DOCSLIB.ORG

Neuroscience

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Neuroscience CATALOG OF ANTIBODIES FOR NEUROSCIENCE For research purposes only. Not for use in humans. Prices subject to change. FAX: 303.730.1966 • WEB: www.novusbio.com 2 Table of Contents Neuroscience Antibodies Neurodegenerative Conditions .. 2-9 Neurodegenerative Conditions ..............2-9 Mitochondrial Dynamics ....................................2 Parkinson’s Disease ...................................... 3-5 SensorySensoryS Systemsystems ...............10-13 Alzheimer’s Disease ..................................... 5-7 Huntington’s Disease ........................................8 Amyotrophic Lateral Sclerosis ............................9 ChannelsCh l ........................14-15 Sensory Systems ................................10-13 Vision ..................................................... 10-13 TRPM2 Hearing ......................................................... 13 Signaling ........................16-17 Channels ............................................14-15 Voltage-gated ......................................... 14-15 TRP ............................................................... 15 NeuralNe ral Cell Markers Marke .........18-20 Signaling ...........................................16-17 SOD1 Neurotrophins ......................................... 17 Neural Cell Markers ..........................18-20 GPCR, NMDA Receptors, In the News .....................21-22 GPCR ........................................................ 21 NMDA Receptors...................................... 21 Application Key New Publications ..................................... 22 Vimentin ELISA - Elisa FACS - Fluorescent Activated Cell Sorting ICC - Immunocytochemistry IF - Immunofluorescence IHC - Immunohistochemistry IHC-Fr - Immunohistochemistry Frozen IHC-P - Immunohistochemistry Paraffin IP - Immunoprecipitation WB - Western Blot Reactivity Key Av - Avian Ma - Mammal Bv - Bovine Mk - Monkey Ca - Canine Mu - Mouse Ch - Chicken Po - Porcine Eq - Equine Rb - Rabbit GAPDH Fe - Feline Rt - Rat About the Cover Image Gp - Guinea Pig Sh - Sheep Quadruple fluorescence image of mouse retina stained to reveal the distribution of GFAP in glial Xp - Xenopus Ha - Hamster cells (green), f-actin in endothelial cells (blue), neurofilament 68kd in optic nerve axons (red), and Hu - Human Ze - Zebra Fish DNA/RNA in cell nuclei and cytoplasm (orange). Daily product updates! 1 TOLL FREE: 888.506.6887 • PHONE: 303.730.1950 www.novusbio.com Mitochondrial Dynamics Mitochondria in healthy cells constantly cycle through Problems with mitochondrial fusion and fission and fusion. These mitochondrial dynamics are fission can be responsible for cell death leading to essential for mitochondrial energy production as well as organism death in the fetal stages or neurodegenerative regulation of cell proliferation and death via apoptosis. conditions such as Parkinson’s disease later in life. DRP1 DRP1 Antibody DRP1 Antibody NB110-55237 NB110-55288 A human dynamin-related protein, DRP1 Staining of renal Staining of renal contributes to mitochondrial division in tubular epithelium tubular epithelium and visceral mammalian cells. It plays this important role and visceral epithelial cells epithelial in mitochondrial fission at steady state and of glomerulus cells of the during apoptosis. DRP1 is required for proper using NB110-55237. glomerulus using NB110-55288. cellular distribution of mitochondria and is Species: Hu, Mu Species: Hu, Mu important in regulating apoptosis and Applications: IHC, WB Applications: IHC, WB triggering cell death through increased DRP1 Antibody DRP1 Antibody mitochondrial fission. Overexpression NB110-55237 NB110-55288 promotes apoptosis. Detection of Lane 1: DRP1 DRP-1 in mouse knockout embryonic Lane 2: