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Pesquisa : D05.750.078.730.475.475.875 [Categoria DeCS]
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[PMID]:28714309
[Au] Autor:Zhang HM; Ji HH; Ni T; Ma RN; Wang A; Li XD
[Ad] Endereço:Group of Cell Motility and Muscle Contraction, State Key Laboratory of Integrated Management of Pest Insects and Rodents, Institute of Zoology, Chinese Academy of Sciences , Beijing, China 100101.
[Ti] Título:Characterization of Blebbistatin Inhibition of Smooth Muscle Myosin and Nonmuscle Myosin-2.
[So] Source:Biochemistry;56(32):4235-4243, 2017 Aug 15.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Blebbistatin is a potent and specific inhibitor of the motor functions of class II myosins, including striated muscle myosin and nonmuscle myosin-2 (NM2). However, the blebbistatin inhibition of NM2c has not been assessed and remains controversial with respect to its efficacy with smooth muscle myosin (SmM), which is highly homologous to NM2. To clarify these issues, we analyzed the effects of blebbistatin on the motor activities of recombinant SmM and three NM2s (NM2a, -2b, and -2c). We found that blebbistatin potently inhibits the actin-activated ATPase activities of SmM and NM2s with following IC values: 6.47 µM for SmM, 3.58 µM for NM2a, 2.30 µM for NM2b, and 1.57 µM for NM2c. To identify the blebbistatin-resistant myosin-2 mutant, we performed mutagenesis analysis of the conserved residues in the blebbistatin-binding site of SmM and NM2s. We found that the A456F mutation renders SmM and NM2s resistant to blebbistatin without greatly altering their motor activities or phosphorylation-dependent regulation, making A456F a useful mutant for investigating the cellular function of NM2s.
[Mh] Termos MeSH primário: Proteínas Aviárias/antagonistas & inibidores
Proteínas Aviárias/química
Compostos Heterocíclicos de 4 ou mais Anéis/química
Miosina não Muscular Tipo IIB/antagonistas & inibidores
Miosina não Muscular Tipo IIB/química
Miosinas de Músculo Liso/antagonistas & inibidores
Miosinas de Músculo Liso/química
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Animais
Proteínas Aviárias/genética
Proteínas Aviárias/metabolismo
Galinhas
Seres Humanos
Camundongos
Mutação de Sentido Incorreto
Miosina não Muscular Tipo IIB/genética
Miosina não Muscular Tipo IIB/metabolismo
Miosinas de Músculo Liso/genética
Miosinas de Músculo Liso/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Avian Proteins); 0 (Heterocyclic Compounds, 4 or More Rings); 20WC4J7CQ6 (blebbistatin); EC 3.6.1.- (Nonmuscle Myosin Type IIB); EC 3.6.1.- (Smooth Muscle Myosins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170718
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00311


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[PMID]:27678004
[Au] Autor:Sobieszek A
[Ad] Endereço:Institute for Biomedical Aging Research, Austrian Academy of Sciences, Dr. Ignaz Seipel-Platz 2, 1010, Wien, Austria. apolinary@sobieszek.at.
[Ti] Título:Helical model of smooth muscle myosin filament and the ribbons made of caldesmon: history revisited.
[So] Source:Eur Biophys J;45(8):861-867, 2016 Dec.
[Is] ISSN:1432-1017
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:In early studies on smooth muscle, I described a crude myosin fraction (CMF) in which self-assembly of myosin filaments was observed. For the first time, the 14-nm periodicity stemming from regular arrangement of myosin heads on the filament surface was observed (Sobieszek in J Mol Biol 70:741-744, 1972). In this fraction, we also observed formation of long ribbon-shaped aggregates exhibiting a 5.6-nm periodicity, characteristic of tropomyosin (TM) paracrystals (Sobieszek and Small in Phil Trans R Soc Lond B 265:203-212, 1973). We therefore concluded that these ribbons were made of TM and they might be related to the myosin ribbons observed in electron micrographs (EM) of intact smooth muscle (Lowy and Small in Nature 227:46-51, 1970; Small and Squire in Mol Biol 67:117-149, 1972). Subsequently, Small (J Cell Sci 24:327-349, 1977) concluded that the ribbons observed in the EM sections were an artifact, but their observation in the CMF was not addressed. I have now revisited two aspects of the above studies. Firstly, based on my new multi-angle laser-scattering data and considering the length and stability of the building unit for the filament, a myosin trimer fit better to the previously proposed helical structure. Secondly, after two decades of systematic examinations of protein compositions in multiple smooth muscle extracts and isolated filaments, I concluded that the ribbons were made of caldesmon and not TM. Thirdly, actin-activated ATPase activity measurements indicated that modulation of this activity (by CaD and TM) was synergistic, cooperative and depended on myosin to actin ratio.
