Lamin and Lamin B receptor knockout
Ontology highlight
ABSTRACT:
ORGANISM(S): Mus musculus
PROVIDER: GSE37076 | GEO | 2013/01/28
SECONDARY ACCESSION(S): PRJNA158295
REPOSITORIES: GEO
Similar Datasets
Project description:influence of lamin B rereceptor knockout and lamin A/C knockout on gene expression in cultured myoblast cells and in striated muscle tissue knockout samples are obtained by mating of heterozygous animals. Homozygous KO and wt animals of one litter are compared. Two boilogical replicates of KO samples are processed in parallel. wt samples are used as controls. One wt sample is processed per KO litter. Where appropriate two wt samples are used as biological replicates.
2013-01-28 | E-GEOD-37076 | biostudies-arrayexpress
Project description:Study muscle regeneration in Emerin and Lamin AC KO mice. Gastrocnemius muscles were injected with cardiotoxin. Muscles were isolated at different time points. Keywords: Time-Series The specific aim is to generate staged muscle degeneration/regeneration of Emerin deficient and Lamin A/C deficient mice. Muscles will then be express profiled using Affymetrix arrays.
2006-07-12 | E-GEOD-5304 | biostudies-arrayexpress
Project description:Transcriptome analysis by RNA-seq of tibialis anterior muscle from control and Smyd1 myocyte-specific conditional knockout mice at 6 weeks of age. Smyd1 is a methyltransferase specifically expressed in striated muscle and CD8+ T cells. Smyd1 deficiency resulted in centronuclear myopathy primarily affecting fast-twitch muscle fibers. These results provide insight into how loss of Smyd1 altered transcriptional programs resulting in centronuclear myopathy. 6 animals per group (control and Smyd1 conditional knockout)
2016-04-05 | E-GEOD-71679 | biostudies-arrayexpress
Project description:DOCK3 is a member of the DOCK family of guanine nucleotide exchange factors that function to regulate cell migration, fusion, and overall viability. Previously, we identified a miR-486/Dock3 signaling cascade that was dysregulated in dystrophin-deficient muscle which resulted in the overexpression of DOCK3, however not much else is known about the role of DOCK3 in muscle. In this work, we characterize the functional role of DOCK3 in normal and dystrophic striated muscle. By utilizing the Dock3 global knockout (Dock3 KO) mice, we found reducing Dock3 gene via haploinsufficiency in DMD mice improved muscle histology, however full loss of Dock3 worsened overall muscle function on a dystrophin-deficient background. Consistent with this, Dock3 KO mice have impaired muscle architecture, myoblast fusion defects, and cardiac functional deficits. Moreover, transcriptomic analyses of Dock3 knockout muscles reveal a decrease in factors known for myoblast fusion, suggesting a possible mechanism of action. These studies identify DOCK3 as a novel modulator of muscle fusion and muscle health, and may yield additional therapeutic targets for treating dystrophic muscle symptoms.
2020-12-24 | GSE141621 | GEO
Project description:Gene expression analysis of Lamin B receptor deficient hematopoietic cells
2011-12-21 | E-TABM-1134 | biostudies-arrayexpress
Project description:Transcriptome analysis by RNA-seq of tibialis anterior muscle from control and Smyd1 myocyte-specific conditional knockout mice at 6 weeks of age. Smyd1 is a methyltransferase specifically expressed in striated muscle and CD8+ T cells. Smyd1 deficiency resulted in centronuclear myopathy primarily affecting fast-twitch muscle fibers. These results provide insight into how loss of Smyd1 altered transcriptional programs resulting in centronuclear myopathy.
