Relevant bibliographies by topics / Non muscle myosin II A

Academic literature on the topic 'Non muscle myosin II A'

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Published: 11 March 2023

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Journal articles on the topic "Non muscle myosin II A"

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Watanabe, T., H. Hosoya, and S. Yonemura. "1P205 Live imaging of Non-muscle myosin II in epithelial cells." Seibutsu Butsuri 45, supplement (2005): S83. http://dx.doi.org/10.2142/biophys.45.s83_1.

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Ubukawa, Kumi, Yong-Mei Guo, Masayuki Takahashi, Makoto Hirokawa, Yoshihiro Michishita, Miho Nara, Hiroyuki Tagawa, et al. "Enucleation of human erythroblasts involves non-muscle myosin IIB." Blood 119, no. 4 (January 26, 2012): 1036–44. http://dx.doi.org/10.1182/blood-2011-06-361907.

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Abstract Mammalian erythroblasts undergo enucleation, a process thought to be similar to cytokinesis. Although an assemblage of actin, non-muscle myosin II, and several other proteins is crucial for proper cytokinesis, the role of non-muscle myosin II in enucleation remains unclear. In this study, we investigated the effect of various cell-division inhibitors on cytokinesis and enucleation. For this purpose, we used human colony-forming unit-erythroid (CFU-E) and mature erythroblasts generated from purified CD34+ cells as target cells for cytokinesis and enucleation assay, respectively. Here we show that the inhibition of myosin by blebbistatin, an inhibitor of non-muscle myosin II ATPase, blocks both cell division and enucleation, which suggests that non-muscle myosin II plays an essential role not only in cytokinesis but also in enucleation. When the function of non-muscle myosin heavy chain (NMHC) IIA or IIB was inhibited by an exogenous expression of myosin rod fragment, myosin IIA or IIB, each rod fragment blocked the proliferation of CFU-E but only the rod fragment for IIB inhibited the enucleation of mature erythroblasts. These data indicate that NMHC IIB among the isoforms is involved in the enucleation of human erythroblasts.
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Dasbiswas, Kinjal, Shiqiong Hu, Frank Schnorrer, Samuel A. Safran, and Alexander D. Bershadsky. "Ordering of myosin II filaments driven by mechanical forces: experiments and theory." Philosophical Transactions of the Royal Society B: Biological Sciences 373, no. 1747 (April 9, 2018): 20170114. http://dx.doi.org/10.1098/rstb.2017.0114.

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Myosin II filaments form ordered superstructures in both cross-striated muscle and non-muscle cells. In cross-striated muscle, myosin II (thick) filaments, actin (thin) filaments and elastic titin filaments comprise the stereotypical contractile units of muscles called sarcomeres. Linear chains of sarcomeres, called myofibrils, are aligned laterally in registry to form cross-striated muscle cells. The experimentally observed dependence of the registered organization of myofibrils on extracellular matrix elasticity has been proposed to arise from the interactions of sarcomeric contractile elements (considered as force dipoles) through the matrix. Non-muscle cells form small bipolar filaments built of less than 30 myosin II molecules. These filaments are associated in registry forming superstructures (‘stacks’) orthogonal to actin filament bundles. Formation of myosin II filament stacks requires the myosin II ATPase activity and function of the actin filament crosslinking, polymerizing and depolymerizing proteins. We propose that the myosin II filaments embedded into elastic, intervening actin network (IVN) function as force dipoles that interact attractively through the IVN. This is in analogy with the theoretical picture developed for myofibrils where the elastic medium is now the actin cytoskeleton itself. Myosin stack formation in non-muscle cells provides a novel mechanism for the self-organization of the actin cytoskeleton at the level of the entire cell. This article is part of the theme issue ‘Self-organization in cell biology’.
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Wrighton, Katharine H. "Non-muscle myosin II in kidney morphogenesis." Nature Reviews Nephrology 13, no. 7 (May 30, 2017): 384. http://dx.doi.org/10.1038/nrneph.2017.77.

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Levinson, Howard, Blaine Mischen, Bruce Klitzman, Detlev Erdmann, and L. Scott Levin. "Non muscle myosin II regulates contractile phenotypes." Journal of the American College of Surgeons 205, no. 3 (September 2007): S60—S61. http://dx.doi.org/10.1016/j.jamcollsurg.2007.06.148.

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Maciver, Sutherland K. "Myosin II function in non-muscle cells." BioEssays 18, no. 3 (March 1996): 179–82. http://dx.doi.org/10.1002/bies.950180304.

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Porro, Chiara, Antonio Pennella, Maria Antonietta Panaro, and Teresa Trotta. "Functional Role of Non-Muscle Myosin II in Microglia: An Updated Review." International Journal of Molecular Sciences 22, no. 13 (June 22, 2021): 6687. http://dx.doi.org/10.3390/ijms22136687.