[Mh] Termos MeSH primário: Proteínas de Ligação a Calmodulina/química
Proteínas de Ligação a Calmodulina/metabolismo
Modelos Moleculares
Miosinas de Músculo Liso/química
Miosinas de Músculo Liso/metabolismo
[Mh] Termos MeSH secundário: Actomiosina/metabolismo
Adenosina Trifosfatases/metabolismo
Regulação Alostérica
Músculo Liso/metabolismo
Músculo Liso/fisiologia
Estrutura Secundária de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Calmodulin-Binding Proteins); 9013-26-7 (Actomyosin); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.1.- (Smooth Muscle Myosins)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160929
[St] Status:MEDLINE


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[PMID]:27528075
[Au] Autor:Alcala DB; Haldeman BD; Brizendine RK; Krenc AK; Baker JE; Rock RS; Cremo CR
[Ad] Endereço:Department of Pharmacology, University of Nevada Reno School of Medicine, Reno, Nevada, USA.
[Ti] Título:Myosin light chain kinase steady-state kinetics: comparison of smooth muscle myosin II and nonmuscle myosin IIB as substrates.
[So] Source:Cell Biochem Funct;34(7):469-474, 2016 Oct.
[Is] ISSN:1099-0844
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Myosin light chain kinase (MLCK) phosphorylates S19 of the myosin regulatory light chain (RLC), which is required to activate myosin's ATPase activity and contraction. Smooth muscles are known to display plasticity in response to factors such as inflammation, developmental stage, or stress, which lead to differential expression of nonmuscle and smooth muscle isoforms. Here, we compare steady-state kinetics parameters for phosphorylation of different MLCK substrates: (1) nonmuscle RLC, (2) smooth muscle RLC, and heavy meromyosin subfragments of (3) nonmuscle myosin IIB, and (4) smooth muscle myosin II. We show that MLCK has a ~2-fold higher k for both smooth muscle myosin II substrates compared with nonmuscle myosin IIB substrates, whereas K values were very similar. Myosin light chain kinase has a 1.6-fold and 1.5-fold higher specificity (k /K ) for smooth versus nonmuscle-free RLC and heavy meromyosin, respectively, suggesting that differences in specificity are dictated by RLC sequences. Of the 10 non-identical RLC residues, we ruled out 7 as possible underlying causes of different MLCK kinetics. The remaining 3 residues were found to be surface exposed in the N-terminal half of the RLC, consistent with their importance in substrate recognition. These data are consistent with prior deletion/chimera studies and significantly add to understanding of MLCK myosin interactions. SIGNIFICANCE OF THE STUDY: Phosphorylation of nonmuscle and smooth muscle myosin by myosin light chain kinase (MLCK) is required for activation of myosin's ATPase activity. In smooth muscles, nonmuscle myosin coexists with smooth muscle myosin, but the two myosins have very different chemo-mechanical properties relating to their ability to maintain force. Differences in specificity of MLCK for different myosin isoforms had not been previously investigated. We show that the MLCK prefers smooth muscle myosin by a significant factor. These data suggest that nonmuscle myosin is phosphorylated more slowly than smooth muscle myosin during a contraction cycle.
