Disease relevance of Myoblasts

• We have tested the ability of a recombinant adenovirus, containing a 6.3 kilobase pair Becker-like dystrophin complementary DNA driven by the Rous sarcoma virus promoter to direct the expression of a 'minidystrophin' in infected 293 cells and C2 myoblasts, and in the mdx mouse, after intramuscular injection [1].
• The fate of injected myoblasts was assessed by coinfecting the cells with two retroviral vectors, one encoding hGH and the other encoding beta-galactosidase from Escherichia coli [2].
• Myositis autoantigen expression is also markedly increased in several cancers known to be associated with autoimmune myositis, but not in their related normal tissues, demonstrating that tumor cells and undifferentiated myoblasts are antigenically similar [3].
• At or near the time of prefusion, it becomes concentrated between adjacent aligned myoblasts and localized on membrane "blebs". H36 is present on both skeletal and cardiac cells but absent from a variety of cells that include fibroblasts, neuronal cells, and smooth muscle [4].
• Three distinct types of adhesive behavior are seen in short term (1 h) assays, typified by secondary murine fibroblasts, adherent only on fibronectin; secondary murine myoblasts, adherent on fibronectin, laminin, and the E8 fragment; and Rugli human glioblastoma cells, adherent on fibronectin, laminin, E8, and E1-4 [5].

Psychiatry related information on Myoblasts

• Nitric oxide synthase gene therapy for erectile dysfunction: comparison of plasmid, adenovirus, and adenovirus-transduced myoblast vectors [6].

High impact information on Myoblasts

• Expression of ubo is induced by Hedgehog (Hh) signaling in prospective slow muscle precursors, and its activity alone is sufficient to direct slow-twitch fiber-specific development by naive myoblasts [7].
• Accordingly, a dominant-negative ARF6 disrupts myoblast fusion in Drosophila embryos and in mammalian myoblasts in culture, mimicking the fusion defects caused by loss of Loner [8].
• IL-4 acts as a myoblast recruitment factor during mammalian muscle growth [9].
• Pavlath and coworkers demonstrate a novel role for Interleukin-4 (IL-4) in regulating the fusion of myoblasts with differentiated myotubes [10].
• Loner and ARF6, which also control the proper membrane localization of another small GTPase, Rac, are key components of a cellular apparatus required for myoblast fusion and muscle development [8].

Chemical compound and disease context of Myoblasts

• However, it is unclear how hypoxia or glucose deprivation in the ischemic microenvironment affects myoblast differentiation [11].
• One of the major laminin receptors of myoblasts is the alpha 7 beta 1 integrin, which was first described in human MeWo melanoma cells and Rugli glioblastoma cells [12].
• When aggregates of HM-1 embryonal carcinoma (EC) cells were exposed to 10(-6) M retinoic acid for 2 days and cultured in medium lacking retinoic acid, they differentiated to nerve cells, endoderm cells, and myoblasts [13].
• We evaluated myoblast implantation therapy in three subjects with Becker muscular dystrophy who received 60 million myoblasts in one tibialis anterior (TA) muscle 2 months after beginning cyclosporine immunosuppression (5 to 10 mg/kg) that continued for 1 year [14].
• Treatment of intact L6 myoblasts or C6 glioma cells with N-ethoxycarbonyl-2-ethoxy-1,2-dihydroquinoline (EEDQ) inactivated beta-adrenergic receptors on membranes prepared from these cells [15].

Biological context of Myoblasts

• Electrophoretic and autoradiographic analyses of the incorporation of 35S--methionine into newly synthesized proteins during myogenesis reveal that presumptive chicken myoblasts synthesize primarily one intermediate filament protein: vimentin [16].
• Transient transfection into L8 myoblasts has been used to study the rat alpha-actin gene promoter [17].
• A 6.7 kb mRNA encodes a transmembrane N-CAM isoform, present predominantly in mononucleate myoblasts, that shows sequence homology with chick brain N-CAM-140 and is down-regulated during myotube formation [18].
• The beta-tropomyosin gene in chicken contains two mutually exclusive exons (exons 6A and 6B) which are used by the splicing apparatus in myogenic cells, respectively, before (myoblast stage) and after (myotube stage) differentiation [19].
• Graft survival was not prolonged with composite grafts of unmodified myoblasts or Fas-expressing myoblasts [20].

