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[PMID]:28470530
[Au] Autor:Buttgereit A
[Ad] Endereço:Institute of Medical Biotechnology, Friedrich-Alexander-Universität Erlangen-Nürnberg, Erlangen, Germany. Andreas.Buttgereit@t-online.de.
[Ti] Título:Second Harmonic Generation Microscopy of Muscle Cell Morphology and Dynamics.
[So] Source:Methods Mol Biol;1601:229-241, 2017.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Microscopy in combination with contrast-increasing dyes allows the visualization and analysis of organs, tissues, and various cells. Because of their better resolution, the development of confocal and laser microscopes enables the investigations of cell components, which are labeled with fluorescent dyes. The imaging of living cells on subcellular level (also in vivo) needs a labeling by gene transfection of GFP or similar labeled proteins. We present a method for visualization of cell structure in skeletal and heart muscle by label-free Second Harmonic Generation (SHG) microscopy and describe analytic methods for quantitative measurements of morphology and dynamics in skeletal muscle fibers.
[Mh] Termos MeSH primário: Fibras Musculares Esqueléticas/ultraestrutura
Miócitos Cardíacos/ultraestrutura
Microscopia de Geração do Segundo Harmônico/métodos
[Mh] Termos MeSH secundário: Animais
Corantes Fluorescentes/química
Proteínas de Fluorescência Verde/química
Imagem Tridimensional
Microscopia Confocal
Fibras Musculares Esqueléticas/química
Miócitos Cardíacos/química
Miosinas/química
Fótons
Sarcômeros/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fluorescent Dyes); 147336-22-9 (Green Fluorescent Proteins); EC 3.6.4.1 (Myosins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180219
[Lr] Data última revisão:
180219
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1007/978-1-4939-6960-9_18


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[PMID]:29331378
[Au] Autor:Paone C; Rudeck S; Etard C; Strähle U; Rottbauer W; Just S
[Ad] Endereço:Molecular Cardiology, Department of Inner Medicine II, University of Ulm, Ulm, Germany.
[Ti] Título:Loss of zebrafish Smyd1a interferes with myofibrillar integrity without triggering the misfolded myosin response.
[So] Source:Biochem Biophys Res Commun;496(2):339-345, 2018 02 05.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Sarcomeric protein turnover needs to be tightly balanced to assure proper assembly and renewal of sarcomeric units within muscle tissues. The mechanisms regulating these fundamental processes are only poorly understood, but of great clinical importance since many cardiac and skeletal muscle diseases are associated with defective sarcomeric organization. The SET- and MYND domain containing protein 1b (Smyd1b) is known to play a crucial role in myofibrillogenesis by functionally interacting with the myosin chaperones Unc45b and Hsp90α1. In zebrafish, Smyd1b, Unc45b and Hsp90α1 are part of the misfolded myosin response (MMR), a regulatory transcriptional response that is activated by disturbed myosin homeostasis. Genome duplication in zebrafish led to a second smyd1 gene, termed smyd1a. Morpholino- and CRISPR/Cas9-mediated knockdown of smyd1a led to significant perturbations in sarcomere structure resulting in decreased cardiac as well as skeletal muscle function. Similar to Smyd1b, we found Smyd1a to localize to the sarcomeric M-band in skeletal and cardiac muscles. Overexpression of smyd1a efficiently compensated for the loss of Smyd1b in flatline (fla) mutant zebrafish embryos, rescued the myopathic phenotype and suppressed the MMR in Smyd1b-deficient embryos, suggesting overlapping functions of both Smyd1 paralogs. Interestingly, Smyd1a is not transcriptionally activated in Smyd1b-deficient fla mutants, demonstrating lack of genetic compensation despite the functional redundancy of both zebrafish Smyd1 paralogs.