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Myosins are a remarkable superfamily of actin-based motor proteins that use the energy derived from ATP hydrolysis to translocate actin filaments and to produce force. Myosins are abundant in different types of tissues and involved in a large variety of cellular functions. Several classes of the myosin superfamily are expressed in the nervous system; among them, non-muscle myosin II (NM II) is expressed in both neurons and non-neuronal brain cells, such as astrocytes, oligodendrocytes, endothelial cells, and microglia. In the nervous system, NM II modulates a variety of functions, such as vesicle transport, phagocytosis, cell migration, cell adhesion and morphology, secretion, transcription, and cytokinesis, as well as playing key roles during brain development, inflammation, repair, and myelination functions. In this review, we will provide a brief overview of recent emerging roles of NM II in resting and activated microglia cells, the principal regulators of immune processes in the central nervous system (CNS) in both physiological and pathological conditions. When stimulated, microglial cells react and produce a number of mediators, such as pro-inflammatory cytokines, free radicals, and nitric oxide, that enhance inflammation and contribute to neurodegenerative diseases. Inhibition of NM II could be a new therapeutic target to treat or to prevent CNS diseases.
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Takubo, T., S. Wakui, K. Daigo, K. Kurokata, T. Ohashi, K. Katayama, and M. Hino. "Expression of non-muscle type myosin heavy polypeptide 9 (MYH9) in mammalian cells." European Journal of Histochemistry 47, no. 4 (June 26, 2009): 345. http://dx.doi.org/10.4081/845.

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Myosin is a functional protein associated with cellular movement, cell division, muscle contraction and other functions. Members of the myosin super-family are distinguished from the myosin heavy chains that play crucial roles in cellular processes. Although there are many studies of myosin heavy chains in this family, there are fewer on non-muscle myosin heavy chains than of muscle myosin heavy chains. Myosin is classified as type I (myosin I) or type II (myosin II). Myosin I, called unconventional myosin or mini-myosin, has one head, while myosin II, called conventional myosin, has two heads. We transfected myosin heavy polypeptide 9 (MYH9) into HeLa cells as a fusion protein with enhanced green fluorescent protein (EGFP) and analyzed the localization and distribution of MYH9 in parallel with those of actin and tubulin. The results indicate that MYH9 colocalizes with actin stress fibers. Since it has recently been shown by genetic analysis that autosomal dominant giant platelet syndromes are MYH9-related disorders, our development of transfected EGFP-MYH9 might be useful for predicting the associations between the function of actin polymerization, the MYH9 motor domain, and these disorders.
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Juanes-García, Alba, Clara Llorente-González, and Miguel Vicente-Manzanares. "Molecular control of non-muscle myosin II assembly." Oncotarget 7, no. 5 (January 18, 2016): 5092–93. http://dx.doi.org/10.18632/oncotarget.6936.

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Wan, Xiaohu. "Counting Molecules in Non-Muscle Myosin II Filaments." Biophysical Journal 108, no. 2 (January 2015): 322a. http://dx.doi.org/10.1016/j.bpj.2014.11.1750.

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Dissertations / Theses on the topic "Non muscle myosin II A"

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Frei, Ryan. "Regulatory Elements of Drosophila Non-Muscle Myosin II." Thesis, University of Oregon, 2013. http://hdl.handle.net/1794/12954.

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Non-muscle myosin II (NM-II) is present in every cell type and moves actin filaments to provide contraction within the cell. NM-II has a motor domain, a neck domain that binds two light chains, a long coiled-coil tail domain, and a carboxyl-terminal tailpiece. NM-II forms bipolar filaments by associating near the carboxyl-terminus of the tail. It has long been known that both the formation of bipolar filaments and enzymatic activity of the motor domain are regulated by phosphorylation of one of the neck-binding light chains, known as the regulatory light chain (RLC). This phosphorylation causes a large-scale conformational shift of both the motor domains and the tail domain. However, the mechanism of this regulation and the elements that mediate the autoinhibition remain unknown. We have taken a deletional approach to finding the elements necessary for autoinhibition and regulation of filament assembly. We have used salt- dependent pelleting assays, cell culture, and analytical ultracentrifugation to identify two small regions in the IQ motifs of the neck and the carboxyl-terminal tailpiece that are essential for autoinhibition. Another necessary element for autoinhibition is the fold the coiled coil of the tail back on itself by means of hinge domains. We used internal deletions, pelleting assays, and thermal stability assays to identify and characterize the flexible hinge domains within the coiled-coil tail of NM-II. These hinges consist of low-stability regions of coiled coil, and can be stiffened by introducing mutations that cause the sequence to mimic a more ideal coiled coil. By defining these essential elements of autoinhibition, this work paves the way for a mechanistic understanding of the complex regulation of NM-II in the cell. This dissertation contains unpublished co-authored material.
2015-07-11
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Swailes, Nathan. "Actin and non-muscle myosin II in pre-fusion myoblasts." Thesis, University of Leeds, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.416842.

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Picariello, Hannah Stubbs. "The Diverse Roles of Non-muscle Myosin II in Tumorigenesis." Case Western Reserve University School of Graduate Studies / OhioLINK, 2019. http://rave.ohiolink.edu/etdc/view?acc_num=case1562680454131993.