Detection fibroblast of DRP-1 in post-nuclear wildtype MEF extracts using lysates using Sample NB110-55237. NB110-55288. Species: Hu, Mu Species: Hu, Mu sizes are Applications: IHC, WB Applications: IHC, WB available for all products on this page. Mitofusin 1 Mitofusin1 Antibody Mitofusin1 Antibody A GTPase embedded in the outer membrane NB110-58853 NB110-58853 of the mitochondrion, Mfn1, along with Intracellular staining of MFN-1 Detection of Mfn2, is an essential promoter of MFN1 using in neuronal cell mitochondrial fusion in mammalian cells. body detected in NB110-58853. sectioned human Overexpression of Mfn1 causes extensive brain using tethering of mitochondria and an inhibition NB110-58853. of apoptosis. Mfn1 is crucial to mediating Species: Hu, Mu Species: Hu, Mu Applications: IHC, WB Applications: IHC, WB the cycled balance between mitochondrial fusion and fission in mammalian cells. OPA1 OPA1 is a dynamin-related protein on the OPA1 Antibody OPA1 Antibody NB110-55290 NB110-55290 inner membrane of the mitochondrion and Staining in Detection of is required for mitochondrial fusion. OPA1 is prostatic smooth Opa-1 in muscle and similar to dynamin-GTPases such as post-nuclear glandular extracts of mouse mitofusin 1. OPA1 is required for regulation epithelium using embryonic NB110-55290. of apoptosis via mitochondrial fusion. fibroblasts using Mutations in the OPA1 gene cause the NB110-55290. Species: Hu, Mu Species: Hu, Mu dominant disease Optic Atrophy type 1. Applications: IHC, WB Applications: IHC, WB For research purposes only. Not for use in humans. Prices subject to change. FAX: 303.730.1966 • WEB: www.novusbio.com 4 Parkinson’s Disease Parkinson’s Disease (PD) is a neurodegenerative develop inside neural cells and displace other cellular condition that primarily affects motor coordination. contents in PD, leading to the neurodegeneration that is PD generally affects the elderly, although early-onset characteristic of the disease. cases do occur. Protein aggregates called Lewy bodies Alpha Synuclein Alpha-synuclein is a presynaptic neuronal Alpha synuclein Antibody Alpha synuclein Antibody [Ser129] protein that is thought to be involved NB110-57475 NB110-57476 in the formation of SNARE complexes. Immunofluores- Detection of cent staining of phospho-alpha Alpha-synuclein aggregations are a major PC12 cells using synuclein in fetal component of the Lewy bodies that cause NB110-57475. brain lysates using NB110-57476. Parkinson’s Disease. Alpha-synuclein aggregations can also be found in other Species: Hu, Mu, Rt Species: Hu neurodegenerative conditions. Mutations in Applications: ICC, WB Applications: WB alpha-synuclein, thought to be responsible for this aggregation, are linked to familial Parkinson’s Disease. DJ-1 (PARK7) DJ-1 Antibody DJ-1 Antibody DJ-1 (PARK7) is related to autosomal- NB300-270 NB100-2272 recessive early-onset Parkinsonism. DJ-1 Staining of Detection of Human works with alpha-synuclein to protect human cortex DJ-1 in HeLa whole using cell extracts using neuronal cells from oxidative damage, and NB300-270. NB100-2272. downregulation or mutation of DJ-1 eliminates this protection, leading to neural degeneration. Several distinct types of DJ-1 Species: Hu, Mu Species: Hu Applications: ICC, IHC, IP, WB Applications: IP, WB mutations have been linked to PD. LRRK2 (PARK8) This gene is a member of the leucine-rich repeat kinase domain, an MLK-like domain, and a WD40 domain. family and encodes a protein with an ankryin repeat The protein is present largely in the cytoplasm but also region, a leucine-rich repeat (LRR) domain, a kinase associates with the mitochondrial outer membrane. domain, a DFG-like motif, a RAS domain, a GTPase Mutations in this gene have been associated with PD. LRRK2 Antibody LRRK2 Antibody LRRK2 Antibody NB300-268 NB300-267 NB110-55289 Detection of Staining of Staining of LRRK2 in neurons and glia neurons and glia transfected mouse in human brain in mouse brain CAD cells using using NB300-267. using NB110-55289. NB300-268. Species: Bv, Hu Species: Hu Species: Mu Applications: IF, IHC, IP, WB Applications: IHC-P, WB Applications: IHC-P, WB Daily product updates! 