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[PMID]: 27174949 [Au] Autor: Sessions AO; Engler AJ [Ad] Endereço: From the Biomedical Sciences Program (A.O.S., A.J.E.) and Department of Bioengineering, University of California, San Diego, La Jolla (A.J.E.); and Sanford Consortium for Regenerative Medicine, La Jolla, CA (A.J.E.). [Ti] Título: Mechanical Regulation of Cardiac Aging in Model Systems. [So] Source: Circ Res;118(10):1553-62, 2016 May 13. [Is] ISSN: 1524-4571 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Unlike diet and exercise, which individuals can modulate according to their lifestyle, aging is unavoidable. With normal or healthy aging, the heart undergoes extensive vascular, cellular, and interstitial molecular changes that result in stiffer less compliant hearts that experience a general decline in organ function. Although these molecular changes deemed cardiac remodeling were once thought to be concomitant with advanced cardiovascular disease, they can be found in patients without manifestation of clinical disease. It is now mostly acknowledged that these age-related mechanical changes confer vulnerability of the heart to cardiovascular stresses associated with disease, such as hypertension and atherosclerosis. However, recent studies have aimed at differentiating the initial compensatory changes that occur within the heart with age to maintain contractile function from the maladaptive responses associated with disease. This work has identified new targets to improve cardiac function during aging. Spanning invertebrate to vertebrate models, we use this review to delineate some hallmarks of physiological versus pathological remodeling that occur in the cardiomyocyte and its microenvironment, focusing especially on the mechanical changes that occur within the sarcomere, intercalated disc, costamere, and extracellular matrix. [Mh] Termos MeSH primário: Doenças Cardiovasculares/genética Drosophila/genética Coração/crescimento & desenvolvimento Miócitos Cardíacos/metabolismo [Mh] Termos MeSH secundário: Animais Doenças Cardiovasculares/metabolismo Costâmeros/metabolismo Modelos Animais de Doenças Drosophila/metabolismo Matriz Extracelular/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE; REVIEW [Em] Mês de entrada: 1704 [Cu] Atualização por classe: 170513 [Lr] Data última revisão: 170513 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 160514 [St] Status: MEDLINE [do] DOI: 10.1161/CIRCRESAHA.116.307472

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[PMID]: 26996782 [Au] Autor: Calvet CM; Silva TA; DE Melo TG; DE Araújo-Jorge TC; Pereira MC [Ad] Endereço: Laboratório de Ultraestrutura Celular,Fundação Oswaldo Cruz,Av. Brasil 4365,Pav. Carlos Chagas 3° andar,Rio de Janeiro,Brazil. [Ti] Título: TGF-ß receptor type II costameric localization in cardiomyocytes and host cell TGF-ß response is disrupted by Trypanosoma cruzi infection. [So] Source: Parasitology;143(6):704-15, 2016 05. [Is] ISSN: 1469-8161 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: Transforming growth factor beta (TGF-ß) cytokine is involved in Chagas disease establishment and progression. Since Trypanosoma cruzi can modulate host cell receptors, we analysed the TGF-ß receptor type II (TßRII) expression and distribution during T. cruzi - cardiomyocyte interaction. TßRII immunofluorescent staining revealed a striated organization in cardiomyocytes, which was co-localized with vinculin costameres and enhanced (38%) after TGF-ß treatment. Cytochalasin D induced a decrease of 45·3% in the ratio of cardiomyocytes presenting TßRII striations, demonstrating an association of TßRII with the cytoskeleton. Western blot analysis showed that cytochalasin D significantly inhibited Smad 2 phosphorylation and fibronectin stimulation after TGF-ß treatment in cardiomyocytes. Trypanosoma cruzi infection elicited a decrease of 79·8% in the frequency of cardiomyocytes presenting TßRII striations, but did not interfere significantly in its expression. In addition, T. cruzi-infected cardiomyocytes present a lower response to exogenous TGF-ß, showing no enhancement of TßRII striations and a reduction of phosphorylated Smad 2, with no significant difference in TßRII expression when compared to uninfected cells. Together, these results suggest that the co-localization