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Article: Metabolic Dysfunction in Motor Neuron Disease: Shedding Light through the Lens of Autophagy.

De Silva, Subhavi / Turner, Bradley J / Perera, Nirma D

2022 Volume 12, Issue 7

Abstract: Amyotrophic lateral sclerosis (ALS) patients show a myriad of energetic abnormalities, such as weight loss, hypermetabolism, and dyslipidaemia. Evidence suggests that these indices correlate with and ultimately affect the duration of survival. This ... ...

Abstract	Amyotrophic lateral sclerosis (ALS) patients show a myriad of energetic abnormalities, such as weight loss, hypermetabolism, and dyslipidaemia. Evidence suggests that these indices correlate with and ultimately affect the duration of survival. This review aims to discuss ALS metabolic abnormalities in the context of autophagy, the primordial system acting at the cellular level for energy production during nutrient deficiency. As the primary pathway of protein degradation in eukaryotic cells, the fundamental role of cellular autophagy is the adaptation to metabolic demands. Therefore, autophagy is tightly coupled to cellular metabolism. We review evidence that the delicate balance between autophagy and metabolism is aberrant in ALS, giving rise to intracellular and systemic pathophysiology observations. Understanding the metabolism autophagy crosstalk can lead to the identification of novel therapeutic targets for ALS.
Language	English
Publishing date	2022-06-22
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2662251-8
ISSN	2218-1989
ISSN	2218-1989
DOI	10.3390/metabo12070574
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Article ; Online: Age-related deficits in retinal autophagy following intraocular pressure elevation in autophagy reporter mouse model.

Afiat, Brianna C / Zhao, Da / Wong, Vickie H Y / Perera, Nirma D / Turner, Bradley J / Nguyen, Christine T O / Bui, Bang V

Neurobiology of aging

2023 Volume 131, Page(s) 74–87

Abstract: This study quantified age-related changes to retinal autophagy using the CAG-RFP-EGFP-LC3 autophagy reporter mice and considered how aging impacts autophagic responses to acute intraocular pressure (IOP) stress. IOP was elevated to 50 mm Hg for 30 ... ...

Abstract	This study quantified age-related changes to retinal autophagy using the CAG-RFP-EGFP-LC3 autophagy reporter mice and considered how aging impacts autophagic responses to acute intraocular pressure (IOP) stress. IOP was elevated to 50 mm Hg for 30 minutes in 3-month-old and 12-month-old CAG-RFP-EGFP-LC3 (n = 7 per age group) and Thy1-YFPh transgenic mice (n = 3 per age group). Compared with younger eyes, older eyes showed diminished basal autophagy in the outer retina, while the inner retina was unaffected. Autophagic flux (red:yellow puncta ratio) was elevated in the inner plexiform layer. Three days following IOP elevation, older eyes showed poorer functional recovery, most notably in ganglion cell responses compared to younger eyes (12 months old: -33.4 ± 5.3% vs. 3 months mice: -13.4 ± 4.5%). This paralleled a reduced capacity to upregulate autophagic puncta volume in the inner retina in older eyes, a response that was seen in younger eyes. Age-related decline in basal and stress-induced autophagy in the retina is associated with greater retinal ganglion cells' susceptibility to IOP elevation.
MeSH term(s)	Mice ; Animals ; Intraocular Pressure ; Retina ; Retinal Ganglion Cells/physiology ; Disease Models, Animal ; Mice, Transgenic ; Autophagy/genetics
Language	English
Publishing date	2023-07-17
Publishing country	United States
Document type	Journal Article
ZDB-ID	604505-4
ISSN	1558-1497 ; 0197-4580
ISSN (online)	1558-1497
ISSN	0197-4580
DOI	10.1016/j.neurobiolaging.2023.07.009
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Zs.A 1685: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: AMPK Signalling and Defective Energy Metabolism in Amyotrophic Lateral Sclerosis.

Perera, Nirma D / Turner, Bradley J

Neurochemical research

2016 Volume 41, Issue 3, Page(s) 544–553

Abstract: Amyotrophic lateral sclerosis (ALS) is caused by selective loss of upper and lower motor neurons by complex mechanisms that are incompletely understood. Motor neurons are large, highly polarised and excitable cells with unusually high energetic demands ... ...