[Mh] Termos MeSH primário: Quinase de Cadeia Leve de Miosina/metabolismo
Miosina não Muscular Tipo IIB/metabolismo
Miosinas de Músculo Liso/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Galinhas
Cinética
Modelos Moleculares
Subfragmentos de Miosina/química
Subfragmentos de Miosina/metabolismo
Quinase de Cadeia Leve de Miosina/química
Miosina não Muscular Tipo IIB/química
Fosforilação
Miosinas de Músculo Liso/química
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Myosin Subfragments); EC 2.7.11.18 (Myosin-Light-Chain Kinase); EC 3.6.1.- (Nonmuscle Myosin Type IIB); EC 3.6.1.- (Smooth Muscle Myosins)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170224
[Lr] Data última revisão:
170224
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160817
[St] Status:MEDLINE
[do] DOI:10.1002/cbf.3209


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[PMID]:27416931
[Au] Autor:Sawyer DM; Pace LA; Pascale CL; Kutchin AC; O'Neill BE; Starke RM; Dumont AS
[Ad] Endereço:Department of Neurosurgery, Tulane Center for Clinical Neurosciences, Tulane University School of Medicine, 131 S. Robertson St. Ste. 1300, 8047, New Orleans, LA, 70112, USA.
[Ti] Título:Lymphocytes influence intracranial aneurysm formation and rupture: role of extracellular matrix remodeling and phenotypic modulation of vascular smooth muscle cells.
[So] Source:J Neuroinflammation;13(1):185, 2016 Jul 14.
[Is] ISSN:1742-2094
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Intracranial aneurysms (IA) are increasingly recognized as a disease driven by chronic inflammation. Recent research has identified key mediators and processes underlying IA pathogenesis, but mechanistic understanding remains incomplete. Lymphocytic infiltrates have been demonstrated in patient IA tissue specimens and have also been shown to play an important role in abdominal aortic aneurysms (AAA) and related diseases such as atherosclerosis. However, no study has systematically examined the contribution of lymphocytes in a model of IA. METHODS: Lymphocyte-deficient (Rag1) and wild-type (WT; C57BL/6 strain) mice were subjected to a robust IA induction protocol. Rates of IA formation and rupture were measured, and cerebral artery tissue was collected and utilized for histology and gene expression analysis. RESULTS: At 2 weeks, the Rag1 group had significantly fewer IA formations and ruptures than the WT group. Histological analysis of unruptured IA tissue showed robust B and T lymphocyte infiltration in the WT group, while there were no differences in macrophage infiltration, IA diameter, and wall thickness. Significant differences in interleukin-6 (IL-6), matrix metalloproteinases 2 (MMP2) and 9 (MMP9), and smooth muscle myosin heavy chain (MHC) were observed between the groups. CONCLUSIONS: Lymphocytes are key contributors to IA pathogenesis and provide a novel target for the prevention of IA progression and rupture in patients.
[Mh] Termos MeSH primário: Aneurisma Roto/patologia
Regulação da Expressão Gênica/fisiologia
Aneurisma Intracraniano/patologia
Linfócitos/fisiologia
Músculo Liso Vascular/metabolismo
[Mh] Termos MeSH secundário: Animais
Antígenos CD/metabolismo
Antígenos de Diferenciação Mielomonocítica/metabolismo
Modelos Animais de Doenças
Citometria de Fluxo
Regulação da Expressão Gênica/genética
Proteínas de Homeodomínio/genética
Proteínas de Homeodomínio/metabolismo
Interleucina-6/metabolismo
Aneurisma Intracraniano/genética
Metaloproteinase 2 da Matriz/metabolismo
Metaloproteinase 9 da Matriz/metabolismo
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Miosinas de Músculo Liso/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, CD); 0 (Antigens, Differentiation, Myelomonocytic); 0 (CD68 antigen, human); 0 (Homeodomain Proteins); 0 (Interleukin-6); 128559-51-3 (RAG-1 protein); EC 3.4.24.24 (Matrix Metalloproteinase 2); EC 3.4.24.35 (Matrix Metalloproteinase 9); EC 3.6.1.- (Smooth Muscle Myosins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170929
[Lr] Data última revisão:
170929
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160716
[St] Status:MEDLINE
[do] DOI:10.1186/s12974-016-0654-z


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[PMID]:26397772
[Au] Autor:Aguiar FN; Cirqueira CS; Bacchi CE; Carvalho FM
[Ad] Endereço:Department of Pathology, Faculdade de Medicina da Universidade de São Paulo, São Paulo, Brazil.
