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Article: Skeletal Muscle Modulates Huntington's Disease Pathogenesis in Mice: Role of Physical Exercise.

Corrochano, Silvia / Blanco, Gonzalo / Acevedo-Arozena, Abraham

2018 Volume 12, Page(s) 1179069518809059

Abstract: Huntington's disease (HD) is a monogenic fatal neurodegenerative disorder. However, there is increasing evidence that HD is a pleiotropic systemic disorder. In particular, skeletal muscle metabolism is greatly affected in HD, which in turn can have a ... ...

Abstract	Huntington's disease (HD) is a monogenic fatal neurodegenerative disorder. However, there is increasing evidence that HD is a pleiotropic systemic disorder. In particular, skeletal muscle metabolism is greatly affected in HD, which in turn can have a major impact on whole-body metabolism and energetic balance. Throughout an unbiased mutagenesis approach in HD mice, we have found that
Language	English
Publishing date	2018-10-30
Publishing country	United States
Document type	Journal Article ; Comment
ZDB-ID	2659991-0
ISSN	1179-0695
ISSN	1179-0695
DOI	10.1177/1179069518809059
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Article ; Online: Pridopidine Promotes Synaptogenesis and Reduces Spatial Memory Deficits in the Alzheimer's Disease APP/PS1 Mouse Model.

Estévez-Silva, Héctor M / Cuesto, Germán / Romero, Ninovska / Brito-Armas, José Miguel / Acevedo-Arozena, Abraham / Acebes, Ángel / Marcellino, Daniel J

Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics

2022 Volume 19, Issue 5, Page(s) 1566–1587

Abstract: Sigma-1 receptor agonists have recently gained a great deal of interest due to their anti-amnesic, neuroprotective, and neurorestorative properties. Compounds such as PRE-084 or pridopidine (ACR16) are being studied as a potential treatment against ... ...

Abstract	Sigma-1 receptor agonists have recently gained a great deal of interest due to their anti-amnesic, neuroprotective, and neurorestorative properties. Compounds such as PRE-084 or pridopidine (ACR16) are being studied as a potential treatment against cognitive decline associated with neurodegenerative disease, also to include Alzheimer's disease. Here, we performed in vitro experiments using primary neuronal cell cultures from rats to evaluate the abilities of ACR16 and PRE-084 to induce new synapses and spines formation, analyzing the expression of the possible genes and proteins involved. We additionally examined their neuroprotective properties against neuronal death mediated by oxidative stress and excitotoxicity. Both ACR16 and PRE-084 exhibited a concentration-dependent neuroprotective effect against NMDA- and H
MeSH term(s)	Mice ; Animals ; Rats ; Alzheimer Disease/complications ; Alzheimer Disease/drug therapy ; Alzheimer Disease/genetics ; Neuroprotective Agents/pharmacology ; Neuroprotective Agents/therapeutic use ; Phosphatidylinositol 3-Kinases/pharmacology ; Phosphatidylinositol 3-Kinases/therapeutic use ; Proto-Oncogene Proteins c-akt ; Neurodegenerative Diseases ; Hydrogen Peroxide/pharmacology ; Hydrogen Peroxide/therapeutic use ; N-Methylaspartate/pharmacology ; N-Methylaspartate/therapeutic use ; Memory Disorders/metabolism ; Mice, Transgenic ; Disease Models, Animal ; Amyloid beta-Protein Precursor/genetics ; Amyloid beta-Protein Precursor/metabolism ; Amyloid beta-Peptides/metabolism ; Maze Learning
Chemical Substances	pridopidine (HD4TW8S2VK) ; Neuroprotective Agents ; Phosphatidylinositol 3-Kinases (EC 2.7.1.-) ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1) ; Hydrogen Peroxide (BBX060AN9V) ; N-Methylaspartate (6384-92-5) ; Amyloid beta-Protein Precursor ; Amyloid beta-Peptides
Language	English
Publishing date	2022-08-02
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2316693-9
ISSN	1878-7479 ; 1933-7213
ISSN (online)	1878-7479
ISSN	1933-7213
DOI	10.1007/s13311-022-01280-1
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Article ; Online: Transgenic and physiological mouse models give insights into different aspects of amyotrophic lateral sclerosis.

De Giorgio, Francesca / Maduro, Cheryl / Fisher, Elizabeth M C / Acevedo-Arozena, Abraham

Disease models & mechanisms

2019 Volume 12, Issue 1

Abstract: A wide range of genetic mouse models is available to help researchers dissect human disease mechanisms. Each type of model has its own distinctive characteristics arising from the nature of the introduced mutation, as well as from the specific changes to ...