Abstract	Amyotrophic lateral sclerosis (ALS) is caused by selective loss of upper and lower motor neurons by complex mechanisms that are incompletely understood. Motor neurons are large, highly polarised and excitable cells with unusually high energetic demands to maintain resting membrane potential and propagate action potentials. This leads to higher ATP consumption and mitochondrial metabolism in motor neurons relative to other cells. Here, we review increasing evidence that defective energy metabolism and homeostasis contributes to selective vulnerability and degeneration of motor neurons in ALS. Firstly, we provide a brief overview of major energetic pathways in the CNS, including glycolysis, oxidative phosphorylation and the AMP-activated protein kinase (AMPK) signalling pathway, while highlighting critical metabolic interactions between neurons and astrocytes. Next, we review evidence from ALS patients and transgenic mutant SOD1 mice for weight loss, hypermetabolism, hyperlipidemia and mitochondrial dysfunction in disease onset and progression. Genetic and therapeutic modifiers of energy metabolism in mutant SOD1 mice will also be summarised. We also present evidence that additional ALS-linked proteins, TDP-43 and FUS, lead to energy disruption and mitochondrial defects in motor neurons. Lastly, we review emerging evidence including our own that dysregulation of the AMPK signalling cascade in motor neurons is an early and common event in ALS pathogenesis. We suggest that an imbalance in energy metabolism should be considered an important factor in both progression and potential treatment of ALS.
MeSH term(s)	AMP-Activated Protein Kinases/metabolism ; Amyotrophic Lateral Sclerosis/genetics ; Amyotrophic Lateral Sclerosis/metabolism ; Animals ; Brain/metabolism ; Energy Metabolism ; Glycolysis ; Humans ; Lipid Metabolism ; Mitochondria/metabolism ; Motor Neurons/metabolism ; Oxidative Phosphorylation ; Signal Transduction ; Spinal Cord/metabolism
Chemical Substances	AMP-Activated Protein Kinases (EC 2.7.11.31)
Language	English
Publishing date	2016-03
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	199335-5
ISSN	1573-6903 ; 0364-3190
ISSN (online)	1573-6903
ISSN	0364-3190
DOI	10.1007/s11064-015-1665-3
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Zs.A 1368: Show issues

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Article: Mapping Motor Neuron Vulnerability in the Neuraxis of Male SOD1

McLeod, Victoria M / Chiam, Mathew D F / Perera, Nirma D / Lau, Chew L / Boon, Wah Chin / Turner, Bradley J

Frontiers in endocrinology

2022 Volume 13, Page(s) 808479

Abstract: Sex steroid hormones have been implicated as disease modifiers in the neurodegenerative disorder amyotrophic lateral sclerosis (ALS). Androgens, ... ...

Abstract	Sex steroid hormones have been implicated as disease modifiers in the neurodegenerative disorder amyotrophic lateral sclerosis (ALS). Androgens, signalling
MeSH term(s)	Amyotrophic Lateral Sclerosis/genetics ; Amyotrophic Lateral Sclerosis/metabolism ; Androgens/metabolism ; Animals ; Male ; Mice ; Mice, Transgenic ; Motor Neurons/metabolism ; Receptors, Androgen/genetics ; Receptors, Androgen/metabolism ; Superoxide Dismutase-1/genetics ; Superoxide Dismutase-1/metabolism
Chemical Substances	Androgens ; Receptors, Androgen ; Superoxide Dismutase-1 (EC 1.15.1.1)
Language	English
Publishing date	2022-02-22
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2592084-4
ISSN	1664-2392
ISSN	1664-2392
DOI	10.3389/fendo.2022.808479
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Article ; Online: Amyotrophic Lateral Sclerosis and Autophagy: Dysfunction and Therapeutic Targeting.

Amin, Azin / Perera, Nirma D / Beart, Philip M / Turner, Bradley J / Shabanpoor, Fazel

Cells

2020 Volume 9, Issue 11

Abstract: Over the past 20 years, there has been a drastically increased understanding of the genetic basis of Amyotrophic Lateral Sclerosis. Despite the identification of more than 40 different ALS-causing mutations, the accumulation of neurotoxic misfolded ... ...

