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FHL3 promotes the formation of fast glycolytic muscle fibers by interacting with YY1 and muscle glycolytic metabolism

ABSTRACT: FHL3 promotes the formation of fast glycolytic muscle fibers by interacting with YY1 and muscle glycolytic metabolism

PROVIDER: PRJNA883593 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR21681905_1.fastq.gz	Fastqsanger.gz
	SRR21681905_2.fastq.gz	Fastqsanger.gz
	SRR21681906_1.fastq.gz	Fastqsanger.gz
	SRR21681906_2.fastq.gz	Fastqsanger.gz
	SRR21681907_1.fastq.gz	Fastqsanger.gz

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FHL3 promotes the formation of fast glycolytic muscle fibers by interacting with YY1 and muscle glycolytic metabolism

Project description:Composition of distinct muscle fiber types plays an important role in the regulation of skeletal muscle metabolism, as well as animal meat production.Four and a half LIM domain protein 3 (FHL3) is highly expressed in fast glycolytic muscle fibers and differentially regulates the expression of MyHC isoforms at cellular levels.Here we knocked out FHL3 in C2C12 cells by CRISPR/Cas9 technology.RNA sequencing analyses revealed that the expression of MYH7 in KO cells was significantly increased, while the expression of MYH1,MYH2 and MYH4 was significantly decreased.Further comfirm FHL3 regulates the transformation of muscle fiber types.

2022-11-17 | GSE213996 | GEO

Transcriptome Profiling of Fast-Glycolytic and Slow-Oxidative Muscle Fibers in Chickens under Short- and Long-Term High-Fat Diets

Project description:Skeletal muscle fiber composition influences meat quality and metabolic regulation in poultry, yet fiber-type–specific responses to high-fat diet (HFD) remain poorly understood. This study examined the effects of short-term (SHFD) and long-term (LHFD) HFD feeding on fast/glycolytic (pectoralis major, PEM) and slow/oxidative (soleus, SOL) muscles in Guangyuan grey chickens. Histological analysis showed SOL fibers underwent oxidative-to-glycolytic transition under LHFD, accompanied by mitochondrial disruption. PEM accumulated more lipids and showed early metabolic stress. Transcriptome profiling revealed 3840 differentially expressed genes between PEM and SOL, with 1761 constitutively different. Under SHFD, SOL activated protective pathways including PPAR and autophagy, while PEM showed limited adaptation. LHFD induced further downregulation of fatty acid metabolism and structural genes (e.g., ALPK1, CA12, PM20D2, SLC27A1, and GADD45G) in PEM, but SOL maintained or enhanced expression of genes (e.g., NR4A3, PRKAG2, NOCT, PPARA, and SLC6A6) involved in muscle organization and lipid processing. Temporal clustering highlighted progressive divergence in transcriptional responses. These results suggest SOL fibers exhibit greater resilience to lipid overload than PEM fibers. Our findings provide insight into the molecular basis of muscle-type–specific adaptations to dietary fat and offer targets for improving metabolic health and meat quality in poultry.

2025-12-02 | GSE304154 | GEO

YY1 regulates skeletal muscle regeneration through controlling metabolic reprogramming during adult muscle stem cell activation

Project description:Skeletal muscle satellite cells (SCs) are adult muscle stem cells responsible for muscle regeneration after acute or chronic injuries. The lineage progression of quiescent satellite cells toward activation, proliferation and differentiation during the regeneration is orchestrated by cascades of transcription factors (TFs). Here we elucidate the functional role of a ubiquitously expressed TF, Yin Yang1 (YY1) in muscle regeneration. Muscle-specific deletion of YY1 in embryonic muscle progenitors leads to severe deformity of diaphragm muscle formation thus postnatal death. Inducible deletion of YY1 in satellite cells almost completely blocks the acute damage induced muscle repair and exacerbates the chronic injury induced dystrophic phenotype. Examination of SCs revealed that YY1 loss results in cell autonomous defect in cell activation and proliferation. Mechanistic search through genome-wide profiling of YY1 regulated transcriptome and YY1 binding revealed that YY1 binds and suppresses mitochondrial gene expression. Simultaneously, it also activates Hif1α mediated glycolytic genes to facilitate a metabolic reprogramming toward glycolysis which is needed for SC activation. Altogether our findings have identified YY1 as a key regulator of SC metabolic reprogramming during cell activation through its dual roles in modulating both mitochondrial and glycolytic pathways.

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Angiogenic potential of skeletal muscle derived extracellular vesicles differs between oxidative and glycolytic muscle

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Project description:Difference in mRNA between fast and slow type muscle fibers

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High-throughput Proteomics fiber typing (ProFiT) for comprehensive characterization of single skeletal muscle fibers

Project description:Skeletal muscles are composed of a heterogeneous collection of fiber types with different physiological adaption in response to a stimulus and disease-related conditions. Each fiber has a specific molecular expression of myosin heavy chain molecules (MyHC). So far MyHCs are currently the best marker proteins for characterization of individual fiber types and several proteome profiling studies have helped to dissect the molecular signature of whole muscles and individual fibers. Herein, we describe a mass spectrometric workflow to measure skeletal muscle fiber type-specific proteomes. To bypass the limited quantities of protein in single fibers, we developed a Proteomics high-throughput Fiber Typing (ProFiT) approach enabling profiling of MyHC in single fibers. Aliquots of protein extracts from separated muscle fibers were subjected to capillary LC-MS gradients to profile MyHC isoforms in a 96-well format. Muscle fibers with the same MyHC protein expression were pooled and subjected to proteomic, pulsed-SILAC and phosphoproteomic analysis. Our fiber type-specific quantitative proteome analysis confirmed the distribution of fiber types in the soleus muscle, substantiates metabolic adaptions in oxidative and glycolytic fibers, and highlighted significant differences between the proteomes of type IIb fibers from different muscle groups, including a differential expression of desmin and actinin-3. A detailed map of the Lys-6 incorporation rates in muscle fibers showed an increased turnover of slow fibers compared to fast fibers. In addition, labeling of mitochondrial respiratory chain complexes revealed a broad range of Lys-6 incorporation rates, depending on the localization of the subunits within distinct complexes.

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Proteomics of slow and fast human muscle fibers reveals extensive fiber type-specific adaptations in response to exercise training

Project description:Skeletal muscle plays an important role in the health-promoting effects of exercise training, yet the underlying mechanisms are not fully elucidated. Proteomics of skeletal muscle is challenging due to presence of non-muscle tissues and existence of different fiber types confounding the results. This can be circumvented by analysis of pure fibers; however this requires isolation of fibers from fresh tissues. We developed a workflow enabling proteomics analysis of isolated muscle fibers from freeze-dried muscle biopsies and identified >4000 proteins. We investigated effects of exercise training on the pool of slow and fast muscle fibers. Exercise altered expression of >500 proteins irrespective of fiber type covering several metabolic processes, mainly related to mitochondria. Furthermore, exercise training altered proteins involved in regulation of post-translational modifications, transcription, Ca++ signaling, fat, and glucose metabolism in a fiber type-specific manner. Our data serves as a valuable resource for elucidating molecular mechanisms underlying muscle performance and health. Finally, our workflow offers methodological advancement allowing proteomic analyses of already stored freeze-dried human muscle biopsies.

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