of TßRII with costameres is important in activating the TGF-ß signalling cascade, and that T. cruzi-derived cytoskeleton disorganization could result in altered or low TGF-ß response in infected cardiomyocytes. [Mh] Termos MeSH primário: Doença de Chagas/fisiopatologia Costâmeros/metabolismo Interações Hospedeiro-Parasita/fisiologia Miócitos Cardíacos/patologia Proteínas Serina-Treonina Quinases/metabolismo Receptores de Fatores de Crescimento Transformadores beta/metabolismo [Mh] Termos MeSH secundário: Animais Células Cultivadas Regulação da Expressão Gênica/efeitos dos fármacos Interações Hospedeiro-Parasita/efeitos dos fármacos Camundongos Miócitos Cardíacos/parasitologia Transporte Proteico/efeitos dos fármacos Transporte Proteico/fisiologia Transdução de Sinais/efeitos dos fármacos Fator de Crescimento Transformador beta/metabolismo Fator de Crescimento Transformador beta/farmacologia Trypanosoma cruzi/fisiologia [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nome de substância: 0 (Receptors, Transforming Growth Factor beta); 0 (Transforming Growth Factor beta); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.30 (transforming growth factor-beta type II receptor) [Em] Mês de entrada: 1704 [Cu] Atualização por classe: 170407 [Lr] Data última revisão: 170407 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 160322 [St] Status: MEDLINE [do] DOI: 10.1017/S0031182016000299

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[PMID]: 26088790 [Au] Autor: Jaka O; Casas-Fraile L; López de Munain A; Sáenz A [Ad] Endereço: Neurosciences Area,BioDonostia Institute,Paseo Dr. Begiristain s/n,20014 San Sebastián,Spain. [Ti] Título: Costamere proteins and their involvement in myopathic processes. [So] Source: Expert Rev Mol Med;17:e12, 2015 Jun 19. [Is] ISSN: 1462-3994 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: Muscle fibres are very specialised cells with a complex structure that requires a high level of organisation of the constituent proteins. For muscle contraction to function properly, there is a need for not only sarcomeres, the contractile structures of the muscle fibre, but also costameres. These are supramolecular structures associated with the sarcolemma that allow muscle adhesion to the extracellular matrix. They are composed of protein complexes that interact and whose functions include maintaining cell structure and signal transduction mediated by their constituent proteins. It is important to improve our understanding of these structures, as mutations in various genes that code for costamere proteins cause many types of muscular dystrophy. In this review, we provide a description of costameres detailing each of their constituent proteins, such as dystrophin, dystrobrevin, syntrophin, sarcoglycans, dystroglycans, vinculin, talin, integrins, desmin, plectin, etc. We describe as well the diseases associated with deficiency thereof, providing a general overview of their importance. [Mh] Termos MeSH primário: Desmina/genética Distroglicanas/genética Distrofina/genética Doenças Musculares/genética [Mh] Termos MeSH secundário: Costâmeros/genética Costâmeros/metabolismo Costâmeros/ultraestrutura Desmina/química Desmina/metabolismo Distroglicanas/química Distroglicanas/metabolismo Distrofina/química Distrofina/metabolismo Proteínas Associadas à Distrofina/química Proteínas Associadas à Distrofina/genética Proteínas Associadas à Distrofina/metabolismo Expressão Gênica Seres Humanos Integrinas/química Integrinas/genética Integrinas/metabolismo Contração Muscular Doenças Musculares/metabolismo Doenças Musculares/patologia Mutação Plectina/química Plectina/genética Plectina/metabolismo Sarcolema/genética Sarcolema/metabolismo Sarcolema/ultraestrutura Sarcômeros/genética Sarcômeros/metabolismo Sarcômeros/ultraestrutura Talina/química Talina/genética Talina/metabolismo Vinculina/química Vinculina/genética Vinculina/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW [Nm] Nome de substância: 0 (Desmin); 0 (Dystrophin); 0 (Dystrophin-Associated Proteins); 0 (Integrins); 0 (Plectin); 0 (Talin); 0 (dystrobrevin); 0 (syntrophin); 125361-02-6 (Vinculin); 146888-27-9 (Dystroglycans) [Em] Mês de entrada: 1603 [Cu] Atualização por classe: 150619 [Lr] Data última revisão: 150619 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 150620 [St] Status: MEDLINE [do] DOI: 10.1017/erm.2015.9