[Ti] Título:Morphologic, molecular and microenvironment factors associated with stromal invasion in breast ductal carcinoma in situ: Role of myoepithelial cells.
[So] Source:Breast Dis;35(4):249-52, 2015.
[Is] ISSN:1558-1551
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Ductal carcinoma in situ is the last step preceding invasive ductal carcinoma in breast carcinogenesis. OBJECTIVE: We investigated the role of myoepithelial cells and epithelium characteristics as predictors of the risk of stromal invasion. METHODS: We selected 236 cases with initial diagnosis of DCIS followed by surgical ressection distributed in groups 1 (without invasion) and 2 (with invasive carcinoma). RESULTS: The risk of stromal invasion after a DCIS diagnosis in biopsy was associated to triple-negative profile and loss of CD10 expression by myoepithelial cells, and inversely associated with CK5/6 expression by neoplastic cells and high expression of Smooth Muscle Myosin Heavy Chain (SMMHC) by myoepithelial cells. CONCLUSIONS: A combination of characteristics of epithelial and myoepithelial cells in DCIS in biopsy specimens is related to the risk of stromal invasion.
[Mh] Termos MeSH primário: Neoplasias da Mama/química
Neoplasias da Mama/patologia
Carcinoma Ductal de Mama/química
Carcinoma Ductal de Mama/patologia
Carcinoma Intraductal não Infiltrante/química
Carcinoma Intraductal não Infiltrante/patologia
[Mh] Termos MeSH secundário: Biomarcadores Tumorais
Carcinoma Intraductal não Infiltrante/cirurgia
Feminino
Seres Humanos
Imuno-Histoquímica
Queratina-5/análise
Queratina-6/análise
Meia-Idade
Invasividade Neoplásica
Neprilisina/análise
Fenótipo
Receptor ErbB-2/análise
Receptores Estrogênicos/análise
Receptores de Progesterona/análise
Miosinas de Músculo Liso/análise
Microambiente Tumoral
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (Keratin-5); 0 (Keratin-6); 0 (Receptors, Estrogen); 0 (Receptors, Progesterone); EC 2.7.10.1 (ERBB2 protein, human); EC 2.7.10.1 (Receptor, ErbB-2); EC 3.4.24.11 (Neprilysin); EC 3.6.1.- (Smooth Muscle Myosins)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:151125
[Lr] Data última revisão:
151125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150924
[St] Status:MEDLINE
[do] DOI:10.3233/BD-150416


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[PMID]:26011134
[Au] Autor:Chen D; Xiong Y; Lin Y; Tang Z; Wang J; Wang L; Yao J
[Ad] Endereço:Department of Pharmacology, Dalian Medical University, Dalian, Liaoning Province, China.
[Ti] Título:Capsaicin alleviates abnormal intestinal motility through regulation of enteric motor neurons and MLCK activity: Relevance to intestinal motility disorders.
[So] Source:Mol Nutr Food Res;59(8):1482-90, 2015 Aug.
[Is] ISSN:1613-4133
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:SCOPE: Capsaicin is an active component of chili peppers, having diverse effects. However, the effects of capsaicin on intestinal motility are still controversial. The present study aimed to investigate the effects of capsaicin on intestinal motility disorder and uncover related mechanisms. MATERIALS AND RESULTS: A rat model with intestinal motility disorder was established in vitro through adding different stimuli into tissue bath; in vivo using constipation and diarrhea model, respectively. Capsaicin exerted dual effects on intestinal motility, i.e. the relaxation and contraction of jejunum induced by corresponding stimulus were, respectively, regulated to be normal contraction by capsaicin. The mechanisms underlined capsaicin-induced dual effects were investigated using Western blotting, qRT-PCR, and whole-cell patch clamp, respectively. Results showed that cholinergic excitatory nerves, adrenergic nerves, and neurons containing nitric oxide synthase, which are the main muscle motor neurons in enteric nervous system (ENS), are involved in capsaicin-induced dual effects. The competition for regulation of Ca(2+) influx by capsaicin induced the interaction with components of the ENS. Capsaicin significantly increased myosin light chain kinase (MLCK) expression and myosin phosphorylation extent in jejunal segments of constipation-prominent rats and significantly decreased MLCK expression and myosin phosphorylation extent in jejunal segments of diarrhea-prominent rats. CONCLUSION: In summary, capsaicin alleviates abnormal intestinal motility through regulating enteric motor neurons and MLCK activity, which is beneficial for the treatment of gastrointestinal motility disorders.