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Khan, Protiti. "The Role of Myosin Light Chain Kinase and Non Muscle Myosin II In Ras Signaling to ERK." Scholarly Repository, 2008. http://scholarlyrepository.miami.edu/oa_theses/177.

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We have previously reported that non-muscle myosin II (NMMII) and myosin light chain kinase (MLCK) are required for oncogenic Ras signaling to ERK in Ki-Ras transformed rat fibroblsasts (Helfman and Pawlak, J. Cell Biochem. 95(5), 1069-80, 2005). Here I examine if MLCK plays a role in ERK signaling in various tumor derived human epithelial cell lines. I also determined whether genetic inhibition of NMMII isoforms IIA and IIB, or MLCK also inhibits ERK activation in the MCF 10A human breast epithelial cell line expressing oncogenic H-Ras. Inhibition of MLCK by pharmacological inhibitors such as ML-7 and ML-9 was used to determine the role of MLCK in ERK signaling in an array of H/K-Ras transformed and tumor derived cell lines: T-24 bladder carcinoma, HCT 116 colon carcinoma, and MCF 10A Ras breast cancer cells. Genetic inhibition was carried out using specific siRNA targeted towards MLCK and NMMIIA or IIB. The knock down of NMM IIA and IIB did not inhibit active ERK, which suggested either a redundant function of NMM IIC or an alternate substrate for MLCK. Inhibition of MLCK by ML-7/ML-9 reduced activated ERK in all H/K-Ras transformed, or human tumor derived cell lines we tested. The possible mechanism of how MLCK could play a role in ERK signaling was tested by co-immunoprecipitation (co-IP) of MAPK scaffolding proteins with MLCK. That the ERK scaffold KSR1 regulates ERK signaling in MCF 10A Ras, was demonstrated through inhibition of KSR1 with siRNA. Moreover, KSR was shown to interact with MLCK because it was found to co-precipitate with MLCK.
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Sankara, Narayana Gautham Hari Narayana. "Role of non-muscle myosin-II isoforms in adherens junction biogenesis and collective migration." Thesis, Université de Paris (2019-....), 2019. https://theses.md.univ-paris-diderot.fr/SANKARA_NARAYANA_Gautham_Hari_Naryana_va.pdf.

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La formation et le remodelage des jonctions intercellulaires sont essentiels pour de nombreux processus biologiques tels que la compaction et la morphogenèse de l’embryon, la formation et la cicatrisation des tissus, le maintien de l’homéostasie tissulaire. Il est maintenant bien décrit que la myosine II non musculaire (NMII) agit comme un générateur de force et un support mécanique pour les jonctions adherens (E-cadhérine-dépendantes) lors de la migration collective et de la morphogenèse. Cependant, la contribution de NMII pendant les premières étapes de la formation de jonctions adherens reste mal connue, probablement en raison de la difficulté technique à capter un tel évènement transitoire mais complexe. Dans ce travail, nous avons étudié le rôle des isoformes non musculaires de la myosine II (NMIIA et NMIIB) au cours de la biogenèse des jonctions adherens dans les cellules MDCK, en utilisant une approche réductionniste in vitro. Cette approche, basée sur l’utilisation de substrats de culture micropatternés, chimiquement activables, mais permit un contrôle spatio-temporel de la formation des contacts intercellulaires. Mes travaux montrent que les cellules forment des contacts irréversibles base de E-cadhérine. L’élongation de ces contacts est accompagnée de la repolarisation du cytosquelette d’actine et de l’axe noyau-centrosome. En utilisant des shRNA spécifiques aux isoformes NMIIA et IIB, j’ai montré que ces deux isoformes ont contributions distinctes la formation et la dynamique des jonctions. NMIIA et NMIIB régulent différemment la biogenèse des jonctions par association avec des réseaux d'actine distincts. L'analyse de la dynamique des jonctions, de l'organisation de l'actine et des forces mécaniques a révélé que NMIIA fournit la force de traction mécanique nécessaire au renforcement et la maintenance des jonctions cellulaires. Le NMIIB est impliquée dans le clustering de la E-cadhérine, le maintien d'une couche d'actine branchée reliant les complexes de cadhérine et les fibres d'actine péri-jonctionnelles conduisant la création d'un stress mécanique anisotrope. Ces données révèlent des fonctions complémentaires imprévues de NMIIA et NMIIB dans la biogenèse et l'intégrité des jonctions adherens
Adherens junction formation and remodeling is essential for many biological processes like embryo compaction, tissue morphogenesis and wound healing. It is now well described that non-muscle myosin II (NMII) acts as a mechanical support and force-generator for E-cadherin junctions during collective migration and morphogenesis. However, the contribution of NMII during early steps of junction formation remains obscure, probably because of the technical difficulty to catch such a transient event. In this work, we investigate the role of non-muscle myosin II isoforms (NMIIA and NMIIB) during adherens junction biogenesis in MDCK cells, using an in vitro reductionist approach. This system, based on chemically switchable micropatterns allows a spatio-temporal control of adherens junction formation. Our observations on MDCK cells show that the cells form irreversible E-cadherin based contacts, junction elongation is accompanied by the repolarization of actin cytoskeleton and nucleus-centrosome axis. Using isoform-specific ShRNA for NMIIA and IIB, we show that they have distinct contributions to junction formation and dynamics. NMIIA and NMIIB differentially regulate biogenesis of AJ through association with distinct actin networks. Analysis of junction dynamics, actin organization, and mechanical forces of control and knockdown cells for myosins revealed that NMIIA provides the mechanical tugging force necessary for cell-cell junction reinforcement and maintenance. NMIIB is involved in E-cadherin clustering, maintenance of a branched actin layer connecting E-cadherin complexes and perijunctional actin fibres leading to the building-up of anisotropic stress. These data reveal unanticipated complementary functions of NMIIA and NMIIB in the biogenesis and integrity of AJ
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Ricketson, Derek Lee. "Drosophila non-muscle myosin II bipolar filament formation : importance of charged residues and specific domains for self-assembly /." Connect to title online (Scholars' Bank) Connect to title online (ProQuest), 2009. http://hdl.handle.net/1794/10285.

