Brain iron and metabolic abnormalities in C19orf12 mutation carriers: A 7.0 tesla MRI study in mitochondrial membrane protein-associated neurodegeneration.

7 Tesla MRI glutamate magnetic resonance spectroscopy mitochondrial membrane protein-associated neurodegeneration (MPAN) neurodegeneration with brain iron accumulation (NBIA) quantitative susceptibility mapping, iron

Journal

Movement disorders : official journal of the Movement Disorder Society
ISSN: 1531-8257
Titre abrégé: Mov Disord
Pays: United States
ID NLM: 8610688

Informations de publication

Date de publication:
01 2020
Historique:
received: 26 02 2019
revised: 20 07 2019
accepted: 24 07 2019
pubmed: 14 9 2019
medline: 18 12 2020
entrez: 14 9 2019
Statut: ppublish

Résumé

Mitochondrial membrane protein-associated neurodegeneration is an autosomal-recessive disorder caused by C19orf12 mutations and characterized by iron deposits in the basal ganglia. The aim of this study was to quantify iron concentrations in deep gray matter structures using quantitative susceptibility mapping MRI and to characterize metabolic abnormalities in the pyramidal pathway using We present data of 4 clinically affected membrane protein-associated neurodegeneration patients (mean age: 21.0 ± 2.9 years) and 9 heterozygous gene mutation carriers (mean age: 50.4 ± 9.8 years), compared to age-matched healthy controls. MRI assessments were performed on a 7.0 Tesla whole-body system, consisting of whole-brain gradient-echo scans and short echo time, single-volume MR spectroscopy in the white matter of the precentral/postcentral gyrus. Quantitative susceptibility mapping, a surrogate marker for iron concentration, was performed using a state-of-the-art multiscale dipole inversion approach with focus on the globus pallidus, thalamus, putamen, caudate nucleus, and SN. In membrane protein-associated neurodegeneration patients, magnetic susceptibilities were 2 to 3 times higher in the globus pallidus (P = 0.02) and SN (P = 0.02) compared to controls. In addition, significantly higher magnetic susceptibility was observed in the caudate nucleus (P = 0.02). Non-manifesting heterozygous mutation carriers exhibited significantly increased magnetic susceptibility (relative to controls) in the putamen (P = 0.003) and caudate nucleus (P = 0.001), which may be an endophenotypic marker of genetic heterozygosity. MR spectroscopy revealed significantly increased levels of glutamate, taurine, and the combined concentration of glutamate and glutamine in membrane protein-associated neurodegeneration, which may be a correlate of corticospinal pathway dysfunction frequently observed in membrane protein-associated neurodegeneration patients. © 2019 International Parkinson and Movement Disorder Society.

Sections du résumé

BACKGROUND
Mitochondrial membrane protein-associated neurodegeneration is an autosomal-recessive disorder caused by C19orf12 mutations and characterized by iron deposits in the basal ganglia.
OBJECTIVES
The aim of this study was to quantify iron concentrations in deep gray matter structures using quantitative susceptibility mapping MRI and to characterize metabolic abnormalities in the pyramidal pathway using
METHODS
We present data of 4 clinically affected membrane protein-associated neurodegeneration patients (mean age: 21.0 ± 2.9 years) and 9 heterozygous gene mutation carriers (mean age: 50.4 ± 9.8 years), compared to age-matched healthy controls. MRI assessments were performed on a 7.0 Tesla whole-body system, consisting of whole-brain gradient-echo scans and short echo time, single-volume MR spectroscopy in the white matter of the precentral/postcentral gyrus. Quantitative susceptibility mapping, a surrogate marker for iron concentration, was performed using a state-of-the-art multiscale dipole inversion approach with focus on the globus pallidus, thalamus, putamen, caudate nucleus, and SN.
RESULTS AND CONCLUSION
In membrane protein-associated neurodegeneration patients, magnetic susceptibilities were 2 to 3 times higher in the globus pallidus (P = 0.02) and SN (P = 0.02) compared to controls. In addition, significantly higher magnetic susceptibility was observed in the caudate nucleus (P = 0.02). Non-manifesting heterozygous mutation carriers exhibited significantly increased magnetic susceptibility (relative to controls) in the putamen (P = 0.003) and caudate nucleus (P = 0.001), which may be an endophenotypic marker of genetic heterozygosity. MR spectroscopy revealed significantly increased levels of glutamate, taurine, and the combined concentration of glutamate and glutamine in membrane protein-associated neurodegeneration, which may be a correlate of corticospinal pathway dysfunction frequently observed in membrane protein-associated neurodegeneration patients. © 2019 International Parkinson and Movement Disorder Society.

