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Article: ERK MAPK signaling pathway inhibition as a potential target to prevent autophagy alterations in Spinal Muscular Atrophy motoneurons.

Sansa, Alba / Miralles, Maria P / Beltran, Maria / Celma-Nos, Ferran / Calderó, Jordi / Garcera, Ana / Soler, Rosa M

Cell death discovery

2023 Volume 9, Issue 1, Page(s) 113

Abstract: Spinal Muscular Atrophy (SMA) is a severe genetic neuromuscular disorder that occurs in childhood and is caused by misexpression of the survival motor neuron (SMN) protein. SMN reduction induces spinal cord motoneuron (MN) degeneration, which leads to ... ...

Abstract	Spinal Muscular Atrophy (SMA) is a severe genetic neuromuscular disorder that occurs in childhood and is caused by misexpression of the survival motor neuron (SMN) protein. SMN reduction induces spinal cord motoneuron (MN) degeneration, which leads to progressive muscular atrophy and weakness. The link between SMN deficiency and the molecular mechanisms altered in SMA cells remains unclear. Autophagy, deregulation of intracellular survival pathways and ERK hyperphosphorylation may contribute to SMN-reduced MNs collapse, offering a useful strategy to develop new therapies to prevent neurodegeneration in SMA. Using SMA MN in vitro models, the effect of pharmacological inhibition of PI3K/Akt and ERK MAPK pathways on SMN and autophagy markers modulation was studied by western blot analysis and RT-qPCR. Experiments involved primary cultures of mouse SMA spinal cord MNs and differentiated SMA human MNs derived from induced pluripotent stem cells (iPSCs). Inhibition of the PI3K/Akt and the ERK MAPK pathways reduced SMN protein and mRNA levels. Importantly, mTOR phosphorylation, p62, and LC3-II autophagy markers protein level were decreased after ERK MAPK pharmacological inhibition. Furthermore, the intracellular calcium chelator BAPTA prevented ERK hyperphosphorylation in SMA cells. Our results propose a link between intracellular calcium, signaling pathways, and autophagy in SMA MNs, suggesting that ERK hyperphosphorylation may contribute to autophagy deregulation in SMN-reduced MNs.
Language	English
Publishing date	2023-04-05
Publishing country	United States
Document type	Journal Article
ISSN	2058-7716
ISSN	2058-7716
DOI	10.1038/s41420-023-01409-x
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Article ; Online: Intracellular pathways involved in cell survival are deregulated in mouse and human spinal muscular atrophy motoneurons.

Sansa, Alba / de la Fuente, Sandra / Comella, Joan X / Garcera, Ana / Soler, Rosa M

Neurobiology of disease

2021 Volume 155, Page(s) 105366

Abstract: Spinal Muscular Atrophy (SMA) is a severe neuromuscular disorder caused by loss of the Survival Motor Neuron 1 gene (SMN1). Due to this depletion of the survival motor neuron (SMN) protein, the disease is characterized by the degeneration of spinal cord ... ...

Abstract	Spinal Muscular Atrophy (SMA) is a severe neuromuscular disorder caused by loss of the Survival Motor Neuron 1 gene (SMN1). Due to this depletion of the survival motor neuron (SMN) protein, the disease is characterized by the degeneration of spinal cord motoneurons (MNs), progressive muscular atrophy, and weakness. Nevertheless, the ultimate cellular and molecular mechanisms leading to cell loss in SMN-reduced MNs are only partially known. We have investigated the activation of apoptotic and neuronal survival pathways in several models of SMA cells. Even though the antiapoptotic proteins FAIM-L and XIAP were increased in SMA MNs, the apoptosis executioner cleaved-caspase-3 was also elevated in these cells, suggesting the activation of the apoptosis process. Analysis of the survival pathway PI3K/Akt showed that Akt phosphorylation was reduced in SMA MNs and pharmacological inhibition of PI3K diminished SMN and Gemin2 at transcriptional level in control MNs. In contrast, ERK phosphorylation was increased in cultured mouse and human SMA MNs. Our observations suggest that apoptosis is activated in SMA MNs and that Akt phosphorylation reduction may control cell degeneration, thereby regulating the transcription of Smn and other genes related to SMN function.
MeSH term(s)	Animals ; Apoptosis/physiology ; Cell Survival ; Humans ; Mice ; Motor Neurons/metabolism ; Motor Neurons/pathology ; Muscular Atrophy, Spinal/physiopathology ; Signal Transduction/physiology
Language	English
Publishing date	2021-04-13
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.2021.105366
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Article: Smn-Deficiency Increases the Intrinsic Excitability of Motoneurons.