[Mh] Termos MeSH primário: Regulação da Expressão Gênica no Desenvolvimento
Histona-Lisina N-Metiltransferase/genética
Músculo Esquelético/metabolismo
Miócitos Cardíacos/metabolismo
Miosinas/genética
Sarcômeros/metabolismo
Proteínas de Peixe-Zebra/genética
Peixe-Zebra/genética
[Mh] Termos MeSH secundário: Animais
Animais Geneticamente Modificados
Sistemas CRISPR-Cas
Embrião não Mamífero
Duplicação Gênica
Edição de Genes
Genes Reporter
Proteínas de Fluorescência Verde/genética
Proteínas de Fluorescência Verde/metabolismo
Proteínas de Choque Térmico HSP90/genética
Proteínas de Choque Térmico HSP90/metabolismo
Histona-Lisina N-Metiltransferase/antagonistas & inibidores
Histona-Lisina N-Metiltransferase/deficiência
Seres Humanos
Chaperonas Moleculares/genética
Chaperonas Moleculares/metabolismo
Morfolinos/genética
Morfolinos/metabolismo
Músculo Esquelético/patologia
Miócitos Cardíacos/patologia
Miosinas/metabolismo
Dobramento de Proteína
Isoformas de Proteínas/deficiência
Isoformas de Proteínas/genética
Sarcômeros/patologia
Peixe-Zebra/crescimento & desenvolvimento
Peixe-Zebra/metabolismo
Proteínas de Peixe-Zebra/antagonistas & inibidores
Proteínas de Peixe-Zebra/deficiência
Proteínas de Peixe-Zebra/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (HSP90 Heat-Shock Proteins); 0 (Molecular Chaperones); 0 (Morpholinos); 0 (Protein Isoforms); 0 (Unc45b protein, zebrafish); 0 (Zebrafish Proteins); 147336-22-9 (Green Fluorescent Proteins); EC 2.1.1.43 (Histone-Lysine N-Methyltransferase); EC 2.1.1.43 (SmyD1 protein, zebrafish); EC 3.6.4.1 (Myosins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180214
[Lr] Data última revisão:
180214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180115
[St] Status:MEDLINE


  3 / 16452 MEDLINE  
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[PMID]:29248727
[Au] Autor:Rula S; Suwa T; Kijima ST; Haraguchi T; Wakatsuki S; Sato N; Duan Z; Tominaga M; Uyeda TQP; Ito K
[Ad] Endereço:Department of Biology, Graduate School of Science, Chiba University, Inage-ku, Chiba 263-8522, Japan.
[Ti] Título:Measurement of enzymatic and motile activities of Arabidopsis myosins by using Arabidopsis actins.
[So] Source:Biochem Biophys Res Commun;495(3):2145-2151, 2018 01 15.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:There are two classes of myosin, XI and VIII, in higher plants. Myosin XI moves actin filaments at high speed and its enzyme activity is also very high. In contrast, myosin VIII moves actin filaments very slowly with very low enzyme activity. Because most of these enzymatic and motile activities were measured using animal skeletal muscle α-actin, but not plant actin, they would not accurately reflect the actual activities in plant cells. We thus measured enzymatic and motile activities of the motor domains of two Arabidopsis myosin XI isoforms (MYA2, XI-B), and one Arabidopsis myosin VIII isoform (ATM1), by using three Arabidopsis actin isoforms (ACT1, ACT2, and ACT7). The measured activities were different from those measured by using muscle actin. Moreover, Arabidopsis myosins showed different enzymatic and motile activities when using different Arabidopsis actin isoforms. Our results suggest that plant actin should be used for measuring enzymatic and motile activities of plant myosins and that different actin isoforms in plant cells might function as different tracks along which affinities and velocities of each myosin isoform are modulated.
[Mh] Termos MeSH primário: Actinas/química
Proteínas de Arabidopsis/química
Proteínas Motores Moleculares/química
Movimento (Física)
Miosinas/química
[Mh] Termos MeSH secundário: Actinas/ultraestrutura
Proteínas de Arabidopsis/ultraestrutura
Ativação Enzimática
Proteínas Motores Moleculares/ultraestrutura
Miosinas/ultraestrutura
Ligação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Actins); 0 (Arabidopsis Proteins); 0 (Molecular Motor Proteins); EC 3.6.4.1 (Myosins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180213
[Lr] Data última revisão:
180213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171218
[St] Status:MEDLINE


  4 / 16452 MEDLINE  
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[PMID]:28467684
[Au] Autor:Wang L; Kazmierczak K; Yuan CC; Yadav S; Kawai M; Szczesna-Cordary D
[Ad] Endereço:Departments of Anatomy and Cell Biology and Internal Medicine, University of Iowa, IA, USA.