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[PMID]: 25567810 [Au] Autor: García-Pelagio KP; Muriel J; O'Neill A; Desmond PF; Lovering RM; Lund L; Bond M; Bloch RJ [Ad] Endereço: Department of Physiology, School of Medicine, University of Maryland, Baltimore, Maryland; [Ti] Título: Myopathic changes in murine skeletal muscle lacking synemin. [So] Source: Am J Physiol Cell Physiol;308(6):C448-62, 2015 Mar 15. [Is] ISSN: 1522-1563 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Diseases of striated muscle linked to intermediate filament (IF) proteins are associated with defects in the organization of the contractile apparatus and its links to costameres, which connect the sarcomeres to the cell membrane. Here we study the role in skeletal muscle of synemin, a type IV IF protein, by examining mice null for synemin (synm-null). Synm-null mice have a mild skeletal muscle phenotype. Tibialis anterior (TA) muscles show a significant decrease in mean fiber diameter, a decrease in twitch and tetanic force, and an increase in susceptibility to injury caused by lengthening contractions. Organization of proteins associated with the contractile apparatus and costameres is not significantly altered in the synm-null. Elastimetry of the sarcolemma and associated contractile apparatus in extensor digitorum longus myofibers reveals a reduction in tension consistent with an increase in sarcolemmal deformability. Although fatigue after repeated isometric contractions is more marked in TA muscles of synm-null mice, the ability of the mice to run uphill on a treadmill is similar to controls. Our results suggest that synemin contributes to linkage between costameres and the contractile apparatus and that the absence of synemin results in decreased fiber size and increased sarcolemmal deformability and susceptibility to injury. Thus synemin plays a moderate but distinct role in fast twitch skeletal muscle. [Mh] Termos MeSH primário: Proteínas de Filamentos Intermediários/deficiência Contração Isométrica Força Muscular Músculo Esquelético/metabolismo Doenças Musculares/metabolismo [Mh] Termos MeSH secundário: Animais Fenômenos Biomecânicos Costâmeros/metabolismo Costâmeros/patologia Genótipo Proteínas de Filamentos Intermediários/genética Masculino Camundongos Endogâmicos C57BL Camundongos Knockout Fadiga Muscular Fibras Musculares de Contração Rápida/metabolismo Fibras Musculares de Contração Rápida/patologia Músculo Esquelético/patologia Músculo Esquelético/fisiopatologia Doenças Musculares/etiologia Doenças Musculares/genética Doenças Musculares/patologia Doenças Musculares/fisiopatologia Fenótipo Corrida Sarcolema/metabolismo Sarcolema/patologia [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nome de substância: 0 (Intermediate Filament Proteins); 0 (synemin protein, mouse) [Em] Mês de entrada: 1509 [Cu] Atualização por classe: 170220 [Lr] Data última revisão: 170220 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 150109 [St] Status: MEDLINE [do] DOI: 10.1152/ajpcell.00331.2014

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[PMID]: 25555464 [Au] Autor: Al Haj A; Mazur AJ; Radaszkiewicz K; Radaszkiewicz T; Makowiecka A; Stopschinski BE; Schönichen A; Geyer M; Mannherz HG [Ad] Endereço: Department of Anatomy and Molecular Embryology, Ruhr-University, Bochum, Germany. [Ti] Título: Distribution of formins in cardiac muscle: FHOD1 is a component of intercalated discs and costameres. [So] Source: Eur J Cell Biol;94(2):101-13, 2015 Feb. [Is] ISSN: 1618-1298 [Cp] País de publicação: Germany [La] Idioma: eng [Ab] Resumo: The formin homology domain-containing protein1 (FHOD1) suppresses actin polymerization by inhibiting nucleation, but bundles actin filaments and caps filament barbed ends. Two polyclonal antibodies against FHOD1 were generated against (i) its N-terminal sequence (residues 1-339) and (ii) a peptide corresponding the sequence from position 358-371, which is unique for FHOD1 and does not occur in its close relative FHOD3. After affinity purification both antibodies specifically stain purified full length FHOD1 and a band of similar molecular mass in homogenates of cardiac muscle. The antibody against the N-terminus of FHOD1 was used for immunostaining cells of established lines, primary