsin 53706 Motoneurons establish a critical link between the CNS and muscles. If motoneurons do not develop correctly, they cannot form the required connections, resulting in movement defects or paralysis. Compromised development can also lead to degeneration because the motoneuron is not set up to function properly. Little is known, however, regarding the mechanisms that control vertebrate motoneuron development, particularly the later stages of axon branch and dendrite formation. The motoneuron disease spinal muscular atrophy (SMA) is caused by low levels of the survival motor neuron (SMN) protein leading to defects in vertebrate motoneuron development and synapse formation. Here we show using zebrafish as a model system that SMN interacts with the RNA binding protein (RBP) HuD in motoneurons in vivo during formation of axonal branches and dendrites. To determine the function of HuD in motoneurons, we generated zebrafish HuD mutants and found that they exhibited decreased motor axon branches, dramatically fewer dendrites, and movement defects. These same phenotypes are present in animals expressing low levels of SMN, indicating that both proteins function in motoneuron development.
    [Show full text]
  • Immunofluorescence Investigations on Neuroendocrine Secretory Protein 55 (NESP55) in Nervous Tissues
    Department of Medical Chemistry and Cell Biology, Institute of Biomedicine, Sahlgrenska Academy, Göteborg University, Göteborg, Sweden Immunofluorescence Investigations on Neuroendocrine Secretory Protein 55 (NESP55) in Nervous Tissues Yongling Li 李永灵 Göteborg 2008 1 Cover picture Confocal images showing the intracellular distribution of NESP55-IR (green), as compared to TGN38-IR (red), in preganglionic sympathetic neurons (top panel) and spinal motoneurons (lower panel) in the rat. Printed in Sweden by Geson, Göteborg 2008 ISBN 978-91-628-7489-6 2 CONTENTS ABSTRACT ...................................................................................................................5 ABBREVIATION...........................................................................................................6 LIST OF PAPERS ..........................................................................................................7 INTRODUCTION ..........................................................................................................9 Chromogranins..........................................................................................................9 Chromogranin family members ...............................................................................9 Structural properties ..............................................................................................10 Tissue distribution and subcellular localization...................................................... 10 Intracellular and extracellular functions ................................................................
    [Show full text]
  • Investigation of Tumor Cell Intrinsic and Extrinsic Regulators Of
    INVESTIGATION OF TUMOR CELL INTRINSIC AND EXTRINSIC REGULATORS OF PANCREATIC NEUROENDOCRINE TUMORIGENESIS by Karen Elizabeth Hunter A Dissertation Presented to the Faculty of the Louis V. Gerstner, Jr. Graduate School of Biomedical Sciences, Memorial Sloan-Kettering Cancer Center in Partial Fulfillment of the Requirements for the Degree of Doctor of Philosophy New York, NY November, 2012 Johanna A Joyce, PhD Dissertation Mentor Copyright by Karen E. Hunter 2012 DEDICATION To my parents, for all of their love and support. iii ABSTRACT Pancreatic neuroendocrine tumors (PanNETs) are a relatively rare, but clinically challenging tumor type, due to their marked disease heterogeneity and limited understanding of the molecular basis for their development. The objective of my thesis research is to identify tumor cell intrinsic and extrinsic regulators of PNET pathogenesis using patient samples in combination with the RT2 mouse model of insulinoma. Heparanase is a matrix-remodeling enzyme, which cleaves heparan sulfate side chains within heparan sulfate proteoglycans, an abundant component of the extracellular matrix. Using tumor tissue microarrays obtained from patients with well-differentiated PanNETs we have found that heparanase expression is significantly correlated with increased malignancy and metastasis in patients with PanNETs. To elucidate the mechanisms by which heparanase promotes pancreatic neuroendocrine tumors we utilized the RIP1-Tag2 (RT2) transgenic mouse model crossed to transgenic mice that constitutively overexpress human heparanase (Hpa-Tg) or heparanase knockout RT2 mice to examine the effects of genetically modulating heparanase levels in vivo. Our analysis revealed that heparanase promotes tumor invasion, and that this invasion is both tumor cell- and macrophage-derived. Further characterization of Hpa-Tg RT2 mice revealed a significant increase in peritumoral lymphangiogenesis in vivo and that Hpa-Tg macrophages have an increased iv ability to form lymphatic endothelial-like structures in cell culture.