[Ti] Título:Cardiac contractility, motor function, and cross-bridge kinetics in N47K-RLC mutant mice.
[So] Source:FEBS J;284(12):1897-1913, 2017 06.
[Is] ISSN:1742-4658
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:We have investigated the physiology and mechanical profiles of skinned papillary muscle fibers from transgenic mice expressing the N47K mutation in the myosin regulatory light chain (RLC), shown to cause hypertrophic cardiomyopathy in humans. The results were compared with wild-type (WT) mice, both expressing the human ventricular RLC. Rate constants of a cross-bridge (XB) cycle were deduced from tension transients induced by sinusoidal length changes during maximal Ca activation, and were studied as a function of MgATP, MgADP, and Pi concentrations. N47K mutant showed slower XB cycles but higher actin-activated ATPase activity compared with WT. Consequently, N47K exhibited larger tension than WT. K (ADP association constant) and K (equilibrium constant of force generation) were larger in N47K, and K (ATP association constant) was slightly larger in N47K vs. WT, demonstrating stronger nucleotide binding and force generation abilities of the mutant, but no changes in rigor acto-myosin binding were observed. Tension per XB was similar among groups, but N47K exhibited more XB distribution in the attached state. Larger values of tension and higher ATPase in N47K suggested that more cross-bridges participated in tension production in the mutant myocardium compared with WT. In vivo analysis of heart function, performed in ~ 12.5-month-old mice by echocardiography and invasive hemodynamics, demonstrated a significant decrease in dP/dt -end-diastolic volume relationship, indicating a depression of ventricular contractility in N47K mice. Our findings suggest that the N47K mutation exerts its action through direct alterations of myosin motor function that ultimately result in pathological hypertrophic remodeling in N47K hearts.
[Mh] Termos MeSH primário: Atividade Motora/fisiologia
Mutação
Contração Miocárdica/fisiologia
Cadeias Leves de Miosina/genética
Músculos Papilares/fisiopatologia
[Mh] Termos MeSH secundário: Actinas/metabolismo
Difosfato de Adenosina/metabolismo
Trifosfato de Adenosina/metabolismo
Animais
Cálcio/metabolismo
Seres Humanos
Cinética
Camundongos
Camundongos Transgênicos
Cadeias Leves de Miosina/metabolismo
Miosinas
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Actins); 0 (Myosin Light Chains); 61D2G4IYVH (Adenosine Diphosphate); 8L70Q75FXE (Adenosine Triphosphate); EC 3.6.4.1 (Myosins); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE
[do] DOI:10.1111/febs.14096


  5 / 16452 MEDLINE  
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[PMID]:29262355
[Au] Autor:Irving M
[Ad] Endereço:Randall Centre for Cell and Molecular Biophysics and BHF Centre of Research Excellence, King's College London, London, United Kingdom. Electronic address: malcolm.irving@kcl.ac.uk.
[Ti] Título:Regulation of Contraction by the Thick Filaments in Skeletal Muscle.
[So] Source:Biophys J;113(12):2579-2594, 2017 Dec 19.
[Is] ISSN:1542-0086
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Contraction of skeletal muscle cells is initiated by a well-known signaling pathway. An action potential in a motor nerve triggers an action potential in a muscle cell membrane, a transient increase of intracellular calcium concentration, binding of calcium to troponin in the actin-containing thin filaments, and a structural change in the thin filaments that allows myosin motors from the thick filaments to bind to actin and generate force. This calcium/thin filament mediated pathway provides the "START" signal for contraction, but it is argued that the functional response of the muscle cell, including the speed of its contraction and relaxation, adaptation to the external load, and the metabolic cost of contraction is largely determined by additional mechanisms. This review considers the role of the thick filaments in those mechanisms, and puts forward a paradigm for the control of contraction in skeletal muscle in which both the thick and thin filaments have a regulatory function. The OFF state of the thick filament is characterized by helical packing of most of the myosin head or motor domains on the thick filament surface in a conformation that makes them unavailable for actin binding or ATP hydrolysis, although a small fraction of the myosin heads are constitutively ON. The availability of the majority fraction of the myosin heads for contraction is controlled in part by the external load on the muscle, so that these heads only attach to actin and hydrolyze ATP when they are required. This phenomenon seems to be the major determinant of the well-known force-velocity relationship of muscle, and controls the metabolic cost of contraction. The regulatory state of the thick filament also seems to control the dynamics of both muscle activation and relaxation.