[Mh] Termos MeSH primário: Capsaicina/uso terapêutico
Constipação Intestinal/prevenção & controle
Diarreia/prevenção & controle
Suplementos Nutricionais
Sistema Nervoso Entérico/metabolismo
Fármacos Gastrointestinais/uso terapêutico
Quinase de Cadeia Leve de Miosina/metabolismo
[Mh] Termos MeSH secundário: Animais
Sinalização do Cálcio
Capsaicina/metabolismo
Células Cultivadas
Constipação Intestinal/metabolismo
Constipação Intestinal/patologia
Constipação Intestinal/fisiopatologia
Diarreia/metabolismo
Diarreia/patologia
Diarreia/fisiopatologia
Sistema Nervoso Entérico/fisiopatologia
Fármacos Gastrointestinais/metabolismo
Mucosa Intestinal/inervação
Mucosa Intestinal/metabolismo
Mucosa Intestinal/fisiopatologia
Jejuno/inervação
Jejuno/metabolismo
Jejuno/patologia
Jejuno/fisiopatologia
Masculino
Neurônios Motores/metabolismo
Músculo Liso/inervação
Músculo Liso/metabolismo
Músculo Liso/patologia
Músculo Liso/fisiopatologia
Quinase de Cadeia Leve de Miosina/antagonistas & inibidores
Quinase de Cadeia Leve de Miosina/química
Quinase de Cadeia Leve de Miosina/genética
Técnicas de Patch-Clamp
Fosforilação
Processamento de Proteína Pós-Traducional
Ratos Sprague-Dawley
Miosinas de Músculo Liso/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Gastrointestinal Agents); EC 2.7.11.18 (Myosin-Light-Chain Kinase); EC 3.6.1.- (Smooth Muscle Myosins); S07O44R1ZM (Capsaicin)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:150804
[Lr] Data última revisão:
150804
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150527
[St] Status:MEDLINE
[do] DOI:10.1002/mnfr.201500039


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[PMID]:25650929
[Au] Autor:Hilbert L; Balassy Z; Zitouni NB; Mackey MC; Lauzon AM
[Ad] Endereço:Department of Physiology, McGill University, Montréal, Québec, Canada; Centre for Applied Mathematics in Bioscience and Medicine, Montréal, Québec, Canada; Meakins-Christie Laboratories, Montréal, Québec, Canada. Electronic address: lennart.hilbert@mail.mcgill.ca.
[Ti] Título:Phosphate and ADP differently inhibit coordinated smooth muscle myosin groups.
[So] Source:Biophys J;108(3):622-31, 2015 Feb 03.
[Is] ISSN:1542-0086
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Actin filaments propelled in vitro by groups of skeletal muscle myosin motors exhibit distinct phases of active sliding or arrest, whose occurrence depends on actin length (L) within a range of up to 1.0 µm. Smooth muscle myosin filaments are exponentially distributed with ≈150 nm average length in vivo--suggesting relevance of the L-dependence of myosin group kinetics. Here, we found L-dependent actin arrest and sliding in in vitro motility assays of smooth muscle myosin. We perturbed individual myosin kinetics with varying, physiological concentrations of phosphate (Pi, release associated with main power stroke) and adenosine diphosphate (ADP, release associated with minor mechanical step). Adenosine triphosphate was kept constant at physiological concentration. Increasing [Pi] lowered the fraction of time for which actin was actively sliding, reflected in reduced average sliding velocity (ν) and motile fraction (fmot, fraction of time that filaments are moving); increasing [ADP] increased the fraction of time actively sliding and reduced the velocity while sliding, reflected in reduced ν and increased fmot. We introduced specific Pi and ADP effects on individual myosin kinetics into our recently developed mathematical model of actin propulsion by myosin groups. Simulations matched our experimental observations and described the inhibition of myosin group kinetics. At low [Pi] and [ADP], actin arrest and sliding were reflected by two distinct chemical states of the myosin group. Upon [Pi] increase, the probability of the active state decreased; upon [ADP] increase, the probability of the active state increased, but the active state became increasingly similar to the arrested state.