Arumugam, Saravanan / Garcera, Ana / Soler, Rosa M / Tabares, Lucía

Frontiers in cellular neuroscience

2017 Volume 11, Page(s) 269

Abstract: During development, motoneurons experience significant changes in their size and in the number and strength of connections that they receive, which requires adaptive changes in their passive and active electrical properties. Even after reaching maturity, ...

Abstract	During development, motoneurons experience significant changes in their size and in the number and strength of connections that they receive, which requires adaptive changes in their passive and active electrical properties. Even after reaching maturity, motoneurons continue to adjust their intrinsic excitability and synaptic activity for proper functioning of the sensorimotor circuit in accordance with physiological demands. Likewise, if some elements of the circuit become dysfunctional, the system tries to compensate for the alterations to maintain appropriate function. In Spinal Muscular Atrophy (SMA), a severe motor disease, spinal motoneurons receive less excitation from glutamatergic sensory fibers and interneurons and are electrically hyperexcitable. Currently, the origin and relationship among these alterations are not completely established. In this study, we investigated whether Survival of Motor Neuron (SMN), the ubiquitous protein defective in SMA, regulates the excitability of motoneurons before and after the establishment of the synaptic contacts. To this end, we performed patch-clamp recordings in embryonic spinal motoneurons forming complex synaptic networks in primary cultures, and in differentiated NSC-34 motoneuron-like cells in the absence of synaptic contacts. Our results show that in both conditions, Smn-deficient cells displayed lower action potential threshold, greater action potential amplitudes, and larger density of voltage-dependent sodium currents than cells with normal Smn-levels. These results indicate that Smn participates in the regulation of the cell-autonomous excitability of motoneurons at an early stage of development. This finding may contribute to a better understanding of motoneuron excitability in SMA during the development of the disease.
Language	English
Publishing date	2017-09-05
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2452963-1
ISSN	1662-5102
ISSN	1662-5102
DOI	10.3389/fncel.2017.00269
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Article ; Online: Calpain system is altered in survival motor neuron-reduced cells from in vitro and in vivo spinal muscular atrophy models.

de la Fuente, Sandra / Sansa, Alba / Hidalgo, Iván / Vivancos, Nuria / Romero-Guevara, Ricardo / Garcera, Ana / Soler, Rosa M

Cell death & disease

2020 Volume 11, Issue 6, Page(s) 487

Abstract: Spinal muscular atrophy (SMA) is a severe neuromuscular disorder caused by loss of the survival motor neuron 1 (SMN1) gene. SMA is characterized by the degeneration of spinal cord motoneurons (MNs), progressive skeletal muscle atrophy, and weakness. The ... ...