Abstract	Over the past 20 years, there has been a drastically increased understanding of the genetic basis of Amyotrophic Lateral Sclerosis. Despite the identification of more than 40 different ALS-causing mutations, the accumulation of neurotoxic misfolded proteins, inclusions, and aggregates within motor neurons is the main pathological hallmark in all cases of ALS. These protein aggregates are proposed to disrupt cellular processes and ultimately result in neurodegeneration. One of the main reasons implicated in the accumulation of protein aggregates may be defective autophagy, a highly conserved intracellular "clearance" system delivering misfolded proteins, aggregates, and damaged organelles to lysosomes for degradation. Autophagy is one of the primary stress response mechanisms activated in highly sensitive and specialised neurons following insult to ensure their survival. The upregulation of autophagy through pharmacological autophagy-inducing agents has largely been shown to reduce intracellular protein aggregate levels and disease phenotypes in different in vitro and in vivo models of neurodegenerative diseases. In this review, we explore the intriguing interface between ALS and autophagy, provide a most comprehensive summary of autophagy-targeted drugs that have been examined or are being developed as potential treatments for ALS to date, and discuss potential therapeutic strategies for targeting autophagy in ALS.
MeSH term(s)	Amyotrophic Lateral Sclerosis/genetics ; Amyotrophic Lateral Sclerosis/pathology ; Amyotrophic Lateral Sclerosis/physiopathology ; Animals ; Autophagy ; Caloric Restriction ; Genetic Predisposition to Disease ; Humans ; Models, Biological ; Molecular Targeted Therapy
Language	English
Publishing date	2020-11-04
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells9112413
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Article ; Online: Stimulation of mTOR-independent autophagy and mitophagy by rilmenidine exacerbates the phenotype of transgenic TDP-43 mice.

Perera, Nirma D / Tomas, Doris / Wanniarachchillage, Nayomi / Cuic, Brittany / Luikinga, Sophia J / Rytova, Valeria / Turner, Bradley J

Neurobiology of disease

2021 Volume 154, Page(s) 105359

Abstract: Autophagy, which mediates the delivery of cytoplasmic substrates to the lysosome for degradation, is essential for maintaining proper cell homeostasis in physiology, ageing, and disease. There is increasing evidence that autophagy is defective in ... ...

Abstract	Autophagy, which mediates the delivery of cytoplasmic substrates to the lysosome for degradation, is essential for maintaining proper cell homeostasis in physiology, ageing, and disease. There is increasing evidence that autophagy is defective in neurodegenerative disorders, including motor neurons affected in amyotrophic lateral sclerosis (ALS). Restoring impaired autophagy in motor neurons may therefore represent a rational approach for ALS. Here, we demonstrate autophagy impairment in spinal cords of mice expressing mutant TDP-43
MeSH term(s)	Amyotrophic Lateral Sclerosis/chemically induced ; Amyotrophic Lateral Sclerosis/genetics ; Amyotrophic Lateral Sclerosis/metabolism ; Animals ; Antihypertensive Agents/toxicity ; Autophagy/physiology ; DNA-Binding Proteins/biosynthesis ; DNA-Binding Proteins/genetics ; Humans ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Mitophagy/physiology ; Phenotype ; Rilmenidine/toxicity ; TOR Serine-Threonine Kinases/biosynthesis ; TOR Serine-Threonine Kinases/genetics
Chemical Substances	Antihypertensive Agents ; DNA-Binding Proteins ; TDP-43 protein, mouse ; mTOR protein, mouse (EC 2.7.1.1) ; TOR Serine-Threonine Kinases (EC 2.7.11.1) ; Rilmenidine (P67IM25ID8)
Language	English
Publishing date	2021-03-30
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1211786-9
ISSN	1095-953X ; 0969-9961
ISSN (online)	1095-953X
ISSN	0969-9961
DOI	10.1016/j.nbd.2021.105359
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Article ; Online: The Amyotrophic Lateral Sclerosis M114T PFN1 Mutation Deregulates Alternative Autophagy Pathways and Mitochondrial Homeostasis.

Teyssou, Elisa / Chartier, Laura / Roussel, Delphine / Perera, Nirma D / Nemazanyy, Ivan / Langui, Dominique / Albert, Mélanie / Larmonier, Thierry / Saker, Safaa / Salachas, François / Pradat, Pierre-François / Meininger, Vincent / Ravassard, Philippe / Côté, Francine / Lobsiger, Christian S / Boillée, Séverine / Turner, Bradley J / Seilhean, Danielle / Millecamps, Stéphanie

International journal of molecular sciences

2022 Volume 23, Issue 10

Abstract: Mutations in profilin 1 (PFN1) have been identified in rare familial cases of Amyotrophic Lateral Sclerosis (ALS). PFN1 is involved in multiple pathways that could intervene in ALS pathology. However, the specific pathogenic role of PFN1 mutations in ALS ...

