Database : MEDLINE
Search on : muscular and diseases [Words]
References found : 74682 [refine]
Displaying: 1 .. 10   in format [Detailed]

page 1 of 7469 go to page                         

  1 / 74682 MEDLINE  
              next record last record
select
to print
Photocopy
Full text

[PMID]: 29524628
[Au] Autor:Gabriel Enge T; Ecroyd H; Jolley DF; Yerbury JJ; Kalmar B; Dosseto A
[Ad] Address:Wollongong Isotope Geochronology Laboratory and School of Earth and Environmental Sciences, University of Wollongong, Australia. Electronic address: tge571@uowmail.edu.au.
[Ti] Title:Assessment of metal concentrations in the SOD1 mouse model of amyotrophic lateral sclerosis and its potential role in muscular denervation, with particular focus on muscle tissue.
[So] Source:Mol Cell Neurosci;, 2018 Mar 07.
[Is] ISSN:1095-9327
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:BACKGROUND: Amyotrophic lateral sclerosis (ALS) is among the most common of the motor neuron diseases, and arguably the most devastating. During the course of this fatal neurodegenerative disorder, motor neurons undergo progressive degeneration. The currently best-understood animal models of ALS are based on the over-expression of mutant isoforms of Cu/Zn superoxide dismutase 1 (SOD1); these indicate that there is a perturbation in metal homeostasis with disease progression. Copper metabolism in particular is affected in the central nervous system (CNS) and muscle tissue. METHODS: This present study assessed previously published and newly gathered concentrations of transition metals (Cu, Zn, Fe and Se) in CNS (brain and spinal cord) and non-CNS (liver, intestine, heart and muscle) tissues from transgenic mice over-expressing the G93A mutant SOD1 isoform (SOD1 ), transgenic mice over-expressing wildtype SOD1 (SOD1 ) and non-transgenic controls. RESULTS: Cu accumulates in non-CNS tissues at pre-symptomatic stages in SOD1 tissues. This accumulation represents a potentially pathological feature that cannot solely be explained by the over-expression of mSOD1. As a result of the lack of Cu uptake into the CNS there may be a deficiency of Cu for the over-expressed mutant SOD1 in these tissues. Elevated Cu concentrations in muscle tissue also preceded the onset of symptoms and were found to be pathological and not be the result of SOD1 over-expression. CONCLUSIONS: It is hypothesized that the observed Cu accumulations may represent a pathologic feature of ALS, which may actively contribute to axonal retraction leading to muscular denervation, and possibly significantly contributing to disease pathology. Therefore, it is proposed that the toxic-gain-of-function and dying-back hypotheses to explain the molecular drivers of ALS may not be separate, individual processes; rather our data suggests that they are parallel processes.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180310
[Lr] Last revision date:180310
[St] Status:Publisher

  2 / 74682 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 29462608
[Au] Autor:Khalil B; Morderer D; Price PL; Liu F; Rossoll W
[Ad] Address:Department of Neuroscience, Mayo Clinic, Jacksonville, FL 32224 USA.
[Ti] Title:mRNP assembly, axonal transport, and local translation in neurodegenerative diseases.
[So] Source:Brain Res;, 2018 Feb 17.
[Is] ISSN:1872-6240
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:The development, maturation, and maintenance of the mammalian nervous system rely on complex spatiotemporal patterns of gene expression. In neurons, this is achieved by the expression of differentially localized isoforms and specific sets of mRNA-binding proteins (mRBPs) that regulate RNA processing, mRNA trafficking, and local protein synthesis at remote sites within dendrites and axons. There is growing evidence that axons contain a specialized transcriptome and are endowed with the machinery that allows them to rapidly alter their local proteome via local translation and protein degradation. This enables axons to quickly respond to changes in their environment during development, and to facilitate axon regeneration and maintenance in adult organisms. Aside from providing autonomy to neuronal processes, local translation allows axons to send retrograde injury signals to the cell soma. In this review, we discuss evidence that disturbances in mRNP transport, granule assembly, axonal localization, and local translation contribute to pathology in various neurodegenerative diseases, including spinal muscular atrophy (SMA), amyotrophic lateral sclerosis (ALS), frontotemporal dementia (FTD), and Alzheimer's disease (AD).
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180311
[Lr] Last revision date:180311
[St] Status:Publisher