Abstract	Spinal muscular atrophy (SMA) is a severe neuromuscular disorder caused by loss of the survival motor neuron 1 (SMN1) gene. SMA is characterized by the degeneration of spinal cord motoneurons (MNs), progressive skeletal muscle atrophy, and weakness. The cellular and molecular mechanisms causing MN loss of function are only partially known. Recent advances in SMA research postulate the role of calpain protease regulating survival motor neuron (SMN) protein and the positive effect on SMA phenotype of treatment with calpain inhibitors. We analyzed the level of calpain pathway members in mice and human cellular SMA models. Results indicate an increase of calpain activity in SMN-reduced MNs. Spinal cord analysis of SMA mice treated with calpeptin, a calpain inhibitor, showed an increase of SMN, calpain, and its endogenous inhibitor calpastatin in MNs. Finally, in vitro calpeptin treatment prevented microtubule-associated protein 1A/1B-light chain 3 (LC3) increase in MNs neurites, indicating that calpain inhibition may reduce autophagosome accumulation in neuron prolongations, but not in soma. Thus, our results show that calpain activity is increased in SMA MNs and its inhibition may have a beneficial effect on SMA phenotype through the increase of SMN in spinal cord MNs.
MeSH term(s)	Animals ; Calcium-Binding Proteins/metabolism ; Calpain/metabolism ; Carrier Proteins/metabolism ; Cell Differentiation/drug effects ; Cell Line ; Cell Survival/drug effects ; Cells, Cultured ; Dipeptides/pharmacology ; Disease Models, Animal ; Fibroblasts/drug effects ; Fibroblasts/pathology ; Humans ; Induced Pluripotent Stem Cells/drug effects ; Induced Pluripotent Stem Cells/metabolism ; Mice ; Mice, Mutant Strains ; Microfilament Proteins/metabolism ; Microtubule-Associated Proteins/metabolism ; Motor Neurons/drug effects ; Motor Neurons/enzymology ; Motor Neurons/pathology ; Muscular Atrophy, Spinal/enzymology ; Muscular Atrophy, Spinal/pathology ; Proteolysis/drug effects ; Spinal Cord/embryology ; Spinal Cord/pathology ; Survival of Motor Neuron 1 Protein/metabolism
Chemical Substances	Calcium-Binding Proteins ; Carrier Proteins ; Dipeptides ; Map1lc3b protein, mouse ; Microfilament Proteins ; Microtubule-Associated Proteins ; Survival of Motor Neuron 1 Protein ; fodrin ; calpeptin (18X9FR245W) ; calpastatin (79079-11-1) ; Calpain (EC 3.4.22.-)
Language	English
Publishing date	2020-06-25
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2541626-1
ISSN	2041-4889 ; 2041-4889
ISSN (online)	2041-4889
ISSN	2041-4889
DOI	10.1038/s41419-020-2688-5
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Article ; Online: Calpain Inhibition Increases SMN Protein in Spinal Cord Motoneurons and Ameliorates the Spinal Muscular Atrophy Phenotype in Mice.

de la Fuente, Sandra / Sansa, Alba / Periyakaruppiah, Ambika / Garcera, Ana / Soler, Rosa M

Molecular neurobiology

2018 Volume 56, Issue 6, Page(s) 4414–4427

Abstract: Spinal muscular atrophy (SMA), a leading genetic cause of infant death, is caused by the loss of survival motor neuron 1 (SMN1) gene. SMA is characterized by the degeneration and loss of spinal cord motoneurons (MNs), muscular atrophy, and weakness. SMN2 ...