Anatomical context of Myoblasts

• Protein synthetic patterns of DMSO-inhibited cells are almost indistinguishable from those of untreated myoblasts and distinct from differentiated myotubes [21].
• 5-azacytidine treatment of mouse C3H10T1/2 embryonic fibroblasts converts them to myoblasts at a frequency suggesting alteration of one or only a few closely linked regulatory loci [22].
• During differentiation of embryonic chick skeletal muscle in culture, elaboration of acetylcholine receptor (AChR) and acetylcholinesterase occurs shortly after myoblast fusion [23].
• IL-4 is expressed by a subset of muscle cells in fusing muscle cultures and requires the IL-4alpha receptor subunit on myoblasts to promote fusion and growth [9].
• We show here that DMAHP expression in myoblasts, muscle and myocardium is reduced by the DM mutation is cis, and the magnitude of this effect depends on the extent of CTG repeat expansion [24].

Associations of Myoblasts with chemical compounds

• Competitive interference of endogenous SET domain-dsPTPase interactions by forced expression of Sbf1 induced oncogenic transformation of NIH 3T3 fibroblasts and impaired the in vitro differentiation of C2 myoblast cells [25].
• Replicating chicken embryo myoblasts were treated with a monoclonal antibody, CSAT, which recognizes and blocks the function of the beta subunit of integrin [26].
• Myogenin is absent in undifferentiated cells, peaks, and then declines following a stimulus to differentiate, and is overexpressed in myoblasts selected with 5-bromodeoxyuridine for the overproduction of factors that regulate the decision to differentiate [27].
• Control of myoblast fusion by a guanine nucleotide exchange factor, loner, and its effector ARF6 [8].
• After a 1 hr pulse of dense amino acids and 3H-lysine, nucleosomes were isolated from chick myoblast organ cultures, and the histones were cross-linked to octamers [28].

Gene context of Myoblasts

• Over-expression of MLP in C2 myoblasts potentiates myogenic differentiation and reduces its sensitivity to TGF beta [29].
• The paired box transcription factor Pax7 was isolated by representational difference analysis as a gene specifically expressed in cultured satellite cell-derived myoblasts [30].
• Finally, the biological activity of Jagged was tested using a cell culture assay in which Jagged activates rat Notch1 expressed in myoblasts and prevents muscle cell differentiation [31].
• Replacement of the missing protein, dystrophin, using myoblast transfer in humans or viral/liposomal delivery in the mouse DMD model is inefficient and short-lived [32].
• We report here the identification and characterization of a new gene, sem-5 (sem, sex muscle abnormal), that acts both in vulval induction and in sex myoblast migration [33].

Analytical, diagnostic and therapeutic context of Myoblasts

• Gene targeting in normal somatic cells: inactivation of the interferon-gamma receptor in myoblasts [34].
• Islet allografts transplanted separately from FasL-expressing myoblasts into the contralateral kidney were rejected, as were similarly transplanted third-party thyroid allografts [20].
• Microinjection of p300/CBP antibodies into myoblasts blocks terminal differentiation, cell fusion, and transcriptional activity of myogenic bHLH proteins [35].
• These results indicate that myoblast transplantation leads to fiber formation when immunocompetent but fully histocompatible donors and recipients are used and that dystrophin incompatibility alone is not sufficient to induce an immunological rejection reaction [36].
• Immunofluorescence staining of chicken embryonic muscle cells in culture also indicates an accumulation of lamin A before the induction of muscle-specific proteins expression [37].

References