Abstract	A wide range of genetic mouse models is available to help researchers dissect human disease mechanisms. Each type of model has its own distinctive characteristics arising from the nature of the introduced mutation, as well as from the specific changes to the gene of interest. Here, we review the current range of mouse models with mutations in genes causative for the human neurodegenerative disease amyotrophic lateral sclerosis. We focus on the two main types of available mutants: transgenic mice and those that express mutant genes at physiological levels from gene targeting or from chemical mutagenesis. We compare the phenotypes for genes in which the two classes of model exist, to illustrate what they can teach us about different aspects of the disease, noting that informative models may not necessarily mimic the full trajectory of the human condition. Transgenic models can greatly overexpress mutant or wild-type proteins, giving us insight into protein deposition mechanisms, whereas models expressing mutant genes at physiological levels may develop slowly progressing phenotypes but illustrate early-stage disease processes. Although no mouse models fully recapitulate the human condition, almost all help researchers to understand normal and abnormal biological processes, providing that the individual characteristics of each model type, and how these may affect the interpretation of the data generated from each model, are considered and appreciated.
MeSH term(s)	Amyotrophic Lateral Sclerosis/genetics ; Amyotrophic Lateral Sclerosis/physiopathology ; Animals ; Disease Models, Animal ; Gene Targeting ; Mice, Transgenic ; Mutagenesis/genetics ; Mutation/genetics
Language	English
Publishing date	2019-01-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2451104-3
ISSN	1754-8411 ; 1754-8403
ISSN (online)	1754-8411
ISSN	1754-8403
DOI	10.1242/dmm.037424
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Article ; Online: TDP-43-M323K causes abnormal brain development and progressive cognitive and motor deficits associated with mislocalised and increased levels of TDP-43.

Godoy-Corchuelo, Juan M / Ali, Zeinab / Brito Armas, Jose M / Martins-Bach, Aurea B / García-Toledo, Irene / Fernández-Beltrán, Luis C / López-Carbonero, Juan I / Bascuñana, Pablo / Spring, Shoshana / Jimenez-Coca, Irene / Muñoz de Bustillo Alfaro, Ramón A / Sánchez-Barrena, Maria J / Nair, Remya R / Nieman, Brian J / Lerch, Jason P / Miller, Karla L / Ozdinler, Hande P / Fisher, Elizabeth M C / Cunningham, Thomas J /

Acevedo-Arozena, Abraham / Corrochano, Silvia

Neurobiology of disease

2024 Volume 193, Page(s) 106437

Abstract: TDP-43 pathology is found in several neurodegenerative disorders, collectively referred to as "TDP-43 proteinopathies". Aggregates of TDP-43 are present in the brains and spinal cords of >97% of amyotrophic lateral sclerosis (ALS), and in brains of ∼50% ... ...

Abstract	TDP-43 pathology is found in several neurodegenerative disorders, collectively referred to as "TDP-43 proteinopathies". Aggregates of TDP-43 are present in the brains and spinal cords of >97% of amyotrophic lateral sclerosis (ALS), and in brains of ∼50% of frontotemporal dementia (FTD) patients. While mutations in the TDP-43 gene (TARDBP) are usually associated with ALS, many clinical reports have linked these mutations to cognitive impairments and/or FTD, but also to other neurodegenerative disorders including Parkinsonism (PD) or progressive supranuclear palsy (PSP). TDP-43 is a ubiquitously expressed, highly conserved RNA-binding protein that is involved in many cellular processes, mainly RNA metabolism. To investigate systemic pathological mechanisms in TDP-43 proteinopathies, aiming to capture the pleiotropic effects of TDP-43 mutations, we have further characterised a mouse model carrying a point mutation (M323K) within the endogenous Tardbp gene. Homozygous mutant mice developed cognitive and behavioural deficits as early as 3 months of age. This was coupled with significant brain structural abnormalities, mainly in the cortex, hippocampus, and white matter fibres, together with progressive cortical interneuron degeneration and neuroinflammation. At the motor level, progressive phenotypes appeared around 6 months of age. Thus, cognitive phenotypes appeared to be of a developmental origin with a mild associated progressive neurodegeneration, while the motor and neuromuscular phenotypes seemed neurodegenerative, underlined by a progressive loss of upper and lower motor neurons as well as distal denervation. This is accompanied by progressive elevated TDP-43 protein and mRNA levels in cortex and spinal cord of homozygous mutant mice from 3 months of age, together with increased cytoplasmic TDP-43 mislocalisation in cortex, hippocampus, hypothalamus, and spinal cord at 12 months of age. In conclusion, we find that Tardbp M323K homozygous mutant mice model many aspects of human TDP-43 proteinopathies, evidencing a dual role for TDP-43 in brain morphogenesis as well as in the maintenance of the motor system, making them an ideal in vivo model system to study the complex biology of TDP-43.
MeSH term(s)	Animals ; Child, Preschool ; Humans ; Mice ; Amyotrophic Lateral Sclerosis/metabolism ; Brain/metabolism ; Cognition ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Frontotemporal Dementia/genetics ; Frontotemporal Dementia/pathology ; TDP-43 Proteinopathies/genetics ; TDP-43 Proteinopathies/pathology
Chemical Substances	DNA-Binding Proteins ; Tardbp protein, mouse
Language	English
Publishing date	2024-02-15
Publishing country	United States
Document type	Journal Article
ZDB-ID	1211786-9
ISSN	1095-953X ; 0969-9961
ISSN (online)	1095-953X
ISSN	0969-9961
DOI	10.1016/j.nbd.2024.106437
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Zs.A 4444: Show issues