neonatal (NRC) and adult (ARC) rat cardiomyocytes and demonstrated the presence of FHOD1 in HeLa and fibroblastic cells along stress fibers and within presumed lamellipodia and actin arcs. In NRCs and ARCs we observed a prominent staining of presumed intercalated discs (ICD). Immunostaining of sections of hearts with both anti-FHOD1 antibodies confirmed the presence of FHOD1 in ICDs and double immunostaining demonstrated its colocalisation with cadherin, plakoglobin and a probably slightly shifted localization to connexin43. Similarly, immunostaining of isolated mouse or pig ICDs corroborated the presence of FHOD1 and its colocalisation with the mentioned cell junctional components. Anti-FHOD1 immunoblots of isolated ICDs demonstrated the presence of an immunoreactive band comigrating with purified FHOD1. Conversely, an anti-peptide antibody specific for FHOD3 with no cross-reactivity against FHOD1 immunostained on sections of cardiac muscle and ARCs the myofibrils in a cross-striated pattern but not the ICDs. In addition, the anti-peptide-FHOD1 antibody stained the lateral sarcolemma of ARCs in a banded pattern. Double immunostaining with anti-cadherin and -integrin-ß1 indicated the additional localization of FHOD1 in costameres. Immunostaining of cardiac muscle sections or ARCs with antibodies against mDia3-FH2-domain showed colocalisation with cadherin along the lateral border of cardiomyocytes suggesting also its presence in costameres. [Mh] Termos MeSH primário: Costâmeros/metabolismo Proteínas Fetais/metabolismo Miocárdio/metabolismo Proteínas Nucleares/metabolismo [Mh] Termos MeSH secundário: Animais Animais Recém-Nascidos Anticorpos/metabolismo Caderinas/metabolismo Linhagem Celular Conexina 43/metabolismo Seres Humanos Camundongos Proteínas dos Microfilamentos/metabolismo Miocárdio/citologia Miócitos Cardíacos/metabolismo Miócitos Cardíacos/ultraestrutura Ratos Fibras de Estresse/metabolismo Suínos gama Catenina/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nome de substância: 0 (Antibodies); 0 (Cadherins); 0 (Connexin 43); 0 (FHOD1 protein, human); 0 (FHOD3 protein, human); 0 (Fetal Proteins); 0 (Microfilament Proteins); 0 (Nuclear Proteins); 0 (gamma Catenin) [Em] Mês de entrada: 1508 [Cu] Atualização por classe: 150209 [Lr] Data última revisão: 150209 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 150104 [St] Status: MEDLINE

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[PMID]: 25488665 [Au] Autor: Mlih M; Host L; Martin S; Niederhoffer N; Monassier L; Terrand J; Messaddeq N; Radke M; Gotthardt M; Bruban V; Kober F; Bernard M; Canet-Soulas E; Abt-Jijon F; Boucher P; Matz RL [Ad] Endereço: From the CNRS, UMR 7213, University of Strasbourg, 67401 Illkirch, France. [Ti] Título: The Src homology and collagen A (ShcA) adaptor protein is required for the spatial organization of the costamere/Z-disk network during heart development. [So] Source: J Biol Chem;290(4):2419-30, 2015 Jan 23. [Is] ISSN: 1083-351X [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Src homology and collagen A (ShcA) is an adaptor protein that binds to tyrosine kinase receptors. Its germ line deletion is embryonic lethal with abnormal cardiovascular system formation, and its role in cardiovascular development is unknown. To investigate its functional role in cardiovascular development in mice, ShcA was deleted in cardiomyocytes and vascular smooth muscle cells by crossing ShcA flox mice with SM22a-Cre transgenic mice. Conditional mutant mice developed signs of severe dilated cardiomyopathy, myocardial infarctions, and premature death. No evidence of a vascular contribution to the phenotype was observed. Histological analysis of the heart revealed aberrant sarcomeric Z-disk and M-band structures, and misalignments of T-tubules with Z-disks. We find that not only the ErbB3/Neuregulin signaling pathway but also the baroreceptor reflex response, which have been functionally associated, are altered in the mutant mice. We further demonstrate that ShcA interacts with Caveolin-1 and the costameric protein plasma membrane Ca(2+)/calmodulin-dependent ATPase (PMCA), and that its deletion leads to abnormal dystrophin signaling. Collectively, these results demonstrate that ShcA interacts with crucial proteins and pathways that link Z-disk and costamere. [Mh] Termos