Identifiants

pubmed: 31518459
doi: 10.1002/mds.27827
doi:

Substances chimiques

C19orf12 protein, human 0
Membrane Proteins 0
Mitochondrial Proteins 0
Iron E1UOL152H7

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

142-150

Informations de copyright

© 2019 International Parkinson and Movement Disorder Society.

Références

Schneider SA, Dusek P, Hardy J, Westenberger A, Jankovic J, Bhatia KP. Genetics and pathophysiology of neurodegeneration with brain iron accumulation (NBIA). Curr Neuropharmacol 2013;11:59-79.
Hartig MB, Iuso A, Haack T, et al. Absence of an orphan mitochondrial protein, c19orf12, causes a distinct clinical subtype of neurodegeneration with brain iron accumulation. Am J Hum Genet 2011;89:543-550.
Venco P, Bonora M, Giorgi C, et al. Mutations of C19orf12, coding for a transmembrane glycine zipper containing mitochondrial protein, cause mis-localization of the protein, inability to respond to oxidative stress and increased mitochondrial Ca(2)(+). Front Genet 2015;6:185.
Hogarth P, Gregory A, Kruer MC, et al. New NBIA subtype: genetic, clinical, pathologic, and radiographic features of MPAN. Neurology 2013;80:268-275.
Gore E, Appleby BS, Cohen ML, et al. Clinical and imaging characteristics of late onset mitochondrial membrane protein-associated neurodegeneration (MPAN). Neurocase 2016;22:476-483.
Selikhova M, Fedotova E, Wiethoff S, et al. A 30-year history of MPAN case from Russia. Clin Neurol Neurosurg 2017;159:111-113.
Skowronska M, Kmiec T, Jurkiewicz E, Malczyk K, Kurkowska-Jastrzebska I, Czlonkowska A. Evolution and novel radiological changes of neurodegeneration associated with mutations in C19orf12. Parkinsonism Relat Disord 2017;39:71-76.
Kurian MA, Hayflick SJ. Pantothenate kinase-associated neurodegeneration (PKAN) and PLA2G6-associated neurodegeneration (PLAN): review of two major neurodegeneration with brain iron accumulation (NBIA) phenotypes. Int Rev Neurobiol 2013;110:49-71.
Dusek P, Skoloudik D, Roth J, Dusek P. Mitochondrial membrane protein-associated neurodegeneration: a case report and literature review. Neurocase 2018;24:161-165.
Lobel U, Schweser F, Nickel M, et al. Brain iron quantification by MRI in mitochondrial membrane protein-associated neurodegeneration under iron-chelating therapy. Ann Clin Transl Neurol 2014;1:1041-1046.
Deistung A, Schweser F, Reichenbach JR. Overview of quantitative susceptibility mapping. NMR Biomed 2017;30. doi: https://doi.org/10.1002/nbm.3569. Epub 2016 Jul 19.
Duarte JM, Lei H, Mlynarik V, Gruetter R. The neurochemical profile quantified by in vivo 1H NMR spectroscopy. NeuroImage 2012;61:342-362.
Mekle R, Mlynarik V, Gambarota G, Hergt M, Krueger G, Gruetter R. MR spectroscopy of the human brain with enhanced signal intensity at ultrashort echo times on a clinical platform at 3T and 7T. Magn Reson Med 2009;61:1279-1285.
Tkac I, Oz G, Adriany G, Ugurbil K, Gruetter R. In vivo 1H NMR spectroscopy of the human brain at high magnetic fields: metabolite quantification at 4T vs. 7T. Magn Reson Med 2009;62:868-879.
Parker DL, Payne A, Todd N, Hadley JR. Phase reconstruction from multiple coil data using a virtual reference coil. Magn Reson Med 2014;72:563-569.
Acosta-Cabronero J, Milovic C, Mattern H, Tejos C, Speck O, Callaghan MF. A robust multi-scale approach to quantitative susceptibility mapping. Neuroimage 2018;183:7-24.
Sanfilipo MP, Benedict RH, Zivadinov R, Bakshi R. Correction for intracranial volume in analysis of whole brain atrophy in multiple sclerosis: the proportion vs. residual method. Neuroimage 2004;22:1732-1743.
Mlynarik V, Gambarota G, Frenkel H, Gruetter R. Localized short-echo-time proton MR spectroscopy with full signal-intensity acquisition. Magn Reson Med 2006;56:965-970.
Tkac I, Starcuk Z, Choi IY, Gruetter R. In vivo 1H NMR spectroscopy of rat brain at 1 ms echo time. Magn Reson Med 1999;41:649-656.