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Article ; Online: Loss of

Stewart, Michelle / Lau, Petrina / Banks, Gareth / Bains, Rasneer Sonia / Castroflorio, Enrico / Oliver, Peter L / Dixon, Christine L / Kruer, Michael C / Kullmann, Dimitri M / Acevedo-Arozena, Abraham / Wells, Sara E / Corrochano, Silvia / Nolan, Patrick M

Disease models & mechanisms

2019 Volume 12, Issue 2

Abstract: Loss-of-function mutations in a human AMPA receptor-associated protein, ferric chelate reductase 1-like (FRRS1L), are associated with a devastating neurological condition incorporating choreoathetosis, cognitive deficits and epileptic encephalopathies. ... ...

Abstract	Loss-of-function mutations in a human AMPA receptor-associated protein, ferric chelate reductase 1-like (FRRS1L), are associated with a devastating neurological condition incorporating choreoathetosis, cognitive deficits and epileptic encephalopathies. Furthermore, evidence from overexpression and
MeSH term(s)	Animals ; Animals, Newborn ; Body Size ; Brain/metabolism ; Brain/pathology ; Cognition ; Cognition Disorders/pathology ; Cytoplasm/metabolism ; Electrophysiological Phenomena ; Glycosylation ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mice, Inbred C57BL ; Motor Activity ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Nervous System/growth & development ; Nervous System/pathology ; Nervous System/physiopathology ; Receptors, AMPA/metabolism ; Sleep ; Survival Analysis ; Synapses/metabolism
Chemical Substances	Frrs1l protein, mouse ; Membrane Proteins ; Nerve Tissue Proteins ; Receptors, AMPA
Language	English
Publishing date	2019-02-22
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2451104-3
ISSN	1754-8411 ; 1754-8403
ISSN (online)	1754-8411
ISSN	1754-8403
DOI	10.1242/dmm.036806
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Article ; Online: Inhibition of the mTOR pathway: A new mechanism of β cell toxicity induced by tacrolimus.

Rodriguez-Rodriguez, Ana Elena / Donate-Correa, Javier / Rovira, Jordi / Cuesto, Germán / Luis-Ravelo, Diego / Fernandes, Miguel X / Acevedo-Arozena, Abraham / Diekmann, Fritz / Acebes, Angel / Torres, Armando / Porrini, Esteban

American journal of transplantation : official journal of the American Society of Transplantation and the American Society of Transplant Surgeons

2019 Volume 19, Issue 12, Page(s) 3240–3249

Abstract: The mechanisms of tacrolimus-induced β cell toxicity are unknown. Tacrolimus (TAC) and rapamycin (Rapa) both bind to FK506-binding protein 12 (FKBP12). Also, both molecular structures are similar. Because of this similarity, we hypothesized that TAC can ... ...