Abstract	Spinal muscular atrophy (SMA), a leading genetic cause of infant death, is caused by the loss of survival motor neuron 1 (SMN1) gene. SMA is characterized by the degeneration and loss of spinal cord motoneurons (MNs), muscular atrophy, and weakness. SMN2 is the centromeric duplication of the SMN gene, whose numbers of copies determine the intracellular levels of SMN protein and define the disease onset and severity. It has been demonstrated that elevating SMN levels can be an important strategy in treating SMA and can be achieved by several mechanisms, including promotion of protein stability. SMN protein is a direct target of the calcium-dependent protease calpain and induces its proteolytic cleavage in muscle cells. In this study, we examined the involvement of calpain in SMN regulation on MNs. In vitro experiments showed that calpain activation induces SMN cleavage in CD1 and SMA mouse spinal cord MNs. Additionally, calpain 1 knockdown or inhibition increased SMN level and prevent neurite degeneration in these cells. We examined the effects of calpain inhibition on the phenotype of two severe SMA mouse models. Treatment with the calpain inhibitor, calpeptin, significantly improved the lifespan and motor function of these mice. Our observations show that calpain regulates SMN level in MNs and calpeptin administration improves SMA phenotype demonstrating the potential utility of calpain inhibitors in SMA therapy.
MeSH term(s)	Animals ; Calpain/antagonists & inhibitors ; Calpain/metabolism ; Cells, Cultured ; Dipeptides/administration & dosage ; Dipeptides/pharmacology ; Gene Knockdown Techniques ; Glycoproteins/pharmacology ; Membrane Potentials/drug effects ; Mice, Transgenic ; Motor Activity/drug effects ; Motor Neurons/drug effects ; Motor Neurons/metabolism ; Motor Neurons/pathology ; Muscular Atrophy, Spinal/complications ; Muscular Atrophy, Spinal/pathology ; Muscular Atrophy, Spinal/physiopathology ; Mutation/genetics ; Nerve Degeneration/complications ; Nerve Degeneration/pathology ; Neurites/drug effects ; Neurites/metabolism ; Phenotype ; Potassium/pharmacology ; Spinal Cord/pathology ; Survival of Motor Neuron 1 Protein/metabolism
Chemical Substances	Dipeptides ; Glycoproteins ; Survival of Motor Neuron 1 Protein ; calpain inhibitors ; calpeptin (18X9FR245W) ; Calpain (EC 3.4.22.-) ; Potassium (RWP5GA015D)
Language	English
Publishing date	2018-10-16
Publishing country	United States
Document type	Journal Article
ZDB-ID	645020-9
ISSN	1559-1182 ; 0893-7648
ISSN (online)	1559-1182
ISSN	0893-7648
DOI	10.1007/s12035-018-1379-z
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Article ; Online: Spinal Muscular Atrophy autophagy profile is tissue-dependent: differential regulation between muscle and motoneurons.

Sansa, Alba / Hidalgo, Ivan / Miralles, Maria P / de la Fuente, Sandra / Perez-Garcia, M Jose / Munell, Francina / Soler, Rosa M / Garcera, Ana

Acta neuropathologica communications

2021 Volume 9, Issue 1, Page(s) 122

Abstract: Spinal muscular atrophy (SMA) is a neuromuscular genetic disease caused by reduced survival motor neuron (SMN) protein. SMN is ubiquitous and deficient levels cause spinal cord motoneurons (MNs) degeneration and muscle atrophy. Nevertheless, the ... ...

Abstract	Spinal muscular atrophy (SMA) is a neuromuscular genetic disease caused by reduced survival motor neuron (SMN) protein. SMN is ubiquitous and deficient levels cause spinal cord motoneurons (MNs) degeneration and muscle atrophy. Nevertheless, the mechanism by which SMN reduction in muscle contributes to SMA disease is not fully understood. Therefore, studies evaluating atrophy mechanisms in SMA muscles will contribute to strengthening current knowledge of the pathology. Here we propose to evaluate autophagy in SMA muscle, a pathway altered in myotube atrophy. We analized autophagy proteins and mTOR in muscle biopsies, fibroblasts, and lymphoblast cell lines from SMA patients and in gastrocnemius muscles from a severe SMA mouse model. Human MNs differentiated from SMA and unaffected control iPSCs were also included in the analysis of the autophagy. Muscle biopsies, fibroblasts, and lymphoblast cell lines from SMA patients showed reduction of the autophagy marker LC3-II. In SMA mouse gastrocnemius, we observed lower levels of LC3-II, Beclin 1, and p62/SQSTM1 proteins at pre-symptomatic stage. mTOR phosphorylation at Ser2448 was decreased in SMA muscle cells. However, in mouse and human cultured SMA MNs mTOR phosphorylation and LC3-II levels were increased. These results suggest a differential regulation in SMA of the autophagy process in muscle cells and MNs. Opposite changes in autophagy proteins and mTOR phosphorylation between muscle cells and neurons were observed. These differences may reflect a specific response to SMN reduction, which could imply diverse tissue-dependent reactions to therapies that should be taken into account when treating SMA patients.
MeSH term(s)	Animals ; Autophagy/physiology ; Female ; Humans ; Male ; Mice ; Motor Neurons/metabolism ; Motor Neurons/pathology ; Muscle, Skeletal/metabolism ; Muscle, Skeletal/pathology ; Muscular Atrophy, Spinal/metabolism ; Muscular Atrophy, Spinal/pathology
Language	English
Publishing date	2021-07-03
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2715589-4
ISSN	2051-5960 ; 2051-5960
ISSN (online)	2051-5960
ISSN	2051-5960
DOI	10.1186/s40478-021-01223-5
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Article ; Online: NF-κB signaling pathways: role in nervous system physiology and pathology.