Brown MA. Time-domain combination of MR spectroscopy data acquired using phased-array coils. Magn Reson Med 2004;52:1207-1213.
Provencher SW. Estimation of metabolite concentrations from localized in vivo proton NMR spectra. Magn Reson Med 1993;30:672-679.
Cudalbu C, Mlynarik V, Gruetter R. Handling macromolecule signals in the quantification of the neurochemical profile. J Alzheimers Dis 2012;31(Suppl 3):S101-S115.
Jenkinson M, Beckmann CF, Behrens TE, Woolrich MW, Smith SM. Fsl. Neuroimage 2012;62:782-790.
Kreis R. The trouble with quality filtering based on relative Cramer-Rao lower bounds. Magn Reson Med 2016;75:15-18.
Delgado RF, Sanchez PR, Speckter H, et al. Missense PANK2 mutation without “eye of the tiger” sign: MR findings in a large group of patients with pantothenate kinase-associated neurodegeneration (PKAN). J Magn Reson Imaging 2012;35:788-794.
Dusek P, Tovar Martinez EM, Madai VI, et al. 7-Tesla magnetic resonance imaging for brain iron quantification in homozygous and heterozygous PANK2 mutation carriers. Mov Disord Clin Pract 2014;1:329-335.
Yoganathan S, Sudhakar SV, Thomas M, Dutta AK, Danda S. “Eye of tiger sign” mimic in an adolescent boy with mitochondrial membrane protein associated neurodegeneration (MPAN). Brain Dev 2016;38:516-519.
Skowronska M, Kmiec T, Kurkowska-Jastrzebska I, Czlonkowska A. Eye of the tiger sign in a 23 year patient with mitochondrial membrane protein associated neurodegeneration. J Neurol Sci 2015;352:110-111.
Govindaraju V, Young K, Maudsley AA. Proton NMR chemical shifts and coupling constants for brain metabolites. NMR Biomed 2000;13:129-153.
Westergaard N, Sonnewald U, Schousboe A. Metabolic trafficking between neurons and astrocytes: the glutamate/glutamine cycle revisited. Dev Neurosci 1995;17:203-211.
Kukley M, Capetillo-Zarate E, Dietrich D. Vesicular glutamate release from axons in white matter. Nat Neurosci 2007;10:311-320.
Doyle S, Hansen DB, Vella J, et al. Vesicular glutamate release from central axons contributes to myelin damage. Nat Commun 2018;9:1032.
Ramadan S, Lin A, Stanwell P. Glutamate and glutamine: a review of in vivo MRS in the human brain. NMR Biomed 2013;26:1630-1646.
Zielman R, Wijnen JP, Webb A, et al. Cortical glutamate in migraine. Brain 2017;140:1859-1871.
Hajek M, Adamovicova M, Herynek V, et al. MR relaxometry and 1H MR spectroscopy for the determination of iron and metabolite concentrations in PKAN patients. Eur Radiol 2005;15:1060-1068.
Binkofski F, Reetz K, Gaser C, et al. Morphometric fingerprint of asymptomatic Parkin and PINK1 mutation carriers in the basal ganglia. Neurology 2007;69:842-850.
Schneider SA, Talelli P, Cheeran B, et al. Motor cortical physiology in patients and asymptomatic carriers of parkin gene mutations. Mov Disord 2008;23:1812-1819.
Ghadery C, Pirpamer L, Hofer E, et al. R2* mapping for brain iron: associations with cognition in normal aging. Neurobiol Aging 2015;36:925-932.
Daugherty AM, Raz N. Appraising the role of iron in brain aging and cognition: promises and limitations of MRI methods. Neuropsychol Rev 2015;25:272-287.
Daugherty AM, Raz N. Accumulation of iron in the putamen predicts its shrinkage in healthy older adults: a multi-occasion longitudinal study. Neuroimage 2016;128:11-20.
Hallgren B, Sourander P. The effect of age on the non-haemin iron in the human brain. J Neurochem 1958;3:41-51.
Pirpamer L, Hofer E, Gesierich B, et al. Determinants of iron accumulation in the normal aging brain. Neurobiol Aging 2016;43:149-155.
Deschauer M, Gaul C, Behrmann C, Prokisch H, Zierz S, Haack TB. C19orf12 mutations in neurodegeneration with brain iron accumulation mimicking juvenile amyotrophic lateral sclerosis. J Neurol 2012;259:2434-2439.
Schottmann G, Stenzel W, Lutzkendorf S, Schuelke M, Knierim E. A novel frameshift mutation of C19ORF12 causes NBIA4 with cerebellar atrophy and manifests with severe peripheral motor axonal neuropathy. Clin Genet 2014;85:290-292.