Abstract	The mechanisms of tacrolimus-induced β cell toxicity are unknown. Tacrolimus (TAC) and rapamycin (Rapa) both bind to FK506-binding protein 12 (FKBP12). Also, both molecular structures are similar. Because of this similarity, we hypothesized that TAC can also inhibit the mTOR signalling, constituting a possible mechanism of β cell toxicity. Thus, we studied the effect of TAC and Rapa over the mTOR pathway, v-maf musculoaponeurotic fibrosarcoma oncogene homolog A (MafA), and insulin secretion and content in INS-1 β cells treated with or without glucose and palmitate and in islets from lean or obese rats. TAC and Rapa inhibited the mTOR pathway as reflected by lower levels of phospho-mTOR, phospo-p70S6K, and phospo-S6. The effect of Rapa was larger than TAC. Both drugs reduced the levels of MafA, insulin secretion, and content although these effects were larger with TAC. The changes on MafA and insulin metabolism were observed in cells on glucose and palmitate, in obese animals, and were absent in cells on maintenance medium or in lean animals. In silico docking and immunoprecipitation experiments confirmed that TAC can form a stable noncovalent interaction with FKBP12-mTOR. Thus, the mTOR inhibition may be a mechanism contributing to the diabetogenic effect of TAC.
MeSH term(s)	Animals ; Apoptosis ; Diabetes Mellitus, Experimental/chemically induced ; Diabetes Mellitus, Experimental/metabolism ; Diabetes Mellitus, Experimental/pathology ; Glucose/metabolism ; Immunosuppressive Agents/toxicity ; Insulin/metabolism ; Insulin-Secreting Cells/drug effects ; Insulin-Secreting Cells/metabolism ; Insulin-Secreting Cells/pathology ; Obesity/physiopathology ; Rats ; Rats, Zucker ; Signal Transduction ; TOR Serine-Threonine Kinases/metabolism ; Tacrolimus/toxicity ; Thinness/physiopathology
Chemical Substances	Immunosuppressive Agents ; Insulin ; mTOR protein, rat (EC 2.7.1.1) ; TOR Serine-Threonine Kinases (EC 2.7.11.1) ; Glucose (IY9XDZ35W2) ; Tacrolimus (WM0HAQ4WNM)
Language	English
Publishing date	2019-07-08
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2060594-8
ISSN	1600-6143 ; 1600-6135
ISSN (online)	1600-6143
ISSN	1600-6135
DOI	10.1111/ajt.15483
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Zs.A 5542: Show issues

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Article ; Online: TDP-43 mutations increase HNRNP A1-7B through gain of splicing function.

Sivakumar, Prasanth / De Giorgio, Francesca / Ule, Agnieszka M / Neeves, Jacob / Nair, Remya R / Bentham, Matthew / Birsa, Nicol / Humphrey, Jack / Plagnol, Vincent / Acevedo-Arozena, Abraham / Cunningham, Thomas J / Fisher, Elizabeth M C / Fratta, Pietro

Brain : a journal of neurology

2018 Volume 141, Issue 12, Page(s) e83

MeSH term(s)	Alternative Splicing ; Amyotrophic Lateral Sclerosis ; DNA-Binding Proteins ; Heterogeneous Nuclear Ribonucleoprotein A1 ; Heterogeneous-Nuclear Ribonucleoprotein Group A-B ; Humans ; Mutation ; RNA Splicing
Chemical Substances	DNA-Binding Proteins ; Heterogeneous Nuclear Ribonucleoprotein A1 ; Heterogeneous-Nuclear Ribonucleoprotein Group A-B ; TARDBP protein, human
Language	English
Publishing date	2018-10-03
Publishing country	England
Document type	Letter ; Research Support, Non-U.S. Gov't ; Comment
ZDB-ID	80072-7
ISSN	1460-2156 ; 0006-8950
ISSN (online)	1460-2156
ISSN	0006-8950
DOI	10.1093/brain/awy260
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Ui II Zs.26: Show issues

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Article ; Online: Erratum: Generation and analysis of innovative genomically humanized knockin

Devoy, Anny / Price, Georgia / De Giorgio, Francesca / Bunton-Stasyshyn, Rosie / Thompson, David / Gasco, Samanta / Allan, Alasdair / Codner, Gemma F / Nair, Remya R / Tibbit, Charlotte / McLeod, Ross / Ali, Zeinab / Noda, Judith / Marrero-Gagliardi, Alessandro / Brito-Armas, José M / Williams, Chloe / Öztürk, Muhammet M / Simon, Michelle / O'Neill, Edward /

Bryce-Smith, Sam / Harrison, Jackie / Atkins, Gemma / Corrochano, Silvia / Stewart, Michelle / Gilthorpe, Jonathan D / Teboul, Lydia / Acevedo-Arozena, Abraham / Fisher, Elizabeth M C / Cunningham, Thomas J

iScience

2022 Volume 25, Issue 4, Page(s) 103999

Abstract: This corrects the article DOI: 10.1016/j.isci.2021.103463.]. ...