    [Show full text]
  • How to Build and to Protect the Neuromuscular Junction: the Role of the Glial Cell Line-Derived Neurotrophic Factor
    International Journal of Molecular Sciences Review How to Build and to Protect the Neuromuscular Junction: The Role of the Glial Cell Line-Derived Neurotrophic Factor Serena Stanga 1,2,3,* , Marina Boido 1,2,3 and Pascal Kienlen-Campard 4 1 Department of Neuroscience Rita Levi Montalcini, University of Turin, 10126 Turin, Italy; [email protected] 2 Laboratory of Brain Development and Disease, Neuroscience Institute Cavalieri Ottolenghi, University of Turin, 10043 Orbassano, Italy 3 National Institute of Neuroscience (INN), 10125 Turin, Italy 4 Institute of Neuroscience (IoNS), Université Catholique de Louvain (UCLouvain), 1200 Bruxelles, Belgium; [email protected] * Correspondence: [email protected] Abstract: The neuromuscular junction (NMJ) is at the crossroad between the nervous system (NS) and the muscle. Following neurotransmitter release from the motor neurons (MNs), muscle contraction occurs and movement is generated. Besides eliciting muscle contraction, the NMJ represents a site of chemical bidirectional interplay between nerve and muscle with the active participation of Schwann cells. Indeed, signals originating from the muscle play an important role in synapse formation, stabilization, maintenance and function, both in development and adulthood. We focus here on the contribution of the Glial cell line-Derived Neurotrophic Factor (GDNF) to these processes and to its potential role in the protection of the NMJ during neurodegeneration. Historically related to the maintenance and survival of dopaminergic neurons of the substantia nigra, GDNF also plays a fundamental role in the peripheral NS (PNS). At this level, it promotes muscle trophism and it participates to the functionality of synapses. Moreover, compared to the other neurotrophic factors, GDNF shows unique peculiarities, which make its contribution essential in neurodegenerative Citation: Stanga, S.; Boido, M.; disorders.
    [Show full text]
  • Understanding Neuronal Connectivity Through the Post-Transcriptional Toolkit
    Downloaded from genesdev.cshlp.org on September 25, 2021 - Published by Cold Spring Harbor Laboratory Press REVIEW Understanding neuronal connectivity through the post-transcriptional toolkit Carlos M. Loya,2 David Van Vactor,1 and Tudor A. Fulga Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA Post-transcriptional regulatory mechanisms have emerged the mid-20th century (Sperry 1963) that neural projec- as a critical component underlying the diversification tions must possess chemical ‘‘tags’’ to specifically guide and spatiotemporal control of the proteome during neurites (i.e., axons or dendrites) to their final destina- the establishment of precise neuronal connectivity. tions and promote synapse differentiation, morphogene- These mechanisms have been shown to be important sis, and function. This suggested the requirement for for virtually all stages of assembling a neural network, possibly billions of chemically distinct neuronal branches from neurite guidance, branching, and growth to synapse and synaptic sites. However, given that our genome is morphogenesis and function. From the moment a gene is composed of only 3 3 104 genes, this implies that am- transcribed, it undergoes a series of post-transcriptional plification of genomic information must be responsible regulatory modifications in the nucleus and cytoplasm for this staggering intricacy. Interestingly, studies of ax- until its final deployment as a functional protein. Ini- onal guidance and synaptogenesis have revealed that tially, a message is subjected to extensive structural a shared and relatively small number of signaling factors regulation through alternative splicing, which is capable and pathways such as Netrins, Ephrins, Wnts, and BMPs of greatly expanding the protein repertoire by generating, are involved in this developmental continuum of es- in some cases, thousands of functionally distinct iso- tablishing neuronal connectivity (Karlstrom et al.
    [Show full text]
  • The Role of Α-Synuclein in the Pathology of Murine
    The role of -synuclein in the pathology of murine Mucopolysaccharidosis type IIIA Kyaw Kyaw Soe (MBBS, MSc) Lysosomal Diseases Research Unit South Australian Health and Medical Research Institute and Department of Paediatrics School of Medicine, Faculty of Health Sciences University of Adelaide Thesis submitted for the degree of Doctor of Philosophy January 2017 TABLE OF CONTENTS List of abbreviations VIII Thesis abstract IX Declaration XI Acknowledgements XII Chapter (1): Introduction and preliminary review 1.1 General introduction 1 1.2 The lysosome and its functions 2 1.3 Biosynthesis of lysosomal enzymes 5 1.4 Functions of mannose-6-phosphate receptors 5 1.5 Lysosomal storage disorders 6 1.6 The mucopolysaccharidoses (MPS) 6 1.7 Sanfilippo syndrome 9 1.8 Sanfilippo syndrome type A (MPS type IIIA) 10 1.9 Clinical presentations of Sanfilippo syndrome 13 1.10 Diagnosis and therapeutic approaches for MPS disorders 15 1.11 MPS IIIA animal models 16 1.12 Primary storage pathology: glycosaminoglycans 18 1.12.1 Structure and functions of glycosaminoglycans 18 1.12.2 Degradation of glycosaminoglycans 19 1.12.3 Heparan sulphate metabolism 19 1.13 Secondary pathology 23 1.13.1 Gangliosides, microglia, neuroinflammation and cell death 23 1.13.2 Secondary proteinaceous accumulation 24 1.13.3 -Synuclein accumulation in lysosomal storage disorders 25 1.14 Cellular protein degradation pathways 26 1.15 The synuclein family 30 1.16 The -synuclein protein 31 II 1.16.1 Structure and location of -synuclein 31 1.16.2 Structural components of -synuclein
    [Show full text]