Auteurs

Petr Dusek (P)

Department of Neurology and Centre of Clinical Neuroscience, Charles University, 1st Faculty of Medicine and General University Hospital in Prague, Prague, Czechia.
Department of Radiology, Charles University, 1st Faculty of Medicine and General University Hospital in Prague, Prague, Czechia.

Ralf Mekle (R)

Physikalisch-Technische Bundesanstalt (PTB), Braunschweig and Berlin, Germany.
Center for Stroke Research Berlin (CSB), Charité Universitätsmedizin Berlin, Berlin, Germany.

Marta Skowronska (M)

2nd Department of Neurology, Institute of Psychiatry and Neurology, Warsaw, Poland.

Julio Acosta-Cabronero (J)

Wellcome Centre for Human Neuroimaging, UCL Institute of Neurology, University College London, London, United Kingdom.

Till Huelnhagen (T)

Berlin Ultrahigh Field Facility (B.U.F.F.), Max Delbrück Center for Molecular Medicine in the Helmholtz Association (MDC), Berlin, Germany.

Simon Daniel Robinson (SD)

High Field MR Centre, Department of Biomedical Imaging and Image-guided Therapy, Medical University of Vienna, Vienna, Austria.

Florian Schubert (F)

Physikalisch-Technische Bundesanstalt (PTB), Braunschweig and Berlin, Germany.

Marcus Deschauer (M)

Department of Neurology, Technical University Munich, Munich, Germany.

Antje Els (A)

Berlin Ultrahigh Field Facility (B.U.F.F.), Max Delbrück Center for Molecular Medicine in the Helmholtz Association (MDC), Berlin, Germany.

Bernd Ittermann (B)

Physikalisch-Technische Bundesanstalt (PTB), Braunschweig and Berlin, Germany.

Gudrun Schottmann (G)

NeuroCure Clinical Research Center and Experimental and Clinical Research Center, Max Delbrueck Center for Molecular Medicine and Charité-Universitaetsmedizin Berlin, Berlin, Germany.

Vince I Madai (VI)

Center for Stroke Research Berlin (CSB), Charité Universitätsmedizin Berlin, Berlin, Germany.
Department of Neurosurgery, Charité Universitätsmedizin Berlin, Berlin, Germany.

Friedemann Paul (F)

NeuroCure Clinical Research Center and Experimental and Clinical Research Center, Max Delbrueck Center for Molecular Medicine and Charité-Universitaetsmedizin Berlin, Berlin, Germany.

Thomas Klopstock (T)

Department of Neurology with Friedrich-Baur-Institute, Ludwig-Maximilians-University of Munich, Munich, Germany.
German Center for Neurodegenerative Diseases (DZNE), Munich, Germany.
Munich Cluster for Systems Neurology (SyNergy), Munich, Germany.

Tomasz Kmiec (T)

Department of Neurology and Epileptology, The Children's Memorial Health Institute, Warsaw, Poland.

Thoralf Niendorf (T)

Berlin Ultrahigh Field Facility (B.U.F.F.), Max Delbrück Center for Molecular Medicine in the Helmholtz Association (MDC), Berlin, Germany.

Jens Wuerfel (J)

NeuroCure Clinical Research Center and Experimental and Clinical Research Center, Max Delbrueck Center for Molecular Medicine and Charité-Universitaetsmedizin Berlin, Berlin, Germany.
Medical Image Analysis Center and Department Biomedical Engineering, University Basel, Basel, Switzerland.

Susanne A Schneider (SA)

Neurology Department, Ludwig Maximilians-University of Munich, Germany.

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