541
Views
21
CrossRef citations to date
0
Altmetric
Clinical

HSC70 expression is reduced in lymphomonocytes of sporadic ALS patients and contributes to TDP-43 accumulation

, ORCID Icon, , ORCID Icon, , , , , , , , ORCID Icon, ORCID Icon, & ORCID Icon show all
Pages 51-62 | Received 02 Jul 2019, Accepted 16 Sep 2019, Published online: 30 Oct 2019

References

  • Neumann M, Sampathu DM, Kwong LK, Truax AC, Micsenyi MC, Chou TT, et al. Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science. 2006;314:130–3.
  • Arai T, Hasegawa M, Akiyama H, Ikeda K, Nonaka T, Mori H, et al. TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Biochem Biophys Res Commun. 2006;351:602–11.
  • Kim SH, Shi Y, Hanson KA, Williams LM, Sakasai R, Bowler MJ, et al. Potentiation of amyotrophic lateral sclerosis (ALS)-associated TDP-43 aggregation by the proteasome-targeting factor, ubiquilin 1. J Biol Chem. 2009;284:8083–92.
  • Urushitani M, Sato T, Bamba H, Hisa Y, Tooyama I. Synergistic effect between proteasome and autophagosome in the clearance of polyubiquitinated TDP-43. J Neurosci Res. 2010;88:784–97.
  • Wang X, Fan H, Ying Z, Li B, Wang H, Wang G. Degradation of TDP-43 and its pathogenic form by autophagy and the ubiquitin-proteasome system. Neurosci Lett. 2010;469:112–6.
  • Filimonenko M, Stuffers S, Raiborg C, Yamamoto A, Malerød L, Fisher EMC, et al. Functional multivesicular bodies are required for autophagic clearance of protein aggregates associated with neurodegenerative disease. J Cell Biol. 2007;179:485–500.
  • Wang I-F, Guo B-S, Liu Y-C, Wu C-C, Yang C-H, Tsai K-J, et al. Autophagy activators rescue and alleviate pathogenesis of a mouse model with proteinopathies of the TAR DNA-binding protein 43. Proc Natl Acad Sci USA. 2012;109:15024–9.
  • Crippa V, Cicardi ME, Ramesh N, Seguin SJ, Ganassi M, Bigi I, et al. The chaperone HSPB8 reduces the accumulation of truncated TDP-43 species in cells and protects against TDP-43-mediated toxicity. Hum Mol Genet. 2016;25:3908–24.
  • Bendotti C, Marino M, Cheroni C, Fontana E, Crippa V, Poletti A, et al. Dysfunction of constitutive and inducible ubiquitin-proteasome system in amyotrophic lateral sclerosis: implication for protein aggregation and immune response. Prog Neurobiol. 2012;97:101–26.
  • Lee JK, Shin JH, Lee JE, Choi EJ. Role of autophagy in the pathogenesis of amyotrophic lateral sclerosis. Biochim Biophys Acta. 2015;1852:2517–24.
  • Huang C-C, Bose JK, Majumder P, Lee K-H, Huang J-TJ, Huang JK, et al. Metabolism and mis-metabolism of the neuropathological signature protein TDP-43. J Cell Sci. 2014;127:3024–38.
  • Dice JF. Peptide sequences that target cytosolic proteins for lysosomal proteolysis. Trends Biochem Sci 1990;15:305–9.
  • Cuervo AM, Dice JF. Regulation of lamp2a levels in the lysosomal membrane. Traffic. 2000;1:570–83.
  • Cuervo AM, Dice JF. Unique properties of lamp2a compared to other lamp2 isoforms. J Cell Sci. 2000;113(Pt 24):4441–50.
  • Coyne AN, Lorenzini I, Chou C-C, Torvund M, Rogers RS, Starr A, et al. Post-transcriptional inhibition of Hsc70-4/HSPA8 expression leads to synaptic vesicle cycling defects in multiple models of ALS. Cell Rep. 2017;21:110–25.
  • Nardo G, Pozzi S, Pignataro M, Lauranzano E, Spano G, Garbelli S, et al. Amyotrophic lateral sclerosis multiprotein biomarkers in peripheral blood mononuclear cells. PLoS One. 2011;6:e25545.
  • De Marco G, Lomartire A, Calvo A, Risso A, De Luca E, Mostert M, et al. Monocytes of patients with amyotrophic lateral sclerosis linked to gene mutations display altered TDP-43 subcellular distribution. Neuropathol Appl Neurobiol. 2017;43:133–53.
  • De Marco G, Lupino E, Calvo A, Moglia C, Buccinnà B, Grifoni S, et al. Cytoplasmic accumulation of TDP-43 in circulating lymphomonocytes of ALS patients with and without TARDBP mutations. Acta Neuropathol. 2011;121:611–22.
  • Cereda C, Leoni E, Milani P, Pansarasa O, Mazzini G, Guareschi S, et al. Altered intracellular localization of SOD1 in leukocytes from patients with sporadic amyotrophic lateral sclerosis. PLoS One. 2013;8:e75916.
  • Brooks BR. Problems in shortening the time to confirmation of ALS diagnosis: lessons from the 1st Consensus Conference, Chicago, May 1998. Amyotroph Lateral Scler Other Motor Neuron Disord. 2000;1:S3–S7.
  • Tremolizzo L, Ferrarese C, Appollonio I. Exploring limits of neuropsychological screening in ALS: the FAB problem. Amyotroph Lateral Scler Frontotemporal Degener. 2013;14:157–8.
  • Sala G, Stefanoni G, Arosio A, Riva C, Melchionda L, Saracchi E, et al. Reduced expression of the chaperone-mediated autophagy carrier hsc70 protein in lymphomonocytes of patients with Parkinson’s disease. Brain Res. 2014;1546:46–52.