Mincheva-Tasheva, Stefka / Soler, Rosa M

The Neuroscientist : a review journal bringing neurobiology, neurology and psychiatry

2013 Volume 19, Issue 2, Page(s) 175–194

Abstract: Intracellular pathways related to cell survival regulate neuronal physiology during development and neurodegenerative disorders. One of the pathways that have recently emerged with an important role in these processes is nuclear factor-κB (NF-κB). The ... ...

Abstract	Intracellular pathways related to cell survival regulate neuronal physiology during development and neurodegenerative disorders. One of the pathways that have recently emerged with an important role in these processes is nuclear factor-κB (NF-κB). The activity of this pathway leads to the nuclear translocation of the NF-κB transcription factors and the regulation of anti-apoptotic gene expression. Different stimuli can activate the pathway through different intracellular cascades (canonical, non-canonical, and atypical), contributing to the translocation of specific dimers of the NF-κB transcription factors, and each of these dimers can regulate the transcription of different genes. Recent studies have shown that the activation of this pathway regulates opposite responses such as cell survival or neuronal degeneration. These apparent contradictory effects depend on conditions such as the pathway stimuli, the origin of the cells, or the cellular context. In the present review, the authors summarize these findings and discuss their significance with respect to survival or death in the nervous system.
MeSH term(s)	Animals ; Cell Survival/physiology ; Humans ; NF-kappa B/metabolism ; Nervous System/metabolism ; Neurons/metabolism ; Signal Transduction/physiology
Chemical Substances	NF-kappa B
Language	English
Publishing date	2013-04
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1233753-5
ISSN	1089-4098 ; 1073-8584
ISSN (online)	1089-4098
ISSN	1073-8584
DOI	10.1177/1073858412444007
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Article: The Y172 Monoclonal Antibody Against p-c-Jun (Ser63) Is a Marker of the Postsynaptic Compartment of C-Type Cholinergic Afferent Synapses on Motoneurons.

Gatius, Alaó / Tarabal, Olga / Cayuela, Paula / Casanovas, Anna / Piedrafita, Lídia / Salvany, Sara / Hernández, Sara / Soler, Rosa M / Esquerda, Josep E / Calderó, Jordi

Frontiers in cellular neuroscience

2020 Volume 13, Page(s) 582

Abstract: C-bouton-type cholinergic afferents exert an important function in controlling motoneuron (MN) excitability. During the immunocytochemical analysis of the role of c-Jun in MNs with a monoclonal (clone Y172) antibody against phospho (p)-c-Jun (serine [Ser] ...