  3 / 74682 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 29031613
[Au] Autor:Majd H; King MS; Smith AC; Kunji ERS
[Ad] Address:Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Wellcome Trust/MRC Building, Cambridge Biomedical Campus, Hills Road, Cambridge CB2 0XY, UK.
[Ti] Title:Pathogenic mutations of the human mitochondrial citrate carrier SLC25A1 lead to impaired citrate export required for lipid, dolichol, ubiquinone and sterol synthesis.
[So] Source:Biochim Biophys Acta;1859(1):1-7, 2018 01.
[Is] ISSN:0006-3002
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:Missense mutations of the human mitochondrial citrate carrier, encoded by the SLC25A1 gene, lead to an autosomal recessive neurometabolic disorder characterised by neonatal-onset encephalopathy with severe muscular weakness, intractable seizures, respiratory distress, and lack of psychomotor development, often resulting in early death. Here, we have measured the effect of all twelve known pathogenic mutations on the transport activity. The results show that nine mutations abolish transport of citrate completely, whereas the other three reduce the transport rate by >70%, indicating that impaired citrate transport is the most likely primary cause of the disease. Some mutations may be detrimental to the structure of the carrier, whereas others may impair key functional elements, such as the substrate binding site and the salt bridge network on the matrix side of the carrier. To understand the consequences of impaired citrate transport on metabolism, the substrate specificity was also determined, showing that the human citrate carrier predominantly transports citrate, isocitrate, cis-aconitate, phosphoenolpyruvate and malate. Although D-2- and L-2 hydroxyglutaric aciduria is a metabolic hallmark of the disease, it is unlikely that the citrate carrier plays a significant role in the removal of hydroxyglutarate from the cytosol for oxidation to oxoglutarate in the mitochondrial matrix. In contrast, computer simulations of central metabolism predict that the export of citrate from the mitochondrion cannot be fully compensated by other pathways, restricting the cytosolic production of acetyl-CoA that is required for the synthesis of lipids, sterols, dolichols and ubiquinone, which in turn explains the severe disease phenotypes.
[Mh] MeSH terms primary: Anion Transport Proteins
Citric Acid/metabolism
Computer Simulation
Dolichol
Mitochondrial Proteins
Models, Biological
Mutation, Missense
Sterols
Ubiquinone
[Mh] MeSH terms secundary: Anion Transport Proteins/chemistry
Anion Transport Proteins/genetics
Anion Transport Proteins/metabolism
Biological Transport, Active/genetics
Brain Diseases, Metabolic, Inborn/enzymology
Brain Diseases, Metabolic, Inborn/genetics
Catalytic Domain
Dolichol/biosynthesis
Dolichol/chemistry
Dolichol/genetics
Humans
Mitochondrial Proteins/chemistry
Mitochondrial Proteins/genetics
Mitochondrial Proteins/metabolism
Sterols/biosynthesis
Sterols/chemistry
Sterols/metabolism
Ubiquinone/biosynthesis
Ubiquinone/chemistry
Ubiquinone/genetics
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Name of substance:0 (Anion Transport Proteins); 0 (Mitochondrial Proteins); 0 (Slc25a1 protein, human); 0 (Sterols); 1339-63-5 (Ubiquinone); 2067-66-5 (Dolichol); 2968PHW8QP (Citric Acid)
[Em] Entry month:1803
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[Js] Journal subset:IM
[Da] Date of entry for processing:171017
[St] Status:MEDLINE