Abstract	[This corrects the article DOI: 10.1016/j.isci.2021.103463.].
Language	English
Publishing date	2022-03-12
Publishing country	United States
Document type	Published Erratum
ISSN	2589-0042
ISSN (online)	2589-0042
DOI	10.1016/j.isci.2022.103999
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Article ; Online: SOD1 and TDP-43 animal models of amyotrophic lateral sclerosis: recent advances in understanding disease toward the development of clinical treatments.

Joyce, Peter I / Fratta, Pietro / Fisher, Elizabeth M C / Acevedo-Arozena, Abraham

Mammalian genome : official journal of the International Mammalian Genome Society

2011 Volume 22, Issue 7-8, Page(s) 420–448

Abstract: Amyotrophic lateral sclerosis (ALS) is a fatal motor neuron disease with no cure. Breakthroughs in understanding ALS pathogenesis came with the discovery of dominant mutations in the superoxide dismutase 1 gene (SOD1) and other genes, including the gene ... ...

Abstract	Amyotrophic lateral sclerosis (ALS) is a fatal motor neuron disease with no cure. Breakthroughs in understanding ALS pathogenesis came with the discovery of dominant mutations in the superoxide dismutase 1 gene (SOD1) and other genes, including the gene encoding transactivating response element DNA binding protein-43 (TDP-43). This has led to the creation of animal models to further our understanding of the disease and identify a number of ALS-causing mechanisms, including mitochondrial dysfunction, protein misfolding and aggregation, oxidative damage, neuronal excitotoxicity, non-cell autonomous effects and neuroinflammation, axonal transport defects, neurotrophin depletion, effects from extracellular mutant SOD1, and aberrant RNA processing. Here we summarise the SOD1 and TDP-43 animal models created to date, report on recent findings supporting the potential mechanisms of ALS pathogenesis, and correlate this understanding with current developments in the clinic.
MeSH term(s)	Amyotrophic Lateral Sclerosis/genetics ; Amyotrophic Lateral Sclerosis/metabolism ; Amyotrophic Lateral Sclerosis/therapy ; Animals ; Caenorhabditis elegans ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Disease Models, Animal ; Dogs ; Drosophila ; Humans ; Mice ; Rats ; Superoxide Dismutase/genetics ; Superoxide Dismutase/metabolism ; Superoxide Dismutase-1 ; Zebrafish
Chemical Substances	DNA-Binding Proteins ; SOD1 protein, human ; Sod1 protein, mouse (EC 1.15.1.1) ; Sod1 protein, rat (EC 1.15.1.1) ; Superoxide Dismutase (EC 1.15.1.1) ; Superoxide Dismutase-1 (EC 1.15.1.1)
Language	English
Publishing date	2011-06-26
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1058547-3
ISSN	1432-1777 ; 0938-8990
ISSN (online)	1432-1777
ISSN	0938-8990
DOI	10.1007/s00335-011-9339-1
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Zs.A 3489: Show issues

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Article ; Online: Pramipexole reduces soluble mutant huntingtin and protects striatal neurons through dopamine D3 receptors in a genetic model of Huntington's disease.

Luis-Ravelo, Diego / Estévez-Silva, Héctor / Barroso-Chinea, Pedro / Afonso-Oramas, Domingo / Salas-Hernández, Josmar / Rodríguez-Núñez, Julia / Acevedo-Arozena, Abraham / Marcellino, Daniel / González-Hernández, Tomás

Experimental neurology

2017 Volume 299, Issue Pt A, Page(s) 137–147

Abstract: Huntington's disease (HD) is a neurodegenerative disorder caused by abnormal expansion of the polyglutamine tract in the huntingtin protein (HTT). The toxicity of mutant HTT (mHTT) is associated with intermediate mHTT soluble oligomers that subsequently ... ...

Abstract	Huntington's disease (HD) is a neurodegenerative disorder caused by abnormal expansion of the polyglutamine tract in the huntingtin protein (HTT). The toxicity of mutant HTT (mHTT) is associated with intermediate mHTT soluble oligomers that subsequently form intranuclear inclusions. Thus, interventions promoting the clearance of soluble mHTT are regarded as neuroprotective. Striatal neurons are particularly vulnerable in HD. Their degeneration underlies motor symptoms and striatal atrophy, the anatomical hallmark of HD. Recent studies indicate that autophagy may be activated by dopamine D
Language	English
Publishing date	2017-10-19
Publishing country	United States
Document type	Journal Article
ZDB-ID	207148-4
ISSN	1090-2430 ; 0014-4886
ISSN (online)	1090-2430
ISSN	0014-4886
DOI	10.1016/j.expneurol.2017.10.019
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