5 TOLL FREE: 888.506.6887 • PHONE: 303.730.1950 www.novusbio.com LRRK2 Antibody LRRK2LR Antibody LRRK2 Antibody NB110-58771 NEW NB110-78625N NB110-78628 Staining Detection of Detection of of mouse LRRK2 in LRRK2 in brainstem human brain using human brain using NB110-78625. using NB110-78628. NB110-58771. Species: Hu, Mu Species: Hu Species: Hu Applications: IHC-Fr, WB Applications: WB Applications: WB 1. [LRRK2 NB300-267] Kingsbury AE, Sancho RM, Law B, Caley A, Lees AJ, Harvey K. Interaction of the Multidomain Protein Lrrk2 with Tubulin. 12th International Congress of Parkinson Disease and Movement Disorders; June 22 2008. Chicago, IL; USA. 2. [LRRK2 NB300-268] Melrose, HL, et al. A comparative analysis of leucine-rich repeat kinase 2 (Lrrk2) expression in mouse brain and Lewy Body disease. Neurosci. 147: 1047-1058 (2007) [Western Blot, Immunohistochemistry] Parkin Mutations in the Parkin (PARK2) gene appear to be of abnormally folded or damaged protein. Loss of this responsible for autosomal recessive juvenile Parkin- ubiquitin ligase activity appears to be the mechanism sonism. Parkin plays a role in the ubiquitin-mediated underlying pathogenesis of Parkin. proteolytic pathway by removal and/or detoxification Parkin Antibody ParkinP Antibody [Ser101] Parkin Antibody [Ser378] NB110-57319 NEW NB100-61106N NB100-61107 Staining of Detection of Parkin Detection of Parkin paraffin-embedded [Ser101] using [Ser378] using human brain using NB100-61106. NB100-61107. NB110-57319. A. HEK293 cells A. HEK293 cells transfected with transfected with phospho Parkin. phospho Parkin. B. HEK293 non- B. HEK293 non- Species: Hu, Mu, Rt Species: Hu phospho
Load more

Recommended publications
  • 1 Evidence for Gliadin Antibodies As Causative Agents in Schizophrenia
    1 Evidence for gliadin antibodies as causative agents in schizophrenia. C.J.Carter PolygenicPathways, 20 Upper Maze Hill, Saint-Leonard’s on Sea, East Sussex, TN37 0LG [email protected] Tel: 0044 (0)1424 422201 I have no fax Abstract Antibodies to gliadin, a component of gluten, have frequently been reported in schizophrenia patients, and in some cases remission has been noted following the instigation of a gluten free diet. Gliadin is a highly immunogenic protein, and B cell epitopes along its entire immunogenic length are homologous to the products of numerous proteins relevant to schizophrenia (p = 0.012 to 3e-25). These include members of the DISC1 interactome, of glutamate, dopamine and neuregulin signalling networks, and of pathways involved in plasticity, dendritic growth or myelination. Antibodies to gliadin are likely to cross react with these key proteins, as has already been observed with synapsin 1 and calreticulin. Gliadin may thus be a causative agent in schizophrenia, under certain genetic and immunological conditions, producing its effects via antibody mediated knockdown of multiple proteins relevant to the disease process. Because of such homology, an autoimmune response may be sustained by the human antigens that resemble gliadin itself, a scenario supported by many reports of immune activation both in the brain and in lymphocytes in schizophrenia. Gluten free diets and removal of such antibodies may be of therapeutic benefit in certain cases of schizophrenia. 2 Introduction A number of studies from China, Norway, and the USA have reported the presence of gliadin antibodies in schizophrenia 1-5. Gliadin is a component of gluten, intolerance to which is implicated in coeliac disease 6.