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Ding, Siyu Serena. "Elucidating the role of non-muscle myosin II in Caenorhabditis elegans stem-like seam cell divisions." Thesis, University of Oxford, 2015. https://ora.ox.ac.uk/objects/uuid:5b5cb805-327a-4a58-b3db-3787f5264efc.

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Caenorhabiditis elegans seam cells (SC) are multipotent neuroectodermal cells that undergo both symmetrical and asymmetrical divisions throughout larval development, thus providing a valuable model system to gain mechanistic insights into the regulation of asymmetric divisions and the switch between the symmetric and asymmetric modes of division. Reiterative SC asymmetric division typically produces a differentiative anterior daughter that moves out of the seam line and joins the hyp7 syncytium and a proliferative posterior daughter that retains seam fate and carries on dividing. Non-muscle myosin II (NMY II) has emerged as a key regulator in the asymmetric divisions of the C. elegans zygote, the C. elegans Q neuroblast, and the Drosophila neuroblast systems. In addition to being an essential player in cytokinesis, nmy-2's roles in cell adhesion and migration processes further underline its potential as a regulator of seam cell asymmetric divisions. In this thesis work, I investigated the role of NMY-2 in C. elegans seam cell divisions. I found that nmy-2 is expressed in the seam and its protein localization is dynamic during SC divisions. Post-embryonic nmy-2 knockdown using a combination of temperature sensitive mutants and RNA interference robustly reduces terminal SC number. This reduction is due to progressive SC loss after each asymmetric division as a consequence of aberrant cell fate determination. I identified three classes of cell fate transformation phenotypes following nmy-2 knockdown, and sought to dissect the cell molecular basis of these phenotypes using a dual-color fate reporter strain. Although prevalent in nmy-2 knockdown, cytokinesis defects are not the only cause of SC losses. nmy-2 also does not appear to regulate SC divisions by affecting spindle positioning. In summary, nmy-2 function is crucial to ensure the proper division and fate specification in post-embryonic SC development.
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Ricketson, Derek Lee 1980. "Drosophila non-muscle myosin II bipolar filament formation: Importance of charged residues and specific domains for self-assembly." Thesis, University of Oregon, 2009. http://hdl.handle.net/1794/10285.

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xii, 107 p. : ill. (some col.) A print copy of this thesis is available through the UO Libraries. Search the library catalog for the location and call number.
Non-muscle myosin II generates contractile forces for processes such as cytokinesis, motility, and polarity. Contractility requires assembly of myosin molecules into bipolar mini-filaments through electrostatic interactions between coiled-coil tail domains of the heavy chains. Analyses of myosin II from various organisms have revealed "assembly domains" within the C-terminal portion of the tail domain that mediate filament formation. However, it has been unclear precisely how assembly domains interact with one another, or otherwise contribute to tail-tail interactions, to form the bipolar mini-filament structure. To understand tail domain interactions, we first identified a 90-residue region (1849-1940) of the Drosophila non-muscle myosin II tail domain that was necessary and sufficient for filament formation, using salt-dependent solubility and a novel fluorescence energy transfer assay. We identified residues within this "assembly domain" that were critical for filament assembly by analyzing the effect of point mutations. We found that single point mutations in specific positively charged regions completely disrupt filament assembly. Surprisingly, none of the negatively charged regions within the assembly domain are required for assembly. Most of the mutations in positively charged residues that disrupted filament assembly clustered within a 15-residue segment (1880-1894) that appears to form a critical interaction surface. Using this information, along with known geometrical constraints and electrostatic calculations, we constructed a structural model of the bipolar mini-filament. This model features one favored anti-parallel tail overlap and multiple slightly less stable alternative overlaps. The ability of the positive segment to interact with multiple negative regions explains the lack of required negatively charged residues in the assembly domain. To our knowledge, this structural model of the non- muscle myosin II bipolar filament is consistent with all physical observations and provides a framework for understanding the detailed mechanism by which this fundamental cellular structure is generated. This dissertation contains previously published and unpublished co-authored material.
Committee in charge: Tom Stevens, Chairperson, Chemistry; Kenneth Prehoda, Advisor, Chemistry; J. Andrew Berglund, Member, Chemistry; Christopher Doe, Member, Biology; Karen Guillemin, Outside Member, Biology
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Sarkar, Saheli. "Combined Experimental and Mathematical Approach for Development of a Microfabrication-Based Model to Investigate Cell-Cell Interaction during Migration." Case Western Reserve University School of Graduate Studies / OhioLINK, 2011. http://rave.ohiolink.edu/etdc/view?acc_num=case1301420667.