[Mh] Termos MeSH primário: Contração Muscular
Músculo Esquelético/fisiologia
[Mh] Termos MeSH secundário: Cálcio/metabolismo
Modelos Biológicos
Músculo Esquelético/citologia
Músculo Esquelético/metabolismo
Miosinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
EC 3.6.4.1 (Myosins); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180210
[Lr] Data última revisão:
180210
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171221
[St] Status:MEDLINE


  6 / 16452 MEDLINE  
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[PMID]:29211998
[Au] Autor:Rynkiewicz MJ; Prum T; Hollenberg S; Kiani FA; Fagnant PM; Marston SB; Trybus KM; Fischer S; Moore JR; Lehman W
[Ad] Endereço:Department of Physiology and Biophysics, Boston University School of Medicine, Boston, Massachusetts.
[Ti] Título:Tropomyosin Must Interact Weakly with Actin to Effectively Regulate Thin Filament Function.
[So] Source:Biophys J;113(11):2444-2451, 2017 Dec 05.
[Is] ISSN:1542-0086
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Elongated tropomyosin, associated with actin-subunits along the surface of thin filaments, makes electrostatic interactions with clusters of conserved residues, K326, K328, and R147, on actin. The association is weak, permitting low-energy cost regulatory movement of tropomyosin across the filament during muscle activation. Interestingly, acidic D292 on actin, also evolutionarily conserved, lies adjacent to the three-residue cluster of basic amino acids and thus may moderate the combined local positive charge, diminishing tropomyosin-actin interaction and facilitating regulatory-switching. Indeed, charge neutralization of D292 is connected to muscle hypotonia in individuals with D292V actin mutations and linked to congenital fiber-type disproportion. Here, the D292V mutation may predispose tropomyosin-actin positioning to a myosin-blocking state, aberrantly favoring muscle relaxation, thus mimicking the low-Ca effect of troponin even in activated muscles. To test this hypothesis, interaction energetics and in vitro function of wild-type and D292V filaments were measured. Energy landscapes based on F-actin-tropomyosin models show the mutation localizes tropomyosin in a blocked-state position on actin defined by a deeper energy minimum, consistent with augmented steric-interference of actin-myosin binding. In addition, whereas myosin-dependent motility of troponin/tropomyosin-free D292V F-actin is normal, motility is dramatically inhibited after addition of tropomyosin to the mutant actin. Thus, D292V-induced blocked-state stabilization appears to disrupt the delicately poised energy balance governing thin filament regulation. Our results validate the premise that stereospecific but necessarily weak binding of tropomyosin to F-actin is required for effective thin filament function.
[Mh] Termos MeSH primário: Citoesqueleto de Actina/metabolismo
Actinas/metabolismo
Tropomiosina/metabolismo
[Mh] Termos MeSH secundário: Actinas/química
Actinas/genética
Cálcio/metabolismo
Seres Humanos
Modelos Moleculares
Mutação
Miosinas/metabolismo
Ligação Proteica
Conformação Proteica em alfa-Hélice
Eletricidade Estática
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (Tropomyosin); EC 3.6.4.1 (Myosins); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180120
[Lr] Data última revisão:
180120
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171207
[St] Status:MEDLINE


  7 / 16452 MEDLINE  
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[PMID]:29287864
[Au] Autor:Jia Y; Li X; Yang D; Xu Y; Guo Y; Li X
[Ad] Endereço:Department of Neurosurgery, Tianjin Medical University General Hospital, Tianjin, China.
[Ti] Título:Identification of two novel pathogenic compound heterozygous MYO7A mutations in Usher syndrome by whole exome sequencing.
[So] Source:Int J Pediatr Otorhinolaryngol;104:186-190, 2018 Jan.
[Is] ISSN:1872-8464
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:The current study aims to identify the pathogenic sites in a core pedigree of Usher syndrome (USH). A core pedigree of USH was analyzed by whole exome sequencing (WES). Mutations were verified by polymerase chain reaction (PCR) amplification and Sanger sequencing. Two pathogenic variations (c.849+2T>C and c.5994G>A) in MYO7A were successfully identified and individually separated from parents. One variant (c.849+2T>C) was nonsense mutation, causing the protein terminated in advance, and the other one (c.5994G>A) located near the boundary of exon could cause aberrant splicing. This study provides a meaningful exploration for identification of clinical core genetic pedigrees.