    [Show full text]
  • Viewed Under 23 (B) Or 203 (C) fi M M Male Cko Mice, and Largely Unaffected Magni Cation; Scale Bars, 500 M (B) and 50 M (C)
    BRIEF COMMUNICATION www.jasn.org Renal Fanconi Syndrome and Hypophosphatemic Rickets in the Absence of Xenotropic and Polytropic Retroviral Receptor in the Nephron Camille Ansermet,* Matthias B. Moor,* Gabriel Centeno,* Muriel Auberson,* † † ‡ Dorothy Zhang Hu, Roland Baron, Svetlana Nikolaeva,* Barbara Haenzi,* | Natalya Katanaeva,* Ivan Gautschi,* Vladimir Katanaev,*§ Samuel Rotman, Robert Koesters,¶ †† Laurent Schild,* Sylvain Pradervand,** Olivier Bonny,* and Dmitri Firsov* BRIEF COMMUNICATION *Department of Pharmacology and Toxicology and **Genomic Technologies Facility, University of Lausanne, Lausanne, Switzerland; †Department of Oral Medicine, Infection, and Immunity, Harvard School of Dental Medicine, Boston, Massachusetts; ‡Institute of Evolutionary Physiology and Biochemistry, St. Petersburg, Russia; §School of Biomedicine, Far Eastern Federal University, Vladivostok, Russia; |Services of Pathology and ††Nephrology, Department of Medicine, University Hospital of Lausanne, Lausanne, Switzerland; and ¶Université Pierre et Marie Curie, Paris, France ABSTRACT Tight control of extracellular and intracellular inorganic phosphate (Pi) levels is crit- leaves.4 Most recently, Legati et al. have ical to most biochemical and physiologic processes. Urinary Pi is freely filtered at the shown an association between genetic kidney glomerulus and is reabsorbed in the renal tubule by the action of the apical polymorphisms in Xpr1 and primary fa- sodium-dependent phosphate transporters, NaPi-IIa/NaPi-IIc/Pit2. However, the milial brain calcification disorder.5 How- molecular identity of the protein(s) participating in the basolateral Pi efflux remains ever, the role of XPR1 in the maintenance unknown. Evidence has suggested that xenotropic and polytropic retroviral recep- of Pi homeostasis remains unknown. Here, tor 1 (XPR1) might be involved in this process. Here, we show that conditional in- we addressed this issue in mice deficient for activation of Xpr1 in the renal tubule in mice resulted in impaired renal Pi Xpr1 in the nephron.
    [Show full text]
  • Table 1. Identified Proteins with Expression Significantly Altered in the Hippocampus of Rats of Exposed Group (Pb) Vs
    Table 1. Identified proteins with expression significantly altered in the hippocampus of rats of exposed group (Pb) vs. Control. Fold Change Accession Id a Protein Description Score Pb P35213 14-3-3 protein beta/alpha 85420 −0.835 P62260 14-3-3 protein epsilon 96570 −0.878 P68511 14-3-3 protein eta 85420 −0.844 P68255 14-3-3 protein theta 85420 −0.835 P63102 14-3-3 protein zeta/delta 105051 −0.803 P13233 2',3'-cyclic-nucleotide 3'-phosphodiesterase 151400 1.405 P68035 Actin, alpha cardiac muscle 1 442584 −0.942 P68136 Actin, alpha skeletal muscle 441060 −0.970 P62738 Actin, aortic smooth muscle 438270 −0.970 P60711 Actin, cytoplasmic 1 630104 −0.942 P63259 Actin, cytoplasmic 2 630104 −0.942 P63269 Actin, gamma-enteric smooth muscle 438270 −0.951 Q05962 ADP/ATP translocase 1 60100 −0.554 Q09073 ADP/ATP translocase 2 49102 −0.482 P84079 ADP-ribosylation factor 1 34675 −0.644 P84082 ADP-ribosylation factor 2 22412 −0.644 P61206 ADP-ribosylation factor 3 34675 −0.619 P61751 ADP-ribosylation factor 4 22412 −0.670 P84083 ADP-ribosylation factor 5 22412 −0.625 P04764 Alpha-enolase 46219 −0.951 P23565 Alpha-internexin 9478 1.062 P37377 Alpha-synuclein 89619 −0.771 P13221 Aspartate aminotransferase, cytoplasmic 23661 1.083 P00507 Aspartate aminotransferase, mitochondrial 46049 1.116 P10719 ATP synthase subunit beta, mitochondrial 232442 −0.835 P85969 Beta-soluble NSF attachment protein 9638 1.419 Q63754 Beta-synuclein 66842 −0.779 P11275 Calcium/calmodulin-dependent protein kinase type II subunit alpha 181954 1.105 P08413 Calcium/calmodulin-dependent protein kinase type II subunit beta 80840 1.127 P15791 Calcium/calmodulin-dependent protein kinase type II subunit delta 62682 1.105 Int.