MeSH primário: Costâmeros/metabolismo Coração/embriologia Miócitos Cardíacos/metabolismo Miócitos de Músculo Liso/metabolismo Proteínas Adaptadoras da Sinalização Shc/metabolismo [Mh] Termos MeSH secundário: Alelos Animais Aorta Torácica/metabolismo Pressão Sanguínea Sobrevivência Celular Distrofina/metabolismo Ecocardiografia Deleção de Genes Regulação da Expressão Gênica no Desenvolvimento Imagem por Ressonância Magnética Camundongos Camundongos Transgênicos Microscopia Confocal Fenótipo ATPases Transportadoras de Cálcio da Membrana Plasmática/metabolismo RNA Interferente Pequeno/metabolismo Ratos Receptor ErbB-3/metabolismo Proteínas Adaptadoras da Sinalização Shc/genética Proteína 1 de Transformação que Contém Domínio 2 de Homologia de Src [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nome de substância: 0 (Dystrophin); 0 (RNA, Small Interfering); 0 (Shc Signaling Adaptor Proteins); 0 (Shc1 protein, mouse); 0 (Src Homology 2 Domain-Containing, Transforming Protein 1); EC 2.7.10.1 (Receptor, ErbB-3); EC 3.6.3.8 (Plasma Membrane Calcium-Transporting ATPases) [Em] Mês de entrada: 1504 [Cu] Atualização por classe: 170220 [Lr] Data última revisão: 170220 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 141210 [St] Status: MEDLINE [do] DOI: 10.1074/jbc.M114.597377

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[PMID]: 25313365 [Au] Autor: Flück M; Li R; Valdivieso P; Linnehan RM; Castells J; Tesch P; Gustafsson T [Ad] Endereço: Balgrist University Hospital, University of Zurich, Switzerland ; Laboratory for Muscle Plasticity, Balgrist University Hospital, Forchstrasse 340, 8008 Zurich, Switzerland. [Ti] Título: Early changes in costameric and mitochondrial protein expression with unloading are muscle specific. [So] Source: Biomed Res Int;2014:519310, 2014. [Is] ISSN: 2314-6141 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: We hypothesised that load-sensitive expression of costameric proteins, which hold the sarcomere in place and position the mitochondria, contributes to the early adaptations of antigravity muscle to unloading and would depend on muscle fibre composition and chymotrypsin activity of the proteasome. Biopsies were obtained from vastus lateralis (VL) and soleus (SOL) muscles of eight men before and after 3 days of unilateral lower limb suspension (ULLS) and subjected to fibre typing and measures for costameric (FAK and FRNK), mitochondrial (NDUFA9, SDHA, UQCRC1, UCP3, and ATP5A1), and MHCI protein and RNA content. Mean cross-sectional area (MCSA) of types I and II muscle fibres in VL and type I fibres in SOL demonstrated a trend for a reduction after ULLS (0.05 ≤ P < 0.10). FAK phosphorylation at tyrosine 397 showed a 20% reduction in VL muscle (P = 0.029). SOL muscle demonstrated a specific reduction in UCP3 content (-23%; P = 0.012). Muscle-specific effects of ULLS were identified for linear relationships between measured proteins, chymotrypsin activity and fibre MCSA. The molecular modifications in costamere turnover and energy homoeostasis identify that aspects of atrophy and fibre transformation are detectable at the protein level in weight-bearing muscles within 3 days of unloading. [Mh] Termos MeSH primário: Costâmeros/metabolismo Proteínas Mitocondriais/metabolismo Músculos/metabolismo [Mh] Termos MeSH secundário: Adulto Quimotripsina/metabolismo Proteína-Tirosina Quinases de Adesão Focal/metabolismo Regulação da Expressão Gênica Seres Humanos Masculino Fibras Musculares Esqueléticas/metabolismo Especificidade de Órgãos Oxirredução Fenótipo Fosforilação Fosfotirosina/metabolismo Complexo de Endopeptidases do Proteassoma/genética Complexo de Endopeptidases do Proteassoma/metabolismo RNA Mensageiro/genética RNA Mensageiro/metabolismo Suporte de Carga [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nome de substância: 0 (Mitochondrial Proteins); 0 (RNA, Messenger); 21820-51-9 (Phosphotyrosine); EC 2.7.10.2 (Focal Adhesion Protein-Tyrosine Kinases); EC 3.4.21.1 (Chymotrypsin); EC 3.4.25.1 (Proteasome Endopeptidase Complex) [Em] Mês de entrada: 1507 [Cu] Atualização por classe: 170220 [Lr] Data última revisão: 170220 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 141015 [St] Status: MEDLINE [do] DOI: 10.1155/2014/519310