[Mh] Termos MeSH primário: Difosfato de Adenosina/farmacologia
Fosfatos/farmacologia
Miosinas de Músculo Liso/antagonistas & inibidores
[Mh] Termos MeSH secundário: Citoesqueleto de Actina/efeitos dos fármacos
Citoesqueleto de Actina/metabolismo
Actinas/metabolismo
Animais
Galinhas
Simulação por Computador
Cinética
Modelos Biológicos
Movimento
Miosinas de Músculo Liso/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Actins); 0 (Phosphates); 61D2G4IYVH (Adenosine Diphosphate); EC 3.6.1.- (Smooth Muscle Myosins)
[Em] Mês de entrada:1510
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150205
[St] Status:MEDLINE


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[PMID]:25428883
[Au] Autor:Zheng X; Reho JJ; Wirth B; Fisher SA
[Ad] Endereço:Division of Cardiovascular Medicine, School of Medicine, University of Maryland, Baltimore, Maryland;
[Ti] Título:TRA2ß controls Mypt1 exon 24 splicing in the developmental maturation of mouse mesenteric artery smooth muscle.
[So] Source:Am J Physiol Cell Physiol;308(4):C289-96, 2015 Feb 15.
[Is] ISSN:1522-1563
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Diversity of smooth muscle within the vascular system is generated by alternative splicing of exons, yet there is limited understanding of its timing or control mechanisms. We examined splicing of myosin phosphatase regulatory subunit (Mypt1) exon 24 (E24) in relation to smooth muscle myosin heavy chain (Smmhc) and smoothelin (Smtn) alternative exons (Smmhc E6 and Smtn E20) during maturation of mouse mesenteric artery (MA) smooth muscle. The role of transformer 2ß (Tra2ß), a master regulator of splicing in flies, in maturation of arterial smooth muscle was tested through gene inactivation. Splicing of alternative exons in bladder smooth muscle was examined for comparative purposes. MA smooth muscle maturation began after postnatal week 2 and was complete at maturity, as indicated by switching to Mypt1 E24+ and Smtn E20- splice variants and 11-fold induction of Smmhc. Similar changes in bladder were complete by postnatal day 3. Splicing of Smmhc E6 was temporally dissociated from Mypt1 E24 and Smtn E20 and discordant between arteries and bladder. Tamoxifen-induced smooth muscle-specific inactivation of Tra2ß within the first week of life but not in maturity reduced splicing of Mypt1 E24 in MAs. Inactivation of Tra2ß causing a switch to the isoform of MYPT1 containing the COOH-terminal leucine zipper motif (E24-) increased arterial sensitivity to cGMP-mediated relaxation. In conclusion, maturation of mouse MA smooth muscle begins postnatally and continues until sexual maturity. TRA2ß is required for specification during this period of maturation, and its inactivation alters the contractile properties of mature arterial smooth muscle.