    [Show full text]
  • Potassium Channels in Epilepsy
    Downloaded from http://perspectivesinmedicine.cshlp.org/ on September 28, 2021 - Published by Cold Spring Harbor Laboratory Press Potassium Channels in Epilepsy Ru¨diger Ko¨hling and Jakob Wolfart Oscar Langendorff Institute of Physiology, University of Rostock, Rostock 18057, Germany Correspondence: [email protected] This review attempts to give a concise and up-to-date overview on the role of potassium channels in epilepsies. Their role can be defined from a genetic perspective, focusing on variants and de novo mutations identified in genetic studies or animal models with targeted, specific mutations in genes coding for a member of the large potassium channel family. In these genetic studies, a demonstrated functional link to hyperexcitability often remains elusive. However, their role can also be defined from a functional perspective, based on dy- namic, aggravating, or adaptive transcriptional and posttranslational alterations. In these cases, it often remains elusive whether the alteration is causal or merely incidental. With 80 potassium channel types, of which 10% are known to be associated with epilepsies (in humans) or a seizure phenotype (in animals), if genetically mutated, a comprehensive review is a challenging endeavor. This goal may seem all the more ambitious once the data on posttranslational alterations, found both in human tissue from epilepsy patients and in chronic or acute animal models, are included. We therefore summarize the literature, and expand only on key findings, particularly regarding functional alterations found in patient brain tissue and chronic animal models. INTRODUCTION TO POTASSIUM evolutionary appearance of voltage-gated so- CHANNELS dium (Nav)andcalcium (Cav)channels, Kchan- nels are further diversified in relation to their otassium (K) channels are related to epilepsy newer function, namely, keeping neuronal exci- Psyndromes on many different levels, ranging tation within limits (Anderson and Greenberg from direct control of neuronal excitability and 2001; Hille 2001).
    [Show full text]
  • Transient Receptor Potential Channel Promiscuity Frustrates Constellation
    the sole sensor responsible for noxious cold responses in M+A+ LETTER neurons (1). However, TRPA1 is also activated by cooling and underlies at least part of the noxious cold responsiveness of Transient receptor potential channel AITC-sensitive neurons (3). Third, the authors used nicardipine 2+ promiscuity frustrates to selectively inhibit CaV1-type voltage-gated Ca channels (1). However, several dihydropyridines, including nicardipine, also constellation pharmacology act as TRPA1 agonists (4). These considerations led us to propose an alternative Sensory neurons from the trigeminal and dorsal root ganglia molecular interpretation of the difference between M+A− (DRG) have nerve endings in the skin and mucosa, where they and M+A+ neurons, which is in much better agreement with detect environmental stimuli and convey this information to published work. In accord with the authors, we conclude that the central nervous system. Several members of the transient M+A− neurons express TRPM8 but lack expression of receptor potential (TRP) superfamily of ion channels act as TRPA1. In contrast to the authors, we propose that M+A+ prime molecular sensors for thermal and chemical stimuli in neurons express TRPA1 as the prime cold and menthol these sensory neurons. However, it is incompletely understood sensor (2, 3). This interpretation is consistent with published how TRP channel expression and modulation affect the stimulus observations that menthol responses in M+A− but not in sensitivities of distinct neuronal subtypes. M+A+ neurons are inhibited by TRPM8 antagonists (5) In a recent article, Teichert et al. (1) described a “constellation and that TRPA1-mediated responses to cold in neurons are pharmacology approach” to identify and characterize subtypes characterized by a higher (colder) threshold (3).