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Messineo, Stefania. "Development of a gene targeting strategy (Recombinase-Mediated CAssette Exchange) to generate cellular models of MYH9-related disease." Doctoral thesis, Università degli studi di Trieste, 2011. http://hdl.handle.net/10077/4603.

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2009/2010
La malattia MYH9-correlata (MYH9-RD) è una malattia autosomica dominante, caratterizzata da trombocitopenia congenita con piastrine di grandi dimensioni, aggregati nei neutrofili, sordità progressiva, cataratta e nefropatia. La MYH9-RD è causata da mutazioni nel gene MYH9 che codifica per la catena pesante della miosina non muscolare di classe II (miosina-9). I meccanismi patogenetici che causano questa malattia non sono ancora stati chiaramente identificati e il loro studio è complicato dalla mancanza di adeguati modelli cellulari e animali. Lo scopo di questo progetto è stato di generare un modello in vitro per studiare la funzione della miosina-9 e il ruolo di due mutazioni che incorrono nel gene MYH9: la R702C e la R1933X, che correlano rispettivamente con un fenotipo grave e lieve. Per questo motivo abbiamo deciso di manipolare le cellule staminali embrionali murine (ES), che sono pluripotenti e possono essere differenziate in diversi linee cellulari, compresa la linea megacariocitica. Per ingegnerizzare queste cellule ad alta efficienza abbiamo messo a punto una strategia nota come "scambio di cassette mediato da ricombinasi" (RMCE). Dopo l'integrazione di una cassetta fiancheggiata da siti FRT (sequenze di riconoscimento per l'enzima flippasi), il sistema ci ha permesso di scambiare diverse sequenze di DNA in presenza dell'enzima flippasi. Quindi il primo esone codificante del gene Myh9 è stato distrutto dall'inserimento, mediante ricombinazione omologa, di una cassetta fiancheggiata da due siti FRT contenente il gene reporter Beta-galattosidasi. Successivamente abbiamo scambiato questa cassetta con altre tre contenenti il cDNA Myh9 murino wild-type e i due mutati, generando i cloni ES che esprimono queste sequenze esogene sotto il controllo del promotore Myh9 endogeno. La caratterizzazione a livello dell'RNA e delle proteine di questi cloni ci ha portato a stabilire che gli alleli mutati e wild-type sono espressi allo stesso livello, suggerendo che le manipolazioni genetiche non interferiscono con i corretti meccanismi fisiologici di trascrizione e traduzione del gene Myh9. Tuttavia, mediante Western Blot abbiamo mostrato che la proteina miosina-9 è espressa a livello inferiore nei cloni mutati rispetto ai wild-type. Le analisi di immunofluorescenza per indagare la presenza di aggregati di miosina-9, che sono sempre presenti nei neutrofili di pazienti, non hanno rilevato alcuna variazione nella distribuzione della miosina-9, fatta eccezione per un segnale di intensità minore. Questi risultati indicano che, nonostante l'espressione dell'allele ingegnerizzato sia normale, la proteina mutata sembra essere degradata, almeno nelle cellule ES murine, determinando un effetto di aploinsufficienza delle mutazioni R702C e R1933X. Per accertare la loro pluripotenza, abbiamo differenziato dei cloni ES in corpi embrioidi e cardiomiociti, senza rivelare alcuna differenza tra i cloni mutanti e i wild-type. Dal momento che una caratteristica congenita dei pazienti MYH9-RD è la macrotrombocitopenia, abbiamo sviluppato un protocollo per differenziare i cloni mutati ES in megacariociti per indagare come le mutazioni in MYH9 portino a una impropria produzione di piastrine. In conclusione, per studiare la MYH9-RD abbiamo sviluppato una strategia che ci ha permesso di esprimere sequenze di interesse in cellule ES di topo sotto il controllo del promotore Myh9 endogeno. La differenziazione in vitro di queste cellule ci permetterà di studiare l'effetto delle mutazioni nel corso della megacariocitopoiesi. Inoltre, poiché le cellule ES possono anche essere usate per generare modelli animali, questa strategia ci permetterà di testare diverse ipotesi patogenetiche in vitro, prima di passare a studi in vivo.
XXIII Ciclo
1982
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Books on the topic "Non muscle myosin II A"

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Turner, Neil, and Bertrand Knebelmann. MYH9 and renal disease. Edited by Neil Turner. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780199592548.003.0342_update_001.