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[PMID]: 24798732 [Au] Autor: Vassilopoulos S; Gentil C; Lainé J; Buclez PO; Franck A; Ferry A; Précigout G; Roth R; Heuser JE; Brodsky FM; Garcia L; Bonne G; Voit T; Piétri-Rouxel F; Bitoun M [Ad] Endereço: Institut National de la Santé et de la Recherche Médicale (INSERM) U974, 2 Centre National de la Recherche Scientifique (CNRS) UMR 7215, and 3 Université Pierre et Marie Curie-Paris 6, UM 76, Paris F-75013, France. [Ti] Título: Actin scaffolding by clathrin heavy chain is required for skeletal muscle sarcomere organization. [So] Source: J Cell Biol;205(3):377-93, 2014 May 12. [Is] ISSN: 1540-8140 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: The ubiquitous clathrin heavy chain (CHC), the main component of clathrin-coated vesicles, is well characterized for its role in intracellular membrane traffic and endocytosis from the plasma membrane (PM). Here, we demonstrate that in skeletal muscle CHC regulates the formation and maintenance of PM-sarcomere attachment sites also known as costameres. We show that clathrin forms large coated lattices associated with actin filaments and the muscle-specific isoform of α-actinin at the PM of differentiated myotubes. Depletion of CHC in myotubes induced a loss of actin and α-actinin sarcomeric organization, whereas CHC depletion in vivo induced a loss of contractile force due to the detachment of sarcomeres from the PM. Our results suggest that CHC contributes to the formation and maintenance of the contractile apparatus through interactions with costameric proteins and highlight an unconventional role for CHC in skeletal muscle that may be relevant to pathophysiology of neuromuscular disorders. [Mh] Termos MeSH primário: Citoesqueleto de Actina/metabolismo Actinas/metabolismo Cadeias Pesadas de Clatrina/metabolismo Costâmeros/metabolismo Fibras Musculares Esqueléticas/metabolismo Sarcômeros/metabolismo [Mh] Termos MeSH secundário: Células 3T3 Actinina/metabolismo Animais Cadeias Pesadas de Clatrina/genética Costâmeros/patologia Proteínas de Ligação a DNA/metabolismo Dependovirus/genética Dinamina II/metabolismo Técnicas de Transferência de Genes Vetores Genéticos Camundongos Camundongos Endogâmicos C57BL Contração Muscular Fibras Musculares Esqueléticas/patologia Força Muscular Distrofias Musculares/metabolismo Distrofias Musculares/patologia Distrofias Musculares/fisiopatologia Miopatias Congênitas Estruturais/metabolismo Miopatias Congênitas Estruturais/patologia Miopatias Congênitas Estruturais/fisiopatologia Sarcômeros/patologia Fatores de Tempo [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 (DNA-Binding Proteins); 0 (Hip1r protein, mouse); 11003-00-2 (Actinin); 114899-12-6 (Clathrin Heavy Chains); EC 3.6.5.5 (Dynamin II) [Em] Mês de entrada: 1406 [Cu] Atualização por classe: 161019 [Lr] Data última revisão: 161019 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 140507 [St] Status: MEDLINE [do] DOI: 10.1083/jcb.201309096

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[PMID]: 24613615 [Au] Autor: Myhre JL; Hills JA; Jean F; Pilgrim DB [Ad] Endereço: Department of Biological Sciences, CW405, Biological Sciences Building, University of Alberta, Edmonton, AB, Canada T6G 2E9. [Ti] Título: Unc45b is essential for early myofibrillogenesis and costamere formation in zebrafish. [So] Source: Dev Biol;390(1):26-40, 2014 Jun 01. [Is] ISSN: 1095-564X [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Despite the prevalence of developmental myopathies resulting from muscle fiber defects, the earliest stages of myogenesis remain poorly understood. Unc45b is a molecular chaperone that mediates the folding of thick-filament myosin during sarcomere formation; however, Unc45b may also mediate specific functions of non-muscle myosins (NMMs). unc45b Mutants have specific defects in striated muscle development, which include myocyte detachment indicative of dysfunctional adhesion complex formation. Given the necessity for non-muscle myosin function in the formation of adhesion complexes and premyofibril templates, we tested the hypothesis that the unc45b mutant phenotype is not mediated solely by interaction with muscle myosin heavy chain (mMHC). We used the advantages of a transparent zebrafish embryo to determine the temporal and spatial patterns of expression for unc45b, non-muscle myosins and mMHC in