    [Show full text]
  • A Computational Approach for Defining a Signature of Β-Cell Golgi Stress in Diabetes Mellitus
    Page 1 of 781 Diabetes A Computational Approach for Defining a Signature of β-Cell Golgi Stress in Diabetes Mellitus Robert N. Bone1,6,7, Olufunmilola Oyebamiji2, Sayali Talware2, Sharmila Selvaraj2, Preethi Krishnan3,6, Farooq Syed1,6,7, Huanmei Wu2, Carmella Evans-Molina 1,3,4,5,6,7,8* Departments of 1Pediatrics, 3Medicine, 4Anatomy, Cell Biology & Physiology, 5Biochemistry & Molecular Biology, the 6Center for Diabetes & Metabolic Diseases, and the 7Herman B. Wells Center for Pediatric Research, Indiana University School of Medicine, Indianapolis, IN 46202; 2Department of BioHealth Informatics, Indiana University-Purdue University Indianapolis, Indianapolis, IN, 46202; 8Roudebush VA Medical Center, Indianapolis, IN 46202. *Corresponding Author(s): Carmella Evans-Molina, MD, PhD ([email protected]) Indiana University School of Medicine, 635 Barnhill Drive, MS 2031A, Indianapolis, IN 46202, Telephone: (317) 274-4145, Fax (317) 274-4107 Running Title: Golgi Stress Response in Diabetes Word Count: 4358 Number of Figures: 6 Keywords: Golgi apparatus stress, Islets, β cell, Type 1 diabetes, Type 2 diabetes 1 Diabetes Publish Ahead of Print, published online August 20, 2020 Diabetes Page 2 of 781 ABSTRACT The Golgi apparatus (GA) is an important site of insulin processing and granule maturation, but whether GA organelle dysfunction and GA stress are present in the diabetic β-cell has not been tested. We utilized an informatics-based approach to develop a transcriptional signature of β-cell GA stress using existing RNA sequencing and microarray datasets generated using human islets from donors with diabetes and islets where type 1(T1D) and type 2 diabetes (T2D) had been modeled ex vivo. To narrow our results to GA-specific genes, we applied a filter set of 1,030 genes accepted as GA associated.
    [Show full text]
  • Emerging Roles for Multifunctional Ion Channel Auxiliary Subunits in Cancer T ⁎ Alexander S
    Cell Calcium 80 (2019) 125–140 Contents lists available at ScienceDirect Cell Calcium journal homepage: www.elsevier.com/locate/ceca Emerging roles for multifunctional ion channel auxiliary subunits in cancer T ⁎ Alexander S. Hawortha,b, William J. Brackenburya,b, a Department of Biology, University of York, Heslington, York, YO10 5DD, UK b York Biomedical Research Institute, University of York, Heslington, York, YO10 5DD, UK ARTICLE INFO ABSTRACT Keywords: Several superfamilies of plasma membrane channels which regulate transmembrane ion flux have also been Auxiliary subunit shown to regulate a multitude of cellular processes, including proliferation and migration. Ion channels are Cancer typically multimeric complexes consisting of conducting subunits and auxiliary, non-conducting subunits. Calcium channel Auxiliary subunits modulate the function of conducting subunits and have putative non-conducting roles, further Chloride channel expanding the repertoire of cellular processes governed by ion channel complexes to processes such as trans- Potassium channel cellular adhesion and gene transcription. Given this expansive influence of ion channels on cellular behaviour it Sodium channel is perhaps no surprise that aberrant ion channel expression is a common occurrence in cancer. This review will − focus on the conducting and non-conducting roles of the auxiliary subunits of various Ca2+,K+,Na+ and Cl channels and the burgeoning evidence linking such auxiliary subunits to cancer. Several subunits are upregu- lated (e.g. Cavβ,Cavγ) and downregulated (e.g. Kvβ) in cancer, while other subunits have been functionally implicated as oncogenes (e.g. Navβ1,Cavα2δ1) and tumour suppressor genes (e.g. CLCA2, KCNE2, BKγ1) based on in vivo studies. The strengthening link between ion channel auxiliary subunits and cancer has exposed these subunits as potential biomarkers and therapeutic targets.