  • Scammell JG, Reynolds PD, Elkhalifa MY, Tucker JA, Moore CM. An EBV-transformed owl monkey B-lymphocyte cell line. In Vitro Cell Dev Biol Anim. 1997;33:88–91.
  • Caputo R, Gianotti R, Grimalt R, Monti M, Alessi E. Soft fibroma-like lesions on the legs of a patient with Kaposi’s sarcoma and lymphedema. Am J Dermatopathol. 1991;13:493–6.
  • Sala G, Brighina L, Saracchi E, Fermi S, Riva C, Carrozza V, et al. Vesicular monoamine transporter 2 mRNA levels are reduced in platelets from patients with Parkinson’s disease. J Neural Transm. 2010;117:1093–8.
  • Crippa V, Sau D, Rusmini P, Boncoraglio A, Onesto E, Bolzoni E, et al. The small heat shock protein B8 (HspB8) promotes autophagic removal of misfolded proteins involved in amyotrophic lateral sclerosis (ALS). Hum Mol Genet. 2010;19:3440–56.
  • Cristofani R, Crippa V, Vezzoli G, Rusmini P, Galbiati M, Cicardi ME, et al. The small heat shock protein B8 (HSPB8) efficiently removes aggregating species of dipeptides produced in C9ORF72-related neurodegenerative diseases. Cell Stress Chaperones. 2018;23:1–12.
  • Sala G, Marinig D, Riva C, Arosio A, Stefanoni G, Brighina L, et al. Rotenone down-regulates HSPA8/hsc70 chaperone protein in vitro: a new possible toxic mechanism contributing to Parkinson’s disease. Neurotoxicology. 2016;54:161.
  • Yang Q, She H, Gearing M, Colla E, Lee M, Shacka JJ, et al. Regulation of neuronal survival factor MEF2D by chaperone-mediated autophagy. Science. 2009;323:124–7.
  • Arosio A, Sala G, Rodriguez-Menendez V, Grana D, Gerardi F, Lunetta C, et al. MEF2D and MEF2C pathways disruption in sporadic and familial ALS patients. Mol Cell Neurosci. 2016;74:10–7.
  • Ayala YM, De Conti L, Avendaño-Vázquez SE, Dhir A, Romano M, D’Ambrogio A, et al. TDP-43 regulates its mRNA levels through a negative feedback loop. EMBO J. 2011;30:277–88.
  • Avendaño-Vázquez SE, Dhir A, Bembich S, Buratti E, Proudfoot N, Baralle FE. Autoregulation of TDP-43 mRNA levels involves interplay between transcription, splicing, and alternative polyA site selection. Genes Dev. 2012;26:1679–84.
  • Chiang HL, Terlecky SR, Plant CP, Dice JF. A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins. Science. 1989;246:382–5.
  • Lüders J, Demand J, Höhfeld J. The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome. J Biol Chem. 2000;275:4613–7.
  • Gamerdinger M, Kaya AM, Wolfrum U, Clement AM, Behl C. BAG3 mediates chaperone-based aggresome-targeting and selective autophagy of misfolded proteins. EMBO Rep. 2011;12:149–56.
  • Rusmini P, Cristofani R, Galbiati M, Cicardi ME, Meroni M, Ferrari V, et al. The role of the heat shock protein B8 (HSPB8) in motoneuron diseases. Front Mol Neurosci. 2017;10:176.
  • Cristofani R, Crippa V, Rusmini P, Cicardi ME, Meroni M, Licata NV, et al. Inhibition of retrograde transport modulates misfolded protein accumulation and clearance in motoneuron diseases. Autophagy. 2017;13:1280–303.
  • Pansarasa O, Bordoni M, Dufruca L, et al. ALS lymphoblastoid cell lines as a considerable model to understand disease mechanisms. Dis Model Mech. 2018;11(3):dmm.031625.
  • Deffit SN, Blum JS. A central role for HSC70 in regulating antigen trafficking and MHC class II presentation. Mol Immunol. 2015;68:85–8.
  • Kettern N, Rogon C, Limmer A, Schild H, Höhfeld J. The Hsc/Hsp70 co-chaperone network controls antigen aggregation and presentation during maturation of professional antigen presenting cells. PLoS One. 2011;6:e16398.
  • Ali KS, Dorgai L, Abrahám M, Hermesz E. Tissue- and stressor-specific differential expression of two hsc70 genes in carp. Biochem Biophys Res Commun. 2003;307:503–9.
  • Watanabe M, Dykes-Hoberg M, Culotta VC, Price DL, Wong PC, Rothstein JD. Histological evidence of protein aggregation in mutant SOD1 transgenic mice and in amyotrophic lateral sclerosis neural tissues. Neurobiol Dis. 2001;8:933–41.
  • Alvarez-Erviti L, Rodriguez-Oroz MC, Cooper JM, Caballero C, Ferrer I, Obeso JA, et al. Chaperone-mediated autophagy markers in Parkinson disease brains. Arch Neurol. 2010;67:1464–72.
  • Silva PN, Furuya TK, Braga IL, Rasmussen LT, Labio RW, Bertolucci PH, et al. Analysis of HSPA8 and HSPA9 mRNA expression and promoter methylation in the brain and blood of Alzheimer’s disease patients. J Alzheimers Dis. 2013;38:165–70.
  • Robinson MB, Taylor AR, Gifondorwa DJ, Tytell M, Milligan CE. Exogenous Hsc70, but not thermal preconditioning, confers protection to motoneurons subjected to oxidative stress. Dev Neurobiol. 2008;68:1–17.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.