Abstract	Mutations in profilin 1 (PFN1) have been identified in rare familial cases of Amyotrophic Lateral Sclerosis (ALS). PFN1 is involved in multiple pathways that could intervene in ALS pathology. However, the specific pathogenic role of PFN1 mutations in ALS is still not fully understood. We hypothesized that PFN1 could play a role in regulating autophagy pathways and that PFN1 mutations could disrupt this function. We used patient cells (lymphoblasts) or tissue (post-mortem) carrying PFN1 mutations (M114T and E117G), and designed experimental models expressing wild-type or mutant PFN1 (cell lines and novel PFN1 mice established by lentiviral transgenesis) to study the effects of PFN1 mutations on autophagic pathway markers. We observed no accumulation of PFN1 in the spinal cord of one E117G mutation carrier. Moreover, in patient lymphoblasts and transfected cell lines, the M114T mutant PFN1 protein was unstable and deregulated the RAB9-mediated alternative autophagy pathway involved in the clearance of damaged mitochondria. In vivo, motor neurons expressing M114T mutant PFN1 showed mitochondrial abnormalities. Our results demonstrate that the M114T PFN1 mutation is more deleterious than the E117G variant in patient cells and experimental models and suggest a role for the RAB9-dependent autophagic pathway in ALS.
MeSH term(s)	Amyotrophic Lateral Sclerosis/metabolism ; Animals ; Autophagy/genetics ; Homeostasis ; Humans ; Mice ; Mitochondria/metabolism ; Mutation ; Profilins/genetics ; Profilins/metabolism ; rab GTP-Binding Proteins/metabolism
Chemical Substances	PFN1 protein, human ; Pfn1 protein, mouse ; Profilins ; RAB9A protein, human (EC 3.6.1.-) ; rab9 protein, mouse (EC 3.6.1.-) ; rab GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2022-05-19
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms23105694
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Article ; Online: Ferroptosis mediates selective motor neuron death in amyotrophic lateral sclerosis.

Wang, Taide / Tomas, Doris / Perera, Nirma D / Cuic, Brittany / Luikinga, Sophia / Viden, Aida / Barton, Samantha K / McLean, Catriona A / Samson, André L / Southon, Adam / Bush, Ashley I / Murphy, James M / Turner, Bradley J

Cell death and differentiation

2021 Volume 29, Issue 6, Page(s) 1187–1198

Abstract: Amyotrophic lateral sclerosis (ALS) is caused by selective degeneration of motor neurons in the brain and spinal cord; however, the primary cell death pathway(s) mediating motor neuron demise remain elusive. We recently established that necroptosis, an ... ...

Abstract	Amyotrophic lateral sclerosis (ALS) is caused by selective degeneration of motor neurons in the brain and spinal cord; however, the primary cell death pathway(s) mediating motor neuron demise remain elusive. We recently established that necroptosis, an inflammatory form of regulated cell death, was dispensable for motor neuron death in a mouse model of ALS, implicating other forms of cell death. Here, we confirm these findings in ALS patients, showing a lack of expression of key necroptotic effector proteins in spinal cords. Rather, we uncover evidence for ferroptosis, a recently discovered iron-dependent form of regulated cell death, in ALS. Depletion of glutathione peroxidase 4 (GPX4), an anti-oxidant enzyme and central repressor of ferroptosis, occurred in post-mortem spinal cords of both sporadic and familial ALS patients. GPX4 depletion was also an early and universal feature of spinal cords and brains of transgenic mutant superoxide dismutase 1 (SOD1
MeSH term(s)	Amyotrophic Lateral Sclerosis/genetics ; Amyotrophic Lateral Sclerosis/metabolism ; Animals ; Cell Death/physiology ; Disease Models, Animal ; Ferroptosis ; Humans ; Mice ; Mice, Transgenic ; Motor Neurons/metabolism ; Spinal Cord/metabolism ; Superoxide Dismutase/genetics ; Superoxide Dismutase/metabolism ; Superoxide Dismutase-1/genetics ; Superoxide Dismutase-1/metabolism
Chemical Substances	Superoxide Dismutase (EC 1.15.1.1) ; Superoxide Dismutase-1 (EC 1.15.1.1)
Language	English
Publishing date	2021-12-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1225672-9
ISSN	1476-5403 ; 1350-9047
ISSN (online)	1476-5403
ISSN	1350-9047
DOI	10.1038/s41418-021-00910-z
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Zs.A 4230: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Rilmenidine promotes MTOR-independent autophagy in the mutant SOD1 mouse model of amyotrophic lateral sclerosis without slowing disease progression.

Perera, Nirma D / Sheean, Rebecca K / Lau, Chew L / Shin, Yea Seul / Beart, Philip M / Horne, Malcolm K / Turner, Bradley J

Autophagy

2017 Volume 14, Issue 3, Page(s) 534–551

Abstract: Macroautophagy/autophagy is the main intracellular catabolic pathway in neurons that eliminates misfolded proteins, aggregates and damaged organelles associated with ageing and neurodegeneration. Autophagy is regulated by both MTOR-dependent and - ... ...