    [Show full text]
  • 1 Metabolic Dysfunction Is Restricted to the Sciatic Nerve in Experimental
    Page 1 of 255 Diabetes Metabolic dysfunction is restricted to the sciatic nerve in experimental diabetic neuropathy Oliver J. Freeman1,2, Richard D. Unwin2,3, Andrew W. Dowsey2,3, Paul Begley2,3, Sumia Ali1, Katherine A. Hollywood2,3, Nitin Rustogi2,3, Rasmus S. Petersen1, Warwick B. Dunn2,3†, Garth J.S. Cooper2,3,4,5* & Natalie J. Gardiner1* 1 Faculty of Life Sciences, University of Manchester, UK 2 Centre for Advanced Discovery and Experimental Therapeutics (CADET), Central Manchester University Hospitals NHS Foundation Trust, Manchester Academic Health Sciences Centre, Manchester, UK 3 Centre for Endocrinology and Diabetes, Institute of Human Development, Faculty of Medical and Human Sciences, University of Manchester, UK 4 School of Biological Sciences, University of Auckland, New Zealand 5 Department of Pharmacology, Medical Sciences Division, University of Oxford, UK † Present address: School of Biosciences, University of Birmingham, UK *Joint corresponding authors: Natalie J. Gardiner and Garth J.S. Cooper Email: [email protected]; [email protected] Address: University of Manchester, AV Hill Building, Oxford Road, Manchester, M13 9PT, United Kingdom Telephone: +44 161 275 5768; +44 161 701 0240 Word count: 4,490 Number of tables: 1, Number of figures: 6 Running title: Metabolic dysfunction in diabetic neuropathy 1 Diabetes Publish Ahead of Print, published online October 15, 2015 Diabetes Page 2 of 255 Abstract High glucose levels in the peripheral nervous system (PNS) have been implicated in the pathogenesis of diabetic neuropathy (DN). However our understanding of the molecular mechanisms which cause the marked distal pathology is incomplete. Here we performed a comprehensive, system-wide analysis of the PNS of a rodent model of DN.
    [Show full text]
  • Mechanisms of Α-Synuclein Induced Synaptopathy in Parkinson’S Disease
    King’s Research Portal DOI: 10.3389/fnins.2018.00080 Document Version Publisher's PDF, also known as Version of record Link to publication record in King's Research Portal Citation for published version (APA): Bridi, J. C., & Hirth, F. (2018). Mechanisms of -Synuclein Induced Synaptopathy in Parkinson's Disease. Frontiers in Neuroscience, 12, 80. DOI: 10.3389/fnins.2018.00080 Citing this paper Please note that where the full-text provided on King's Research Portal is the Author Accepted Manuscript or Post-Print version this may differ from the final Published version. If citing, it is advised that you check and use the publisher's definitive version for pagination, volume/issue, and date of publication details. And where the final published version is provided on the Research Portal, if citing you are again advised to check the publisher's website for any subsequent corrections. General rights Copyright and moral rights for the publications made accessible in the Research Portal are retained by the authors and/or other copyright owners and it is a condition of accessing publications that users recognize and abide by the legal requirements associated with these rights. •Users may download and print one copy of any publication from the Research Portal for the purpose of private study or research. •You may not further distribute the material or use it for any profit-making activity or commercial gain •You may freely distribute the URL identifying the publication in the Research Portal Take down policy If you believe that this document breaches copyright please contact [email protected] providing details, and we will remove access to the work immediately and investigate your claim.
    [Show full text]
  • Chapter Four – TRPA1 Channels: Chemical and Temperature Sensitivity
    CHAPTER FOUR TRPA1 Channels: Chemical and Temperature Sensitivity Willem J. Laursen1,2, Sviatoslav N. Bagriantsev1,* and Elena O. Gracheva1,2,* 1Department of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, CT, USA 2Program in Cellular Neuroscience, Neurodegeneration and Repair, Yale University School of Medicine, New Haven, CT, USA *Corresponding author: E-mail: [email protected], [email protected] Contents 1. Introduction 90 2. Activation and Regulation of TRPA1 by Chemical Compounds 91 2.1 Chemical activation of TRPA1 by covalent modification 91 2.2 Noncovalent activation of TRPA1 97 2.3 Receptor-operated activation of TRPA1 99 3. Temperature Sensitivity of TRPA1 101 3.1 TRPA1 in mammals 101 3.2 TRPA1 in insects and worms 103 3.3 TRPA1 in fish, birds, reptiles, and amphibians 103 3.4 TRPA1: Molecular mechanism of temperature sensitivity 104 Acknowledgments 107 References 107 Abstract Transient receptor potential ankyrin 1 (TRPA1) is a polymodal excitatory ion channel found in sensory neurons of different organisms, ranging from worms to humans. Since its discovery as an uncharacterized transmembrane protein in human fibroblasts, TRPA1 has become one of the most intensively studied ion channels. Its function has been linked to regulation of heat and cold perception, mechanosensitivity, hearing, inflam- mation, pain, circadian rhythms, chemoreception, and other processes. Some of these proposed functions remain controversial, while others have gathered considerable experimental support. A truly polymodal ion channel, TRPA1 is activated by various stimuli, including electrophilic chemicals, oxygen, temperature, and mechanical force, yet the molecular mechanism of TRPA1 gating remains obscure. In this review, we discuss recent advances in the understanding of TRPA1 physiology, pharmacology, and molecular function.