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MYH9 encodes one of three heavy chain isoforms for the non-muscle myosin II (NM II) molecule. NM II is involved in cell structure and shape and motility. Myosin II is very widely expressed but MYH9 is highly expressed in podocytes. MYH9 diseases are characterized by various combinations of autosomal dominant progressive, proteinuric renal disease, giant platelets with low platelet counts, progressive sensorineural hearing impairment, granulocyte inclusions, and in some patients also cataracts. Although the eponyms Epstein and Fechtner have been given to MYH9 renal syndromes, there is a spectrum of manifestations of MYH9 diseases that do not correlate perfectly with genotype. They are best described as MYH9-associated renal disease. The occurrence of progressive deafness and renal failure led to this condition being considered an Alport syndrome variant in the past, but phenotype as well as molecular genetics clearly separate the disorders.
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Barker, Alan R., and Neil Armstrong. Pulmonary oxygen uptake kinetics. Edited by Neil Armstrong and Willem van Mechelen. Oxford University Press, 2017. http://dx.doi.org/10.1093/med/9780198757672.003.0013.

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The pulmonary oxygen uptake (pV̇O2) kinetic response to exercise provides valuable non-invasive insight into the control of oxidative phosphorylation and determinants of exercise tolerance in children and adolescents. Few methodologically robust studies have investigated pV̇O2 kinetics in children and adolescents, but age- and sex-related differences have been identified. There is a clear age-related slowing of phase II pV̇O2 kinetics during heavy and very heavy exercise, with a trend showing during moderate intensity exercise. During heavy and very heavy exercise the oxygen cost is higher for phase II and the pV̇O2 component is truncated in children. Sex-related differences occur during heavy, but not moderate, intensity exercise, with boys having faster phase II pV̇O2 kinetics and a smaller pV̇O2 slow component compared to girls. The mechanisms underlying these differences are likely related to changes in phosphate feedback controllers of oxidative phosphorylation, muscle oxygen delivery, and/or muscle fibre recruitment strategies.
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Book chapters on the topic "Non muscle myosin II A"

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Betapudi, Venkaiah. "Non-muscle Myosin II Motor Proteins in Human Health and Diseases." In Genome Analysis and Human Health, 79–107. Singapore: Springer Singapore, 2017. http://dx.doi.org/10.1007/978-981-10-4298-0_5.

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Goonewardene, Sanchia S., Raj Persad, Hanif Motiwala, and David Albala. "NMIBC and Intravesical Chemotherapy—HIVEC I and HIVEC II." In Management of Non-Muscle Invasive Bladder Cancer, 223–24. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-28646-0_43.

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Bandman, E., D. L. Bourke, and M. Wick. "Regulation of Myosin Heavy Chain Expression during Development, Maturation, and Regeneration in Avian Muscles: The Role of Myogenic and Non-Myogenic Factors." In The Dynamic State of Muscle Fibers, edited by Dirk Pette, 127–38. Berlin, Boston: De Gruyter, 1990. http://dx.doi.org/10.1515/9783110884784-013.

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Zolty, Ronald. "The Role of Neurohormonal Systems, Inflammatory Mediators and Oxydative Stress in Cardiomyopathy." In Cardiomyopathy - Disease of the Heart Muscle. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.97345.

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Cardiomyopathy and more specifically the dilated cardiomyopathy, regardless of severity, is associated with activation of neuro-hormonal, cytokine and oxidative stress signaling pathways that alter the structure and function of cardiac myocytes and non-myocyte cells. These cellular alterations culminate in the morphological changes in cardiac structure termed as cardiac remodeling, a maladaptive process that contributes to further left ventricular dysfunction and heart failure development. This pathological progression is mainly driven by circulating mediators, in particular angiotensin II and norepinephrine. Natriuretic peptides, endothelin-1, vasopressin play also an important role in the progression of the cardiomyopathy. Cardiac inflammation, mediated by cytokines such as tumor necrosis factor-α (TNF-α), interleukins 1 (IL-1) and 6 (IL-6), as well as the oxidative stress were also shown to worsen the cardiac function. Although these pathways have been described separately, they are critically inter-dependent in the response to the development and progression of the dilated cardiomyopathy. This chapter reviews the cellular basis for cardiac remodeling and the mechanisms that contribute to these cellular abnormalities and, more broadly, to the pathophysiology of dilated cardiomyopathy, its progression and its potential treatments.
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Lee-Gannon, Theo, Hannah Lehrenbaum, Rahul Sheth, and Pradeep P.A. Mammen. "Clinical Management of DMD-Associated Cardiomyopathy." In Cardiomyopathy - Disease of the Heart Muscle. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.98919.