Abstract	Macroautophagy/autophagy is the main intracellular catabolic pathway in neurons that eliminates misfolded proteins, aggregates and damaged organelles associated with ageing and neurodegeneration. Autophagy is regulated by both MTOR-dependent and -independent pathways. There is increasing evidence that autophagy is compromised in neurodegenerative disorders, which may contribute to cytoplasmic sequestration of aggregation-prone and toxic proteins in neurons. Genetic or pharmacological modulation of autophagy to promote clearance of misfolded proteins may be a promising therapeutic avenue for these disorders. Here, we demonstrate robust autophagy induction in motor neuronal cells expressing SOD1 or TARDBP/TDP-43 mutants linked to amyotrophic lateral sclerosis (ALS). Treatment of these cells with rilmenidine, an anti-hypertensive agent and imidazoline-1 receptor agonist that induces autophagy, promoted autophagic clearance of mutant SOD1 and efficient mitophagy. Rilmenidine administration to mutant SOD1
MeSH term(s)	Amyotrophic Lateral Sclerosis/metabolism ; Animals ; Autophagy/drug effects ; DNA-Binding Proteins/metabolism ; Disease Models, Animal ; Humans ; Mice, Transgenic ; Motor Neurons/drug effects ; Rilmenidine/pharmacology ; Superoxide Dismutase-1/genetics ; TOR Serine-Threonine Kinases/metabolism
Chemical Substances	DNA-Binding Proteins ; SOD1 protein, human ; Sod1 protein, mouse (EC 1.15.1.1) ; Superoxide Dismutase-1 (EC 1.15.1.1) ; MTOR protein, human (EC 2.7.1.1) ; mTOR protein, mouse (EC 2.7.1.1) ; TOR Serine-Threonine Kinases (EC 2.7.11.1) ; Rilmenidine (P67IM25ID8)
Language	English
Publishing date	2017-12-17
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2454135-7
ISSN	1554-8635 ; 1554-8627
ISSN (online)	1554-8635
ISSN	1554-8627
DOI	10.1080/15548627.2017.1385674
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Article ; Online: Necroptosis is dispensable for motor neuron degeneration in a mouse model of ALS.

Wang, Taide / Perera, Nirma D / Chiam, Mathew D F / Cuic, Brittany / Wanniarachchillage, Nayomi / Tomas, Doris / Samson, André L / Cawthorne, Wayne / Valor, Eric N / Murphy, James M / Turner, Bradley J

Cell death and differentiation

2019 Volume 27, Issue 5, Page(s) 1728–1739

Abstract: Motor neuron degeneration in amyotrophic lateral sclerosis (ALS) is proposed to occur by necroptosis, an inflammatory form of regulated cell death. Prior studies implicated necroptosis in ALS based on accumulation of necroptotic markers in affected ... ...

Abstract	Motor neuron degeneration in amyotrophic lateral sclerosis (ALS) is proposed to occur by necroptosis, an inflammatory form of regulated cell death. Prior studies implicated necroptosis in ALS based on accumulation of necroptotic markers in affected tissues of patients and mouse models, and amelioration of disease in mutant superoxide dismutase 1 (SOD1
MeSH term(s)	Amyotrophic Lateral Sclerosis/pathology ; Animals ; Brain/pathology ; Disease Models, Animal ; Disease Progression ; Humans ; Mice, Inbred C57BL ; Mice, Transgenic ; Motor Neurons/metabolism ; Motor Neurons/pathology ; Necroptosis ; Nerve Degeneration/pathology ; Neuroglia/metabolism ; Neuroglia/pathology ; Protein Kinases/metabolism ; Receptor-Interacting Protein Serine-Threonine Kinases/metabolism ; Spinal Cord/pathology ; Superoxide Dismutase/metabolism ; Up-Regulation
Chemical Substances	Superoxide Dismutase (EC 1.15.1.1) ; MLKL protein, mouse (EC 2.7.-) ; Protein Kinases (EC 2.7.-) ; Receptor-Interacting Protein Serine-Threonine Kinases (EC 2.7.11.1) ; Ripk1 protein, mouse (EC 2.7.11.1)
Language	English
Publishing date	2019-11-19
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1225672-9
ISSN	1476-5403 ; 1350-9047
ISSN (online)	1476-5403
ISSN	1350-9047
DOI	10.1038/s41418-019-0457-8
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