  4 / 74682 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 28448298
[Au] Autor:Katz JA; Murphy GS
[Ad] Address:Northshore University Health System, University of Chicago, Pritzker School of Medicine, Illinois, USA.
[Ti] Title:Anesthetic consideration for neuromuscular diseases.
[So] Source:Curr Opin Anaesthesiol;30(3):435-440, 2017 Jun.
[Is] ISSN:1473-6500
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:PURPOSE OF REVIEW: The aim of this review is to examine data relating to perioperative management of the patient with neuromuscular disorders RECENT FINDINGS: Patients with pre-existing neuromuscular disorders are at risk for a number of postoperative complications that are related to anesthetic drugs that are administered intraoperatively. Careful preoperative assessment is necessary to reduce morbidity and mortality. In particular, the risk of postoperative respiratory failure and need for long-term ventilation should be reviewed with patients. The use of succinylcholine should be avoided in muscular dystrophies, motor neuron diseases, and intrinsic muscle disease due to a risk of malignant hyperthermia, hyperkalemia, rhabdomyolysis, and cardiac arrest. The use of quantitative neuromuscular monitoring should be strongly considered whenever nondepolarizing neuromuscular blocking agents are administered. A number of case series and reports have been recently published demonstrating that sugammadex can be safely used in patients with neuromuscular disease; the risk of residual neuromuscular is nearly eliminated when this agent is administered intraoperatively. SUMMARY: Careful assessment and management of patients with underlying neuromuscular diseases is required to reduce postoperative complications. This article reviews the anesthetic implications of patients undergoing surgery with neuromuscular disorder.
[Mh] MeSH terms primary: Anesthesia/adverse effects
Anesthetics/adverse effects
Neuromuscular Blocking Agents/adverse effects
Neuromuscular Diseases/complications
Perioperative Care/methods
Postoperative Complications/etiology
Surgical Procedures, Operative/adverse effects
[Mh] MeSH terms secundary: Anesthesia/methods
Anesthetics/administration & dosage
Heart Arrest/chemically induced
Heart Arrest/prevention & control
Humans
Hyperkalemia/chemically induced
Intraoperative Complications/chemically induced
Intraoperative Complications/prevention & control
Malignant Hyperthermia/etiology
Neuromuscular Blocking Agents/administration & dosage
Neuromuscular Diseases/epidemiology
Neuromuscular Monitoring
Postoperative Complications/prevention & control
Prevalence
Respiratory Insufficiency/prevention & control
Rhabdomyolysis/chemically induced
Rhabdomyolysis/prevention & control
Risk Assessment
Succinylcholine/administration & dosage
Succinylcholine/adverse effects
gamma-Cyclodextrins/administration & dosage
gamma-Cyclodextrins/adverse effects
[Pt] Publication type:JOURNAL ARTICLE; REVIEW
[Nm] Name of substance:0 (Anesthetics); 0 (Neuromuscular Blocking Agents); 0 (gamma-Cyclodextrins); 361LPM2T56 (Sugammadex); J2R869A8YF (Succinylcholine)
[Em] Entry month:1803
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[Js] Journal subset:IM
[Da] Date of entry for processing:170428
[St] Status:MEDLINE
[do] DOI:10.1097/ACO.0000000000000466

  5 / 74682 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 29518415
[Au] Autor:Bersini S; Gilardi M; Mora M; Krol S; Arrigoni C; Candrian C; Zanotti S; Moretti M
[Ad] Address:Cell and Tissue Engineering Laboratory, IRCCS Istituto Ortopedico Galeazzi, via Galeazzi, 4, 20161, Milan, Italy.
[Ti] Title:Tackling muscle fibrosis: From molecular mechanisms to next generation engineered models to predict drug delivery.
[So] Source:Adv Drug Deliv Rev;, 2018 Mar 05.
[Is] ISSN:1872-8294
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:Muscle fibrosis represents the end stage consequence of different diseases, among which muscular dystrophies, leading to severe impairment of muscle functions. Muscle fibrosis involves the production of several growth factors, cytokines and proteolytic enzymes and is strictly associated to inflammatory processes. Moreover, fibrosis causes profound changes in tissue properties, including increased stiffness and density, lower pH and oxygenation. Up to now, there is no therapeutic approach able to counteract the fibrotic process and treatments directed against muscle pathologies are severely impaired by the harsh conditions of the fibrotic environment. The design of new therapeutics thus need innovative tools mimicking the obstacles posed by the fibrotic environment to their delivery. This review will critically discuss the role of in vivo and 3D in vitro models in this context and the characteristics that an ideal model should possess to help the translation from bench to bedside of new candidate anti-fibrotic agents.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180308
[Lr] Last revision date:180308
[St] Status:Publisher

  6 / 74682 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 29480216
[Au] Autor:Mohassel P; Mammen AL
[Ad] Address:National Institutes of Health, NINDS, Bethesda, MD, USA.
[Ti] Title:Anti-HMGCR Myopathy.
[So] Source:J Neuromuscul Dis;5(1):11-20, 2018.
[Is] ISSN:2214-3599
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:Anti-HMGCR myopathy was first recognized and characterized in patients with a history of statin exposure and immune-mediated necrotizing myopathy. After the discovery of anti-HMGCR autoantibodies, several international groups identified and characterized more patients, expanding the phenotypic spectrum of this disease to include pediatric patients and young adults without statin exposure and those with a chronic myopathy resembling limb-girdle muscular dystrophy. We provide a summary of clinical findings, pathologic features, muscle imaging, and immunogenetic risk factors of the disease. We also discuss the current treatment strategies and approaches to monitoring the therapeutic response. Lastly, we briefly summarize the current understanding of the pathophysiology of the disease and postulate a model for autoimmunity initiation and propagation in this disease.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[St] Status:In-Data-Review
[do] DOI:10.3233/JND-170282