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Over the past decade, cardiomyopathy has become the leading cause of mortality among patients with Duchenne muscular dystrophy (DMD). The majority of DMD patients over the age of 18 experience some degree of cardiac involvement. The primary cardiac manifestations of DMD include progressive left ventricular (LV) wall stress leading to LV dilatation and wall thinning, and the development of cardiac fibrosis, all of which culminate in decreased LV contractility and reduced cardiac output. Mortality in these patients is predominantly related to pump failure and fatal arrhythmias leading to sudden cardiac death. While basic guidelines for the management of cardiomyopathy in DMD patients exist, these recommendations are by no means comprehensive, and this chapter aims to provide further insight into appropriate clinical diagnosis and management of DMD-associated cardiomyopathy. Notably, earlier and more frequent cardiac assessment and care can allow for better outcomes for these patients. Pharmacological treatments typically include an angiotensin-converting enzyme inhibitor or angiotensin II receptor blocker, beta-adrenergic receptor blockers, mineralocorticoid receptor antagonists, and corticosteroids. Non-pharmacological therapies include automated implantable cardioverter defibrillators and left ventricular assist devices, as well as in rare cases cardiac transplantation. Additionally, many emerging therapies show great promise for improving standards of care. These novel therapies, based primarily on applied gene therapy and genome editing, have great potential to significantly alter the DMD care landscape in the near future.
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Partanen, Juhani, Urho Sompa, and Miguel Muñoz-Ruiz. "Recording of Proprioceptive Muscle Reflexes in the Lower Extremity." In Proprioception [Working Title]. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.95575.

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Electromyography (EMG) is routinely used in diagnostics of root syndromes in the lower extremity. By studying signs of axonal damage of different root levels in the corresponding myotomes of the lower extremity and back muscles with needle EMG reveals, which of the motor roots are injured in patients with suspected root compression. But by EMG study only injuries of the anterior motor roots are diagnosed. Routine electroneuromyography does not disclose specific injury of the afferent sensory posterior roots. However, the integrity of some the posterior roots is readily studied with myotatic reflexes. We have routinely measured a proprioceptive reflex, the H-reflex of the soleus muscle with stimulation of the posterior tibial nerve, and found it to be useful in the diagnostics of the S1 root syndrome. It seems to be possible to record H-reflex of the peroneus longus muscle at the L5 level. We discuss the serious problems with volume conduction, when trials to measure proprioceptive reflexes of the L4 and L5 levels are performed. It may also be useful to record the medium latency reflexes in the area of the posterior tibial nerve, which seems to have a different reflex arch (II-afferents – β-efferents) from H-reflex (Ia afferents – α efferents). These measurements are non-invasive and not time consuming, and we hope to be able to add them for the routine ENMG diagnostics, when appropriate.
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Conference papers on the topic "Non muscle myosin II A"

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Zhang, Wenwu, Yidi Wu, and Susan J. Gunst. "The Small GTPase RhoA Regulates Non-Muscle Myosin II Activity During Contractile Stimulation In Canine Tracheal Smooth Muscle." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a4131.

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Li, Xiaona, Meiwen An, Li Wang, and Wenzhou Wu. "The Experimental Study on the Functions of Non-Muscle Myosin II in Dividing Mammalian Cells." In 2009 3rd International Conference on Bioinformatics and Biomedical Engineering (iCBBE 2009). IEEE, 2009. http://dx.doi.org/10.1109/icbbe.2009.5163614.

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Hsu, Hui-Ju, Andrea Locke, Susan Q. Vanderzyl, and Roland Kaunas. "Stretch-Induced Stress Fiber Remodeling and MAPK Activations Depend on Mechanical Strain Rate." In ASME 2011 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2011. http://dx.doi.org/10.1115/sbc2011-53464.

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Actin stress fibers (SFs), bundles of actin filaments crosslinked by α-actinin and myosin II in non-muscle cells, are mechanosensitive structural elements that respond to applied stress and strain to regulate cell morphology, signal transduction and cell function. Results from various studies indicate that myosin-generated contraction extends SFs beyond their unloaded lengths and cells maintain fiber strain at an optimal level that depends on actomyosin activity (Lu et al., 2008). Stretching the matrix upon which cells adhere perturbs the cell-matrix traction forces and cells respond by actively re-establishing the preexisting level of force (Brown et al., 1998; Gavara et al., 2008). We have developed a sarcomeric model of SF networks (Kaunas et al., 2011) to predict the effects of stretch on SF reorganization depending on the rates of matrix stretching, SF turnover, and SF stress relaxation.
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Siegler, Jessica, Biji Mathew, Ting Wang, Tong Zhou, Michael S. Wade, Ralph Weichselbaum, Liliana Moreno-Vinasco, and Joe G. Garcia. "Non-Muscle Myosin Light Chain Kinase Participates In Tumor Metastasis In Mice." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a5084.

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Aprodu, Iuliana, Alberto Redaelli, Franco Maria Montevecchi, and Monica Soncini. "Mechanical Characterization of Myosin II, Actin and Their Complexes by Molecular Mechanics Approach." In ASME 8th Biennial Conference on Engineering Systems Design and Analysis. ASMEDC, 2006. http://dx.doi.org/10.1115/esda2006-95670.