2016-04-05 | GSE71679 | GEO
Project description:HSPB3 is a member of the HSPB family that is absent in cycling cells. HSPB3 expression is induced by the myogenic specific transcription factor MyoD in muscle cells, where HSPB3 localizes to the nucleus. Yet, whether HSPB3 participates to muscle cell differentiation is unknown. One of the early events of cell differentiation consists in the switch between the lamin B receptor (LBR) and the lamin A/C (LMNA) tethers, which modulates chromatin remodeling and transcription. Here, we identified LBR as a specialized substrate regulated by HSPB3. HSPB3 affected the expression and nuclear distribution of LBR mimicking the changes that occur during differentiation. HSPB3 upregulation promoted the differentiation of two human muscle cell types: LHCNM2 cells, derived from satellite cells and fusion-negative rhabdomyosarcoma cells, which fail to commit to terminal differentiation. Conversely, HSPB3 depletion stabilized the LBR tether and affected the myogenic transcriptional program. Four mutations in the HSPB3 gene are linked to distal hereditary motor neuropathy and congenital myopathy with unknown mechanisms. We focused on R116P-HSPB3, which was discovered in a myopathy patient with chromatin alterations and muscle fiber disorganization. Upon overexpression in cells R116-HSPB3 formed nuclear aggregates that immobilized LBR-GFP. In LHCNM2 cells R116-HSPB3 deregulated the transcriptional program required for cytoskeleton and ECM remodeling, while activating the unfolded protein response. We propose that HSPB3 is a highly specialized chaperone that participates to muscle cell differentiation by targeting LBR. Our findings pave the way for a better understanding of HSPB3 implication in the physiology and pathology of the neuromuscular system.
2021-05-12 | GSE160027 | GEO
Project description:C2C12 is a myoblast cell line usually used for study of muscle differentiation. Myod1 is a pro-differentiation factor for myogenesis. We found that CRISPR/Cas9-mediated Myod1 gene knockout in C2C12 cells led to the loss of myoblast identity and gain of neural properties.
2021-01-27 | GSE137507 | GEO
Project description:Polycomb group of proteins (PcG) and the nuclear Lamin A are key factors in the maintenance of chromatin higher order structures required for preserving cell identity. Mutations in the Lamin A/C gene cause several diseases, belonging to the class of laminopathies, including Emery-Dreifuss Muscular Dystrophy. Nevertheless, epigenetic mechanisms involved in the pathogenesis of lamin-dependent dystrophy are still largely unknown. We show that Lamin A loss causes deregulated PcG positioning in muscular stem cells followed by upregulation of adipogenic markers and induction of the senescence’s driver p16INK4a from Cdkn2a locus. This aberrant transcriptional programme causes impairment in self-renewal, loss of cell identity and premature exhaustion of quiescent satellite cell pool. Genetic ablation of Cdkn2a locus restores muscle growth and muscle stem cell properties in Lamin A/C null dystrophic mice. In conclusion, our findings suggest that Lamin A has an essential role in preserving satellite cell self-renewal capacity and indicate that Lamin A-dependent muscular dystrophy can be ascribed to intrinsic epigenetic dysfunctions of muscle stem cells
2020-02-04 | GSE123724 | GEO
Project description:Polycomb group of proteins (PcG) and the nuclear Lamin A are key factors in the maintenance of chromatin higher order structures required for preserving cell identity. Mutations in the Lamin A/C gene cause several diseases, belonging to the class of laminopathies, including Emery-Dreifuss Muscular Dystrophy. Nevertheless, epigenetic mechanisms involved in the pathogenesis of lamin-dependent dystrophy are still largely unknown. We show that Lamin A loss causes deregulated PcG positioning in muscular stem cells followed by upregulation of adipogenic markers and induction of the senescence’s driver p16INK4a from Cdkn2a locus. This aberrant transcriptional programme causes impairment in self-renewal, loss of cell identity and premature exhaustion of quiescent satellite cell pool. Genetic ablation of Cdkn2a locus restores muscle growth and muscle stem cell properties in Lamin A/C null dystrophic mice. In conclusion, our findings suggest that Lamin A has an essential role in preserving satellite cell self-renewal capacity and indicate that Lamin A-dependent muscular dystrophy can be ascribed to intrinsic epigenetic dysfunctions of muscle stem cells
2020-02-04 | GSE123723 | GEO