    [Show full text]
  • Transcriptomic Analysis of Native Versus Cultured Human and Mouse Dorsal Root Ganglia Focused on Pharmacological Targets Short
    bioRxiv preprint doi: https://doi.org/10.1101/766865; this version posted September 12, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-ND 4.0 International license. Transcriptomic analysis of native versus cultured human and mouse dorsal root ganglia focused on pharmacological targets Short title: Comparative transcriptomics of acutely dissected versus cultured DRGs Andi Wangzhou1, Lisa A. McIlvried2, Candler Paige1, Paulino Barragan-Iglesias1, Carolyn A. Guzman1, Gregory Dussor1, Pradipta R. Ray1,#, Robert W. Gereau IV2, # and Theodore J. Price1, # 1The University of Texas at Dallas, School of Behavioral and Brain Sciences and Center for Advanced Pain Studies, 800 W Campbell Rd. Richardson, TX, 75080, USA 2Washington University Pain Center and Department of Anesthesiology, Washington University School of Medicine # corresponding authors [email protected], [email protected] and [email protected] Funding: NIH grants T32DA007261 (LM); NS065926 and NS102161 (TJP); NS106953 and NS042595 (RWG). The authors declare no conflicts of interest Author Contributions Conceived of the Project: PRR, RWG IV and TJP Performed Experiments: AW, LAM, CP, PB-I Supervised Experiments: GD, RWG IV, TJP Analyzed Data: AW, LAM, CP, CAG, PRR Supervised Bioinformatics Analysis: PRR Drew Figures: AW, PRR Wrote and Edited Manuscript: AW, LAM, CP, GD, PRR, RWG IV, TJP All authors approved the final version of the manuscript. 1 bioRxiv preprint doi: https://doi.org/10.1101/766865; this version posted September 12, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity.
    [Show full text]
  • Rescue of Motor Coordination by Purkinje Cell-Targeted Restoration of Kv3.3 Channels in Kcnc3-Null Mice Requires Kcnc1
    The Journal of Neuroscience, December 16, 2009 • 29(50):15735–15744 • 15735 Cellular/Molecular Rescue of Motor Coordination by Purkinje Cell-Targeted Restoration of Kv3.3 Channels in Kcnc3-Null Mice Requires Kcnc1 Edward C. Hurlock, Mitali Bose, Ganon Pierce, and Rolf H. Joho Department of Neuroscience, The University of Texas Southwestern Medical Center, Dallas, Texas 75390-9111 The role of cerebellar Kv3.1 and Kv3.3 channels in motor coordination was examined with an emphasis on the deep cerebellar nuclei (DCN). Kv3 channel subunits encoded by Kcnc genes are distinguished by rapid activation and deactivation kinetics that support high-frequency, narrow action potential firing. Previously we reported that increased lateral deviation while ambulating and slips while traversing a narrow beam of ataxic Kcnc3-null mice were corrected by restoration of Kv3.3 channels specifically to Purkinje cells, whereas Kcnc3-mutant mice additionally lacking one Kcnc1 allele were partially rescued. Here, we report mice lacking all Kcnc1 and Kcnc3 alleles exhibit no such rescue. For Purkinje cell output to reach the rest of the brain it must be conveyed by neurons of the DCN or vestibular nuclei. As Kcnc1, but not Kcnc3, alleles are lost, mutant mice exhibit increasing gait ataxia accompanied by spike broadening and deceleration in DCN neurons, suggesting the facet of coordination rescued by Purkinje-cell-restricted Kv3.3 restoration in mice lacking just Kcnc3 is hypermetria, while gait ataxia emerges when additionally Kcnc1 alleles are lost. Thus, fast repolarization in Purkinje cells appears important for normal movement velocity, whereas DCN neurons are a prime candidate locus where fast repolarization is necessary for normal gait patterning.
    [Show full text]