[Mh] Termos MeSH primário: Processamento Alternativo
Diferenciação Celular
Éxons
Músculo Liso Vascular/enzimologia
Miócitos de Músculo Liso/enzimologia
Quinase de Cadeia Leve de Miosina/metabolismo
Proteínas Nucleares/metabolismo
Proteínas de Ligação a RNA/metabolismo
[Mh] Termos MeSH secundário: Fatores Etários
Animais
GMP Cíclico/análogos & derivados
GMP Cíclico/farmacologia
Proteínas do Citoesqueleto/genética
Proteínas do Citoesqueleto/metabolismo
Relação Dose-Resposta a Droga
Feminino
Regulação da Expressão Gênica no Desenvolvimento
Genótipo
Técnicas In Vitro
Masculino
Artérias Mesentéricas/enzimologia
Camundongos Endogâmicos C57BL
Camundongos Knockout
Proteínas Musculares/genética
Proteínas Musculares/metabolismo
Músculo Liso Vascular/efeitos dos fármacos
Miócitos de Músculo Liso/efeitos dos fármacos
Cadeias Pesadas de Miosina/genética
Cadeias Pesadas de Miosina/metabolismo
Quinase de Cadeia Leve de Miosina/genética
Fosfatase de Miosina-de-Cadeia-Leve
Proteínas Nucleares/deficiência
Proteínas Nucleares/genética
Fenótipo
Proteínas de Ligação a RNA/genética
Fatores de Processamento de Serina-Arginina
Miosinas de Músculo Liso/genética
Miosinas de Músculo Liso/metabolismo
Vasodilatação
Vasodilatadores/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Cytoskeletal Proteins); 0 (Muscle Proteins); 0 (Nuclear Proteins); 0 (RNA-Binding Proteins); 0 (Smtn protein, mouse); 0 (Tra2b protein, mouse); 0 (Vasodilator Agents); 170974-22-8 (Serine-Arginine Splicing Factors); 31356-94-2 (8-bromocyclic GMP); EC 2.7.11.18 (Myosin-Light-Chain Kinase); EC 3.1.3.53 (Myosin-Light-Chain Phosphatase); EC 3.1.3.53 (Ppp1r12a protein, mouse); EC 3.6.1.- (Smooth Muscle Myosins); EC 3.6.4.1 (Myosin Heavy Chains); H2D2X058MU (Cyclic GMP)
[Em] Mês de entrada:1504
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141128
[St] Status:MEDLINE
[do] DOI:10.1152/ajpcell.00304.2014


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[PMID]:25319851
[Au] Autor:Ogata F; Fujiu K; Koshima I; Nagai R; Manabe I
[Ad] Endereço:Department of Cardiovascular Medicine, Graduate School of Medicine, University of Tokyo, 7-3-1 Hongo, Bunkyo, Tokyo, 113-8655, Japan.
[Ti] Título:Phenotypic modulation of smooth muscle cells in lymphoedema.
[So] Source:Br J Dermatol;172(5):1286-93, 2015.
[Is] ISSN:1365-2133
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Lymphoedema is a debilitating progressive condition that is frequently observed following cancer surgery and severely restricts quality of life. Although it is known that lymphatic dysfunction and obstruction underlie lymphoedema, the pathogenic mechanism is poorly understood. Smooth muscle cells (SMCs) play pivotal roles in the pathogenesis of various vascular diseases, including atherosclerosis. OBJECTIVES: We analysed SMCs in lymphatic vessels from the lymphoedematous legs of 29 patients. METHODS: Expression of smooth muscle α-actin (SMαA) and smooth muscle myosin heavy chain (SM-MHC) isoforms SM1 and SM2 was investigated using immunohistochemistry. RESULTS: Compared with normal lymphatic vessels, all affected lymphatic vessels in chronic lymphoedema showed marked wall thickening. In addition to increases in the numbers of rows of SMαA(+) SM1(+) SMCs in the tunica media, SMCs were also observed in the subendothelial region (tunica intima). While most intimal and medial cells were positive for SMαA and SM1, staining for SM1 and particularly SM2, a marker of mature SMCs, progressively declined in lymphatic vessels in increasingly severe lymphoedema lesions. Consequently, the SM1(+) and SM2(+) cell fractions were significantly reduced in the tunica media and intima of lymphatic vessels. CONCLUSIONS: These observations indicate that the lymphatic tunica media and tunica intima consist mainly of phenotypically modulated SMCs, and that SMCs play a key role in the development of lymphoedema.
[Mh] Termos MeSH primário: Linfedema/patologia
Miócitos de Músculo Liso/fisiologia
[Mh] Termos MeSH secundário: Actinas/metabolismo
Adulto
Idoso
Idoso de 80 Anos ou mais
Doença Crônica
Feminino
Fibrose/patologia
Seres Humanos
Imuno-Histoquímica
Vasos Linfáticos/metabolismo
Vasos Linfáticos/patologia
Linfedema/metabolismo
Masculino
Microscopia Eletrônica de Transmissão
Meia-Idade
Miócitos de Músculo Liso/metabolismo
Cadeias Pesadas de Miosina/metabolismo
Fenótipo
Miosinas de Músculo Liso/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Actins); EC 3.6.1.- (Smooth Muscle Myosins); EC 3.6.4.1 (Myosin Heavy Chains)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:150512
[Lr] Data última revisão:
150512
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141017
[St] Status:MEDLINE
[do] DOI:10.1111/bjd.13482


  10 / 134 MEDLINE  
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[PMID]:25324571
[Au] Autor:Rozenberg JM; Tesfu DB; Musunuri S; Taylor JM; Mack CP
[Ad] Endereço:From the Department of Pathology, University of North Carolina, Chapel Hill.