  7 / 74682 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 29475025
[Au] Autor:Ito M; Ohno K
[Ad] Address:Division of Neurogenetics, Center for Neurological Diseases and Cancer, Nagoya University Graduate School of Medicine, Japan. Electronic address: ito@med.nagoya-u.ac.jp.
[Ti] Title:Protein-anchoring therapy to target extracellular matrix proteins to their physiological destinations.
[So] Source:Matrix Biol;, 2018 Feb 20.
[Is] ISSN:1569-1802
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:Endplate acetylcholinesterase (AChE) deficiency is a form of congenital myasthenic syndrome (CMS) caused by mutations in COLQ, which encodes collagen Q (ColQ). ColQ is an extracellular matrix (ECM) protein that anchors AChE to the synaptic basal lamina. Biglycan, encoded by BGN, is another ECM protein that binds to the dystrophin-associated protein complex (DAPC) on skeletal muscle, which links the actin cytoskeleton and ECM proteins to stabilize the sarcolemma during repeated muscle contractions. Upregulation of biglycan stabilizes the DPAC. Gene therapy can potentially ameliorate any disease that can be recapitulated in cultured cells. However, the difficulty of tissue-specific and developmental stage-specific regulated expression of transgenes, as well as the difficulty of introducing a transgene into all cells in a specific tissue, prevents us from successfully applying gene therapy to many human diseases. In contrast to intracellular proteins, an ECM protein is anchored to the target tissue via its specific binding affinity for protein(s) expressed on the cell surface within the target tissue. Exploiting this unique feature of ECM proteins, we developed protein-anchoring therapy in which a transgene product expressed even in remote tissues can be delivered and anchored to a target tissue using specific binding signals. We demonstrate the application of protein-anchoring therapy to two disease models. First, intravenous administration of adeno-associated virus (AAV) serotype 8-COLQ to Colq-deficient mice, resulting in specific anchoring of ectopically expressed ColQ-AChE at the NMJ, markedly improved motor functions, synaptic transmission, and the ultrastructure of the neuromuscular junction (NMJ). In the second example, Mdx mice, a model for Duchenne muscular dystrophy, were intravenously injected with AAV8-BGN. The treatment ameliorated motor deficits, mitigated muscle histopathologies, decreased plasma creatine kinase activities, and upregulated expression of utrophin and DAPC component proteins. We propose that protein-anchoring therapy could be applied to hereditary/acquired defects in ECM and secreted proteins, as well as therapeutic overexpression of such factors.
[Pt] Publication type:JOURNAL ARTICLE; REVIEW
[Em] Entry month:1802
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[St] Status:Publisher

  8 / 74682 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 29467464
[Au] Autor:Pareek G; Thomas RE; Pallanck LJ
[Ad] Address:Department of Genome Sciences, University of Washington, 3720 15th Avenue, NE, Seattle, WA, 98195, USA.
[Ti] Title:Loss of the Drosophila m-AAA mitochondrial protease paraplegin results in mitochondrial dysfunction, shortened lifespan, and neuronal and muscular degeneration.
[So] Source:Cell Death Dis;9(3):304, 2018 Feb 21.
[Is] ISSN:2041-4889
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:The progressive accumulation of dysfunctional mitochondria is implicated in aging and in common diseases of the elderly. To oppose this occurrence, organisms employ a variety of strategies, including the selective degradation of oxidatively damaged and misfolded mitochondrial proteins. Genetic studies in yeast indicate that the ATPase Associated with diverse cellular Activities (AAA ) family of mitochondrial proteases account for a substantial fraction of this protein degradation, but their metazoan counterparts have been little studied, despite the fact that mutations in the genes encoding these proteases cause a variety of human diseases. To begin to explore the biological roles of the metazoan mitochondrial AAA protease family, we have created a CRISPR/Cas9 allele of the Drosophila homolog of SPG7, which encodes an inner membrane-localized AAA protease known as paraplegin. Drosophila SPG7 mutants exhibited shortened lifespan, progressive locomotor defects, sensitivity to chemical and environmental stress, and muscular and neuronal degeneration. Ultrastructural examination of photoreceptor neurons indicated that the neurodegenerative phenotype of SPG7 mutants initiates at the synaptic terminal. A variety of mitochondrial defects accompanied the degenerative phenotypes of SPG7 mutants, including altered axonal transport of mitochondria, accumulation of electron-dense material in the matrix of flight muscle mitochondria, reduced activities of respiratory chain complexes I and II, and severely swollen and dysmorphic mitochondria in the synaptic terminals of photoreceptors. Drosophila SPG7 mutants recapitulate key features of human diseases caused by mutations in SPG7, and thus provide a foundation for the identification of Drosophila paraplegin substrates and strategies that could be used to ameliorate the symptoms of these diseases.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[St] Status:In-Data-Review
[do] DOI:10.1038/s41419-018-0365-8

