Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Dysferlin deficient mice proteomics

ABSTRACT: Investigation of age-dependent changes in the proteomic profile of Dysferlin-deficient mouse skeletal muscle relative to healthy muscle.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Mus Musculus (ncbitaxon:10090)

SUBMITTER: Stephanie Cologna

PROVIDER: MSV000088639 | MassIVE | Tue Jan 04 15:30:00 GMT 2022

REPOSITORIES: MassIVE

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Publications

Relative quantification of progressive changes in healthy and dysferlin-deficient mouse skeletal muscle proteomes.

Golding Adriana E AE Li Wenping W Blank Paul S PS Cologna Stephanie M SM Zimmerberg Joshua J

Muscle & nerve 20230914 5

<h4>Introduction/aims</h4>Individuals with dysferlinopathies, a group of genetic muscle diseases, experience delay in the onset of muscle weakness. The cause of this delay and subsequent muscle wasting are unknown, and there are currently no clinical interventions to limit or prevent muscle weakness. To better understand molecular drivers of dysferlinopathies, age-dependent changes in the proteomic profile of skeletal muscle (SM) in wild-type (WT) and dysferlin-deficient mice were identified.<h4 ...[more]

PMID: 37706611

Similar Datasets

Soleus Muscle of Aged PAPP-A-Deficient Mice

Project description:Mice deficient in pregnancy-associated plasma protein-A (PAPP-A) have extended lifespan associated with decreased incidence and severity of degenerative diseases of age, such as cardiomyopathy and nephropathy. In this study, the effect of PAPP-A deficiency on aging skeletal muscle was investigated.

2016-07-15 | GSE84390 | GEO

Cardiac and skeletal muscle gene expression profiles in dysferlin deficient mice

2005-07-10 | GSE2507 | GEO

Transcription profiling of skeletal and cardiac muscles in dysferlin-deficient SJL/J mice and wild type mice to understand the protective mechanisms against dysferlin deficiency in cardiac muscles.

Project description:Dysferlin is expressed in skeletal and cardiac muscle. However, dysferlin deficiency, namely limb girdle muscular dystrophy 2B (LGMD2B) and Myoshi myopathy, results in skeletal muscle weakness and spares the heart. This dichotomy could be caused by differential regulation of protective mechanisms. Therefore, we compared intraindividual mRNA expression profiles between cardiac and skeletal muscle in dysferlin-deficient SJL/J mice and normal C57BL/6 mice. Experiment Overall Design: 20 chips were analyzed. They represent 4 groups of 5 replicates each. Experiment Overall Design: The 4 groups are cardiac (LV) and skeletal muscle of normal and dysferlin deficient mice. Experiment Overall Design: Tissues from normal mice are the controls in comparison to tissues of dysferlin deficient mice.

2007-09-04 | E-GEOD-2507 | biostudies-arrayexpress

Muscle from patients with mitochondrial myopathies and congenital muscular dystrophies versus normal human muscle

Project description:Global gene expression analysis was performed comparing human skeletal muscle samples from patients with various forms of muscular dystrophy and mitochondrial myopathies in order to identify specific gene expression changes associated with collagen VI deficiency (leading to UllrichM-BM-4s Congenital Muscular Dystrophy) and depletion of mitochondrial DNA relative to other mitochondrial myopathies We analysed the gene expression profile of skeletal muscle from children suffering from mitochondrial myopathies and various forms of muscular dystrophy relative to skeletal muscle from healthy children using commercially available arrays that represents the complete human genome (Agilent Human SurePrintGE, 8x60K )

2015-01-20 | E-GEOD-43698 | biostudies-arrayexpress

Muscle specific proteasome deficient mice

Project description:The ubiquitin-proteasome and autophagy-lysosome pathways are the two major routes for protein and organelle clearance. In skeletal muscle, both systems’ excessive activation induces severe muscle loss. Although altered proteasomal function has been observed in various myopathies, the specific role of proteasomal activity in skeletal muscle has not been determined by loss-of-function approaches. Here, we report that muscle-specific deletion of a crucial proteasomal gene, Rpt3, resulted in profound muscle atrophy and decrease in force. Rpt3 null muscles showed reduced proteasomal activity in early age, accumulation of basophilic structure, disorganization of sarcomere, and formation of vacuoles and concentric membranous structures in electronmicroscope. We also observed accumulation of ubiquitin, p62, LC3, TDP43, FUS and VCP proteins. Proteasomal activity is important to preserve muscle mass and to maintain myofiber integrity. Our results suggest that inhibition/alteration of proteasomal activity can contribute to myofiber degeneration and weakness in muscle disorders, such as inclusion body myositis, characterized by accumulation of abnormal inclusions.

2014-09-30 | GSE34896 | GEO

Skeletal Muscle Transcriptomics

Project description:Healthy human skeletal muscle samples were processed and analyzed to infer age associated skeletal muscle changes.

2020-04-07 | GSE129643 | GEO

Skeletal Muscle Transcriptome in Healthy Aging

Project description:Healthy human skeletal muscle samples were processed and analyzed to infer age associated skeletal muscle changes

2021-01-08 | GSE164471 | GEO

Muscle specific proteasome deficient mice

2014-09-30 | E-GEOD-34896 | biostudies-arrayexpress

Proteomics analysis of skeletal muscle from leptin-deficient ob/ob mice reveals adaptive remodeling of metabolic characteristics and fiber type composition

Project description:Skeletal muscle insulin resistance, an early metabolic defect in the pathogenesis of type 2 diabetes, may be a cause or consequence of altered protein expressions profiles. Proteomics technology offers enormous promise to investigate molecular mechanisms underlying pathologies, however, the analysis of skeletal muscle is challenging. Using a state-of-the-art mass spectrometry (MS) based workflow, we performed a global proteomics analysis of skeletal muscle from leptin-deficient, obese, type 2 diabetic (ob/ob) and lean mice, identifying more than 6,000 proteins with 118 proteins differentially regulated in obesity. This included protein kinases, phosphatases, and secreted and fiber type associated proteins. Enzymes involved in lipid metabolism in skeletal muscle from ob/ob mice were increased, providing evidence against reduced fatty acid oxidation in lipid-induced insulin resistance. Mitochondrial and peroxisomal proteins, as well as components of pyruvate and lactate metabolism were likewise increased. Finally, the skeletal muscle proteome from ob/ob mice displayed a shift towards the ‘slow fiber type’. This detailed characterization of obese rodent models of type 2 diabetes demonstrates an efficient workflow for skeletal muscle proteomics, which may easily be adapted to other complex tissues.

2018-01-26 | PXD007697 | Pride