[Ti] Título:DNA methylation of a GC repressor element in the smooth muscle myosin heavy chain promoter facilitates binding of the Notch-associated transcription factor, RBPJ/CSL1.
[So] Source:Arterioscler Thromb Vasc Biol;34(12):2624-31, 2014 Dec.
[Is] ISSN:1524-4636
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: The goal of the present study was to identify novel mechanisms that regulate smooth muscle cell (SMC) differentiation marker gene expression. APPROACH AND RESULTS: We demonstrate that the CArG-containing regions of many SMC-specific promoters are imbedded within CpG islands. A previously identified GC repressor element in the SM myosin heavy chain (MHC) promoter was highly methylated in cultured aortic SMC but not in the aorta, and this difference was inversely correlated with SM MHC expression. Using an affinity chromatography/mass spectroscopy-based approach, we identified the multifunctional Notch transcription factor, recombination signal binding protein for immunoglobulin κ J region (RBPJ), as a methylated GC repressor-binding protein. RBPJ protein levels and binding to the endogenous SM MHC GC repressor were enhanced by platelet-derived growth factor-BB treatment. A methylation mimetic mutation to the GC repressor that facilitated RBPJ binding inhibited SM MHC promoter activity as did overexpression of RBPJ. Consistent with this, knockdown of RBPJ in phenotypically modulated human aortic SMC enhanced endogenous SMC marker gene expression, an effect likely mediated by increased recruitment of serum response factor and Pol II to the SMC-specific promoters. In contrast, the depletion of RBPJ in differentiated transforming growth factor-ß-treated SMC inhibited SMC-specific gene activation, supporting the idea that the effects of RBPJ/Notch signaling are context dependent. CONCLUSIONS: Our results indicate that methylation-dependent binding of RBPJ to a GC repressor element can negatively regulate SM MHC promoter activity and that RBPJ can inhibit SMC marker gene expression in phenotypically modulated SMC. These results will have important implications on the regulation of SMC phenotype and on Notch-dependent transcription.
[Mh] Termos MeSH primário: Proteína de Ligação a Sequências Sinal de Recombinação J de Imunoglobina/metabolismo
Cadeias Pesadas de Miosina/genética
Regiões Promotoras Genéticas
Miosinas de Músculo Liso/genética
[Mh] Termos MeSH secundário: Animais
Sequência de Bases
Diferenciação Celular/genética
Diferenciação Celular/fisiologia
Células Cultivadas
Ilhas de CpG
Metilação de DNA
Sequência Rica em GC
Seres Humanos
Proteína de Ligação a Sequências Sinal de Recombinação J de Imunoglobina/deficiência
Proteína de Ligação a Sequências Sinal de Recombinação J de Imunoglobina/genética
Camundongos
Camundongos Knockout
Dados de Sequência Molecular
Miócitos de Músculo Liso/citologia
Miócitos de Músculo Liso/metabolismo
Ligação Proteica
Proteínas Proto-Oncogênicas c-sis/metabolismo
Receptores Notch/metabolismo
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Immunoglobulin J Recombination Signal Sequence-Binding Protein); 0 (Proto-Oncogene Proteins c-sis); 0 (RBPJ protein, human); 0 (Rbpj protein, mouse); 0 (Receptors, Notch); 1B56C968OA (becaplermin); EC 3.6.1.- (Smooth Muscle Myosins); EC 3.6.4.1 (Myosin Heavy Chains)
[Em] Mês de entrada:1504
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141018
[St] Status:MEDLINE
[do] DOI:10.1161/ATVBAHA.114.304634



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