[Mh] Termos MeSH primário: Miosinas/genética
Síndromes de Usher/genética
[Mh] Termos MeSH secundário: Adolescente
Criança
Códon sem Sentido
Feminino
Heterozigoto
Seres Humanos
Masculino
Mutação
Linhagem
Reação em Cadeia da Polimerase
Sequenciamento Completo do Exoma/métodos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Codon, Nonsense); EC 3.6.4.1 (Myosins); EC 3.6.4.1 (myosin VIIa)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171231
[St] Status:MEDLINE


  8 / 16452 MEDLINE  
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[PMID]:29287847
[Au] Autor:Kooshavar D; Razipour M; Movasat M; Keramatipour M
[Ad] Endereço:Department of Medical Genetics, School of Medicine, Tehran University of Medical Sciences, Tehran, Iran.
[Ti] Título:Targeted next generation sequencing identified a novel mutation in MYO7A causing Usher syndrome type 1 in an Iranian consanguineous pedigree.
[So] Source:Int J Pediatr Otorhinolaryngol;104:10-13, 2018 Jan.
[Is] ISSN:1872-8464
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Usher syndrome (USH) is characterized by congenital hearing loss and retinitis pigmentosa (RP) with a later onset. It is an autosomal recessive trait with clinical and genetic heterogeneity which makes the molecular diagnosis much difficult. In this study, we introduce a pedigree with two affected members with USH type 1 and represent a cost and time effective approach for genetic diagnosis of USH as a genetically heterogeneous disorder. METHODS: Target region capture in the genes of interest, followed by next generation sequencing (NGS) was used to determine the causative mutations in one of the probands. Then segregation analysis in the pedigree was conducted using PCR-Sanger sequencing. RESULTS: Targeted NGS detected a novel homozygous nonsense variant c.4513G > T (p.Glu1505Ter) in MYO7A. The variant is segregating in the pedigree with an autosomal recessive pattern. CONCLUSION: In this study, a novel stop gained variant c.4513G > T (p.Glu1505Ter) in MYO7A was found in an Iranian pedigree with two affected members with USH type 1. Bioinformatic as well as pedigree segregation analyses were in line with pathogenic nature of this variant. Targeted NGS panel was showed to be an efficient method for mutation detection in hereditary disorders with locus heterogeneity.
[Mh] Termos MeSH primário: Sequenciamento de Nucleotídeos em Larga Escala/métodos
Miosinas/genética
Síndromes de Usher/genética
[Mh] Termos MeSH secundário: Códon sem Sentido
Consanguinidade
Feminino
Homozigoto
Seres Humanos
Irã (Geográfico)
Masculino
Mutação
Linhagem
Fenótipo
Reação em Cadeia da Polimerase
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Codon, Nonsense); EC 3.6.4.1 (Myosins); EC 3.6.4.1 (myosin VIIa)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171231
[St] Status:MEDLINE


  9 / 16452 MEDLINE  
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[PMID]:29235801
[Au] Autor:Labyntseva RD; Bevza OV; Lytvyn KV; Borovyk MO; Rodik RV; Kalchenko VI; Kosterin SO
[Ti] Título:Calix[4]arene C-90 and its analogs activate ATPase of the myometrium myosin subfragment-1.
[So] Source:Ukr Biochem J;88(5):48-61, 2016 Sep-Oct.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:Numerous female reproductive abnormalities are consequences of disorders in uterus smooth muscle (myometrium) contractile function. In this work, we described activators of ATPase, which could be used for development of effective treatments for correcting this dysfunction. Myosin ATPase localized in the catalytic domain of myosin subfragment-1 transforms a chemical energy deposited in macroergic bonds of ATP into mechanical movement. It was shown that сalix[4]arene C-90 and its structural analogs functionalized at the upper rim of macrocycle with four or at least two N-phenylsulfonуltrifluoroacetamidine groups, are able to activate ATP hydrolysis catalyzed by myometrium myosin subfragment-1. It was shown with the method of computer modeling that N-phenylsulfonуltrifluoroacetamidine groups of calix[4]arene C-90 interact with responsible for binding, coordination and the hydrolysis of ATP amino acid residues of myosin subfragment-1. The results can be used for further research aimed at using calix[4]arene C-90 and its analogs as pharmacological compounds that can effectively normalize myometrium contractile hypofunction.