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The knowledge of the mechanical properties of myosin and actin is of a crucial importance in order to better understand the molecular mechanism of sliding force generation in muscle contraction. The aim of our work was to realize a mechanical characterization of myosin II and actin monomer using the molecular mechanics approach, by assessing the elastic properties of the two proteins, and by establishing the interaction forces between the two monomers of the actomyosin complex, and between myosin’s scissure and adenine nucleotides (ATP and ADP). A restraining method was used in order to modify the axial length of the proteins or the intermolecular distances. The interaction force and the stiffness were calculated as first and second order derivative of the potential energy with respect to the applied elongation and intermolecular distance respectively. According to our results, the values of elastic modulus of myosin motor domain and actin are 0.48 GPa, and 0.13 GPa respectively, and myosin-ATP complex is characterized by an attraction force of 130 pN which is twofold greater than the interaction force between myosin and ADP. As for the actomyosin complex, the interaction force has a maximum value of 180 pN. The results of our simulations comply with theoretical and experimental remarks about mechanical properties of myosin II, actin, and their complex.
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Siegler, Jessica, Biji Mathew, Frances Lennon, Lynnette Gerhold, Chin-tu Chen, Patrick La Riviere, Christian Wietholt, et al. "Non-Muscle Myosin Light Chain Kinase Promotes The Development Of Non-Small-Cell Lung Cancer." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a2062.

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Alanazi, Samar M., Rosalin Mishra, Long Yuan, Hima Patel, and Joan Garrett. "Abstract 4205: The role of non-muscle myosin IIA in HER2+ breast cancers." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-4205.

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Martin, Ryan D., Jayashree Banerjee, Meenakshi Lakshminarayanan, Yuxia Cao, and Maria I. Ramirez. "T1± Interacts With Myh9, A Non-Muscle Myosin, In Type I Lung Epithelial Cells." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a6310.

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Bowers, Robert, Danyelle M. Townsend, Yefim Manevich, and Kenneth D. Tew. "Abstract 5136: Sulfiredoxin promotes cell migration through direct interaction with non muscle myosin IIa." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-5136.

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Moreno-Vinasco, Liliana, Syed R. Zaidi, Saad Sammani, Tamara Mirzapoiazova, Roberto F. Machado, and Joe G. N. Garcia. "Role Of Non-muscle Myosin Light Chain Kinase In Hypoxia-induced Murine Pulmonary Hypertension." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a5245.

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Reports on the topic "Non muscle myosin II A"

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Kanner, Joseph, Edwin Frankel, Stella Harel, and Bruce German. Grapes, Wines and By-products as Potential Sources of Antioxidants. United States Department of Agriculture, January 1995. http://dx.doi.org/10.32747/1995.7568767.bard.

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Several grape varieties and red wines were found to contain large concentration of phenolic compounds which work as antioxidant in-vitro and in-vivo. Wastes from wine production contain antioxidants in large amounts, between 2-6% on dry material basis. Red wines but also white wines were found to prevent lipid peroxidation of turkey muscle tissues stored at 5oC. The antioxidant reaction of flavonoids found in red wines against lipid peroxidation were found to depend on the structure of the molecule. Red wine flavonoids containing an orthodihydroxy structure around the B ring were found highly active against LDL and membrane lipid peroxidation. The antioxidant activity of red wine polyphenols were also found to be dependent on the catalyzer used. In the presence of H2O2-activated myoglobin, the inhibition efficiency was malvidin 3-glucoside>catechin>malvidin>resveratol. However, in the presence of an iron redox cycle catalyzer, the order of effectiveness was resveratol>malvidin 3-glucoside = malvidin>catechin. Differences in protein binding were found to affect antioxidant activity in inhibiting LDL oxidation. A model protein such as BSA, was investigated on the antioxidant activity of phenolic compounds, grape extracts, and red wines in a lecithin-liposome model system. Ferulic acid followed by malvidin and rutin were the most efficient in inhibiting both lipid and protein oxidation. Catechin, a flavonal found in red-wines in relatively high concentration was found to inhibit myoglobin catalyzed linoleate membrane lipid peroxidation at a relatively very low concentration. This effect was studied by the determination of the by-products generated from linoleate during oxidation. The study showed that hydroperoxides are catalytically broken down, not to an alcohol but most probably to a non-radical adduct. The ability of wine-phenolics to reduce iron and from complexes with metals were also demonstrated. Low concentration of wine phenolics were found to inhibit lipoxygenase type II activity. An attempt to understand the bioavailability in humans of antocyanins from red wine showed that two antocyanins from red wine were found unchanged in human urine. Other antocyanins seems to undergo molecular modification. In hypercholesterolemic hamsters, aortic lipid deposition was significantly less in animals fed diets supplemented with either catechin or vitamin E. The rate of LDL accumulation in the carotid arteries was also significantly lower in the catechin and vitamin E animal groups. These results suggested a novel mechanism by which wine phenolics are associated with decreased risk of coronary heart diseases. This study proves in part our hypothesis that the "French Paradox" could be explained by the action of the antioxidant effects of phenolic compounds found at high concentration in red wines. The results of this study argue that it is in the interest of public health to increase the consumption of dietary plant falvonoids. Our results and these from others, show that the consumption of red wine or plant derived polyphenolics can change the antioxidant tone of animal and human plasma and its isolated components towards oxidative reactions. However, we need more research to better understand bioavailability and the mechanism of how polyphenolics affect health and disease.
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