Abstract	C-bouton-type cholinergic afferents exert an important function in controlling motoneuron (MN) excitability. During the immunocytochemical analysis of the role of c-Jun in MNs with a monoclonal (clone Y172) antibody against phospho (p)-c-Jun (serine [Ser]63), unexpected labeling was identified in the cell body cytoplasm. As predicted for c-Jun in adult spinal cord, very few, if any MNs exhibited nuclear immunoreactivity with the Y172 antibody; conversely, virtually all MNs displayed strong Y172 immunostaining in cytoplasmic structures scattered throughout the soma and proximal dendrites. The majority of these cytoplasmic Y172-positive profiles was closely associated with VAChT-positive C-boutons, but not with other types of nerve afferents contacting MNs. Ultrastructural analysis revealed that cytoplasmic Y172 immunostaining was selectively located at the subsurface cistern (SSC) of C-boutons and also in the inner areas of the endoplasmic reticulum (ER). We also described changes in cytoplasmic Y172 immunoreactivity in injured and degenerating MNs. Moreover, we noticed that MNs from NRG1 type III-overexpressing transgenic mice, which show abnormally expanded SSCs, exhibited an increase in the density and size of peripherally located Y172-positive profiles. A similar immunocytochemical pattern to that of the Y172 antibody in MNs was found with a polyclonal antibody against p-c-Jun (Ser63) but not with another polyclonal antibody that recognizes c-Jun phosphorylated at a different site. No differential band patterns were found by western blotting with any of the antibodies against c-Jun or p-c-Jun used in our study. In cultured MNs, Y172-positive oval profiles were distributed in the cell body and proximal dendrites. The
Language	English
Publishing date	2020-01-24
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2452963-1
ISSN	1662-5102
ISSN	1662-5102
DOI	10.3389/fncel.2019.00582
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Article ; Online: Regulation of Survival Motor Neuron Protein by the Nuclear Factor-Kappa B Pathway in Mouse Spinal Cord Motoneurons.

Arumugam, Saravanan / Mincheva-Tasheva, Stefka / Periyakaruppiah, Ambika / de la Fuente, Sandra / Soler, Rosa M / Garcera, Ana

Molecular neurobiology

2017 Volume 55, Issue 6, Page(s) 5019–5030

Abstract: Survival motor neuron (SMN) protein deficiency causes the genetic neuromuscular disorder spinal muscular atrophy (SMA), characterized by spinal cord motoneuron degeneration. Since SMN protein level is critical to disease onset and severity, analysis of ... ...

Abstract	Survival motor neuron (SMN) protein deficiency causes the genetic neuromuscular disorder spinal muscular atrophy (SMA), characterized by spinal cord motoneuron degeneration. Since SMN protein level is critical to disease onset and severity, analysis of the mechanisms involved in SMN stability is one of the central goals of SMA research. Here, we describe the role of several members of the NF-κB pathway in regulating SMN in motoneurons. NF-κB is one of the main regulators of motoneuron survival and pharmacological inhibition of NF-κB pathway activity also induces mouse survival motor neuron (Smn) protein decrease. Using a lentiviral-based shRNA approach to reduce the expression of several members of NF-κB pathway, we observed that IKK and RelA knockdown caused Smn reduction in mouse-cultured motoneurons whereas IKK or RelB knockdown did not. Moreover, isolated motoneurons obtained from the severe SMA mouse model showed reduced protein levels of several NF-κB members and RelA phosphorylation. We describe the alteration of NF-κB pathway in SMA cells. In the context of recent studies suggesting regulation of altered intracellular pathways as a future pharmacological treatment of SMA, we propose the NF-κB pathway as a candidate in this new therapeutic approach.
MeSH term(s)	Animals ; Cells, Cultured ; Disease Models, Animal ; Female ; Gene Expression Regulation/physiology ; Male ; Mice ; Mice, Transgenic ; Motor Neurons/cytology ; Motor Neurons/metabolism ; NF-kappa B/metabolism ; Phosphorylation ; Signal Transduction/physiology ; Spinal Cord/cytology ; Spinal Cord/metabolism ; Survival of Motor Neuron 1 Protein/genetics ; Survival of Motor Neuron 1 Protein/metabolism
Chemical Substances	NF-kappa B ; Survival of Motor Neuron 1 Protein
Language	English
Publishing date	2017-08-14
Publishing country	United States
Document type	Journal Article
ZDB-ID	645020-9
ISSN	1559-1182 ; 0893-7648
ISSN (online)	1559-1182
ISSN	0893-7648
DOI	10.1007/s12035-017-0710-4
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Article ; Online: Autophagy modulators regulate survival motor neuron protein stability in motoneurons.

Periyakaruppiah, Ambika / de la Fuente, Sandra / Arumugam, Saravanan / Bahí, Núria / Garcera, Ana / Soler, Rosa M

Experimental neurology

2016 Volume 283, Issue Pt A, Page(s) 287–297

Language	English
Publishing date	2016-09
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.2016.06.032
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