[Mh] Termos MeSH primário: Trifosfato de Adenosina/química
Calixarenos/química
Miométrio/química
Subfragmentos de Miosina/química
Miosinas/química
Fenóis/química
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Motivos de Aminoácidos
Animais
Sítios de Ligação
Calixarenos/síntese química
Domínio Catalítico
Ativação Enzimática
Feminino
Hidrólise
Cinética
Simulação de Acoplamento Molecular
Miométrio/enzimologia
Subfragmentos de Miosina/agonistas
Subfragmentos de Miosina/isolamento & purificação
Subfragmentos de Miosina/metabolismo
Miosinas/isolamento & purificação
Miosinas/metabolismo
Fenóis/síntese química
Ligação Proteica
Conformação Proteica em alfa-Hélice
Conformação Proteica em Folha beta
Domínios e Motivos de Interação entre Proteínas
Relação Estrutura-Atividade
Sulfonas/química
Suínos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Myosin Subfragments); 0 (Phenols); 0 (Sulfones); 0 (calix(4)arene); 130036-26-9 (Calixarenes); 8L70Q75FXE (Adenosine Triphosphate); EC 3.6.4.1 (Myosins)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171214
[St] Status:MEDLINE
[do] DOI:10.15407/ubj88.05.048


  10 / 16452 MEDLINE  
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[PMID]:29195076
[Au] Autor:Gaertner F; Ahmad Z; Rosenberger G; Fan S; Nicolai L; Busch B; Yavuz G; Luckner M; Ishikawa-Ankerhold H; Hennel R; Benechet A; Lorenz M; Chandraratne S; Schubert I; Helmer S; Striednig B; Stark K; Janko M; Böttcher RT; Verschoor A; Leon C; Gachet C; Gudermann T; Mederos Y Schnitzler M; Pincus Z; Iannacone M; Haas R; Wanner G; Lauber K; Sixt M; Massberg S
[Ad] Endereço:Medizinische Klinik und Poliklinik I, Ludwig-Maximilians-Universität, 81377 Munich, Germany; Deutsches Zentrum für Herz-Kreislaufforschung (DZHK), 13347 Berlin, Germany. Electronic address: f.gaertner@med.uni-muenchen.de.
[Ti] Título:Migrating Platelets Are Mechano-scavengers that Collect and Bundle Bacteria.
[So] Source:Cell;171(6):1368-1382.e23, 2017 Nov 30.
[Is] ISSN:1097-4172
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Blood platelets are critical for hemostasis and thrombosis and play diverse roles during immune responses. Despite these versatile tasks in mammalian biology, their skills on a cellular level are deemed limited, mainly consisting in rolling, adhesion, and aggregate formation. Here, we identify an unappreciated asset of platelets and show that adherent platelets use adhesion receptors to mechanically probe the adhesive substrate in their local microenvironment. When actomyosin-dependent traction forces overcome substrate resistance, platelets migrate and pile up the adhesive substrate together with any bound particulate material. They use this ability to act as cellular scavengers, scanning the vascular surface for potential invaders and collecting deposited bacteria. Microbe collection by migrating platelets boosts the activity of professional phagocytes, exacerbating inflammatory tissue injury in sepsis. This assigns platelets a central role in innate immune responses and identifies them as potential targets to dampen inflammatory tissue damage in clinical scenarios of severe systemic infection.
[Mh] Termos MeSH primário: Infecções Bacterianas/imunologia
Plaquetas/imunologia
[Mh] Termos MeSH secundário: Animais
Bactérias/classificação
Plaquetas/citologia
Vasos Sanguíneos/lesões
Vasos Sanguíneos/patologia
Cálcio/metabolismo
Movimento Celular
Polaridade Celular
Seres Humanos
Inflamação/imunologia
Integrinas/metabolismo
Camundongos
Miosinas/metabolismo
Neutrófilos/citologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Integrins); EC 3.6.4.1 (Myosins); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171222
[Lr] Data última revisão:
171222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171202
[St] Status:MEDLINE



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