  9 / 74682 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 29421943
[Au] Autor:Um J; Lee JH; Jung DW; Williams DR
[Ad] Address:a New Drug Targets Laboratory, School of Life Sciences, Gwangju Institute of Science and Technology , Buk-Gu , Gwangju , Republic of Korea.
[Ti] Title:Re-education begins at home: an overview of the discovery of in vivo-active small molecule modulators of endogenous stem cells.
[So] Source:Expert Opin Drug Discov;13(4):307-326, 2018 Apr.
[Is] ISSN:1746-045X
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:INTRODUCTION: Degenerative diseases, such as Alzheimer's disease, heart disease and arthritis cause great suffering and are major socioeconomic burdens. An attractive treatment approach is stem cell transplantation to regenerate damaged or destroyed tissues. However, this can be problematic. For example, donor cells may not functionally integrate into the host tissue. An alternative methodology is to deliver bioactive agents, such as small molecules, directly into the diseased tissue to enhance the regenerative potential of endogenous stem cells. Areas covered: In this review, the authors discuss the necessity of developing these small molecules to treat degenerative diseases and survey progress in their application as therapeutics. They describe both the successes and caveats of developing small molecules that target endogenous stem cells to induce tissue regeneration. This article is based on literature searches which encompass databases for biomedical research and clinical trials. These small molecules are also categorized per their target disease and mechanism of action. Expert opinion: The development of small molecules targeting endogenous stem cells is a high-profile research area. Some compounds have made the successful transition to the clinic. Novel approaches, such as modulating the stem cell niche or targeted delivery to disease sites, should increase the likelihood of future successes in this field.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[St] Status:In-Data-Review
[do] DOI:10.1080/17460441.2018.1437140

  10 / 74682 MEDLINE  
              first record previous record
select
to print
Photocopy
Full text

[PMID]: 29278895
[Au] Autor:Yoon S; Beermann ML; Yu B; Shao D; Bachschmid M; Miller JB
[Ad] Address:Department of Neurology, Boston University School of Medicine, Boston, MA, USA.
[Ti] Title:Aberrant Caspase Activation in Laminin-α2-Deficient Human Myogenic Cells is Mediated by p53 and Sirtuin Activity.
[So] Source:J Neuromuscul Dis;5(1):59-73, 2018.
[Is] ISSN:2214-3599
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:BACKGROUND: Mutations in the LAMA2 gene encoding laminin-α2 cause congenital muscular dystrophy Type 1A (MDC1A), a severe recessive disease with no effective treatment. Previous studies have shown that aberrant activation of caspases and cell death through a pathway regulated by BAX and KU70 is a significant contributor to pathogenesis in laminin-α2-deficiency. OBJECTIVES: To identify mechanisms of pathogenesis in MDC1A. METHODS: We used immunocytochemical and molecular studies of human myogenic cells and mouse muscles-comparing laminin-α2-deficient vs. healthy controls-to identify mechanisms that regulate pathological activation of caspase in laminin-α2-deficiency. RESULTS: In cultures of myogenic cells from MDC1A donors, p53 accumulated in a subset of nuclei and aberrant caspase activation was inhibited by the p53 inhibitor pifithrin-alpha. Also, the p53 target BBC3 (PUMA) was upregulated in both MDC1A myogenic cells and Lama2-/- mouse muscles. In addition, studies with sirtuin inhibitors and SIRT1 overexpression showed that caspase activation in MDC1A myotubes was inversely related to sirtuin deacetylase activity. Caspase activation in laminin-α2-deficiency was, however, not associated with increased phosphorylation of p38 MAPK. CONCLUSIONS: Aberrant caspase activation in MDC1A cells was mediated both by sirtuin deacetylase activity and by p53. Interventions that inhibit aberrant caspase activation by targeting sirtuin or p53 function could potentially be useful in ameliorating MDC1A.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1712
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[St] Status:In-Data-Review
[do] DOI:10.3233/JND-170262


page 1 of 7469 go to page                         
   


Refine the search
  Database : MEDLINE Advanced form   

    Search in field  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/PAHO/WHO - Latin American and Caribbean Center on Health Sciences Information