developing somites. We also examined the formation of myocyte attachment complexes (costameres) in wild-type and unc45b mutant embryos. Our results demonstrate co-expression and co-regulation of Unc45b and NMM in myogenic tissue several hours before any muscle myosin heavy chain is expressed. We also note deficiencies in the localization of costamere components and NMM in unc45b mutants that is consistent with an NMM-mediated role for Unc45b during early myogenesis. This represents a novel role for Unc45b in the earliest stages of muscle development that is independent of muscle mMHC folding. [Mh] Termos MeSH primário: Costâmeros/genética Chaperonas Moleculares/genética Miofibrilas/genética Proteínas de Peixe-Zebra/genética Peixe-Zebra/genética [Mh] Termos MeSH secundário: Animais Costâmeros/metabolismo Embrião não Mamífero/embriologia Embrião não Mamífero/metabolismo Regulação da Expressão Gênica no Desenvolvimento Hibridização In Situ Microscopia Confocal Chaperonas Moleculares/metabolismo Mutação Mioblastos/metabolismo Miofibrilas/metabolismo Miosina não Muscular Tipo IIB/genética Miosina não Muscular Tipo IIB/metabolismo Somitos/embriologia Somitos/metabolismo Fatores de Tempo Peixe-Zebra/embriologia Peixe-Zebra/metabolismo Proteínas de Peixe-Zebra/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nome de substância: 0 (Molecular Chaperones); 0 (Unc45b protein, zebrafish); 0 (Zebrafish Proteins); EC 3.6.1.- (Nonmuscle Myosin Type IIB) [Em] Mês de entrada: 1406 [Cu] Atualização por classe: 140411 [Lr] Data última revisão: 140411 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 140312 [St] Status: MEDLINE

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MEDLINE

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[PMID]: 24218011 [Au] Autor: Estrella NL; Naya FJ [Ad] Endereço: Department of Biology, Program in Cell and Molecular Biology, Boston University, 24 Cummington Mall, Boston, MA, 02215, USA. [Ti] Título: Transcriptional networks regulating the costamere, sarcomere, and other cytoskeletal structures in striated muscle. [So] Source: Cell Mol Life Sci;71(9):1641-56, 2014 May. [Is] ISSN: 1420-9071 [Cp] País de publicação: Switzerland [La] Idioma: eng [Ab] Resumo: Structural abnormalities in striated muscle have been observed in numerous transcription factor gain- and loss-of-function phenotypes in animal and cell culture model systems, indicating that transcription is important in regulating the cytoarchitecture. While most characterized cytoarchitectural defects are largely indistinguishable by histological and ultrastructural criteria, analysis of dysregulated gene expression in each mutant phenotype has yielded valuable information regarding specific structural gene programs that may be uniquely controlled by each of these transcription factors. Linking the formation and maintenance of each subcellular structure or subset of proteins within a cytoskeletal compartment to an overlapping but distinct transcription factor cohort may enable striated muscle to control cytoarchitectural function in an efficient and specific manner. Here we summarize the available evidence that connects transcription factors, those with established roles in striated muscle such as MEF2 and SRF, as well as other non-muscle transcription factors, to the regulation of a defined cytoskeletal structure. The notion that genes encoding proteins localized to the same subcellular compartment are coordinately transcriptionally regulated may prompt rationally designed approaches that target specific transcription factor pathways to correct structural defects in muscle disease. [Mh] Termos MeSH primário: Costâmeros/metabolismo Redes Reguladoras de Genes Sarcômeros/metabolismo [Mh] Termos MeSH secundário: Animais Costâmeros/genética Citoesqueleto/química Citoesqueleto/metabolismo Seres Humanos Músculo Esquelético/metabolismo Miócitos Cardíacos/metabolismo Sarcômeros/genética Fatores de Transcrição/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; REVIEW [Nm] Nome de substância: 0 (Transcription Factors) [Em] Mês de entrada: 1406 [Cu] Atualização por classe: 170220 [Lr] Data última revisão: 170220 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 131113 [St] Status: MEDLINE [do] DOI: 10.1007/s00018-013-1512-0

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