LCR_F1 EMSA Kit
- Known as:
- LCR_F1 EMSA Kit
- Catalog number:
- AY1202
- Product Quantity:
- 25 rxn
- Category:
- -
- Supplier:
- Panomics
- Gene target:
- LCR_F1 EMSA Kit
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- Proteolytic stress frequently arises during disease and aging, particularly in long-lived, post-mitotic cells such as cardiomyocytes. To maintain proteostasis, cardiomyocytes depend on coordinated protein quality control pathways, including the ubiquitin-proteasome system and autophagy. Mechanisms that activate these pathways hold therapeutic potential for heart disease. Here, we demonstrate that transient activation of nuclear factor erythroid 2-like 1 (Nfe2l1, also known as Nrf1), a transcriptional regulator of proteasome activity, in cardiomyocytes during ischemia/reperfusion injury improves cardiac function. In addition to regulating the proteasome, we identify a critical role for Nrf1 in activating autophagy, which is essential for its cardioprotective effects. Through multi-omics analyses, we define both transcriptional and post-transcriptional functions of Nrf1 that underlie its cardioprotective activity. Loss-of-function studies in mice demonstrate that Nrf1, but not its homolog Nrf2, is required for autophagy and baseline cardiac function. Together, our findings establish a dual function of Nrf1 in promoting cardiac proteostasis by regulating both proteasomal and autophagic protein quality control pathways. Activating Nrf1 thus offers a therapeutic strategy for treating ischemic heart disease. - Source: PubMed
Publication date: 2026/04/17
Kankanamge Lakindu PAn HyunjiGuo QinProndzynski MaksymillianKwon Soon HoBonde Durgesh AnilPu William TOlson Eric NCui Miao - The cytosolic peptide:N-glycanase (PNGase, NGLY1 in mammals) is an enzyme that removes N-glycans from misfolded glycoproteins. NGLY1 contributes to cytosolic glycan degradation (non-lysosomal glycan degradation) and is one of the quality control systems for newly synthesized proteins, i.e., ER-associated degradation (ERAD). NGLY1 is also responsible for the activation of a transcription factor, NFE2L1, which participates in several stress responses, including regulation of proteasome subunit expression and oxidative stress. In 2012, NGLY1 deficiency, a human genetic disorder caused by the biallelic mutations in the NGLY1 gene, was discovered. Since then, research on the physiological functions of NGLY1 and the pathogenic mechanism of NGLY1 deficiency has expanded rapidly. Here, we will briefly overview the early history of NGLY1 research and then introduce its versatile functions. We will also provide mechanistic insights into the pathogenesis of NGLY1 deficiency based on studies using model animals, such as worms, flies, and rodents. - Source: PubMed
Fujihira HaruhikoSuzuki Tadashi - As multiple sclerosis (MS) progresses, myelin repair becomes inefficient. To gain insight into the underlying causes, we RNA-sequenced postmortem brain tissues from 4 and 6 patients, comparing remyelinating versus chronically active MS lesions. We identified the transcription factor FoxF2 as highly expressed within remyelinating lesions. Immunohistochemistry and in situ hybridization showed FoxF2 co-expression in GFAP-positive astrocytes, suggesting a subpopulation of astrocytes with a potential role in repair. To investigate how FoxF2 may influence repair, we examined cuprizone (CPZ)-induced de- and remyelination in CreERT2 FoxF2 conditional knockout (FoxF2 KO) mice. In the absence of FoxF2, RNA sequencing of the isolated corpus callosum (CC) showed high gene activation during demyelination and reduced gene activation during remyelination. Upregulated genes in FoxF2 KO mice were related to immune functions and metabolism. Specifically, upregulation of MHC-II and TNF-associated pathway genes, while astrocyte-specific FoxF2 deletion significantly reduced Tgfb2 and Tgfbr2 expression, implicating disrupted TGF-β signaling. The FoxF2 KO mice exhibited upregulation of ribosomal and sphingolipid metabolism genes during demyelination, while structurally related genes, including Mog expression, were impaired in the FoxF2 KO mice. Using network analysis to group highly correlated genes in the CC transcriptome, we identified gene regulatory network (GRN) changes. GRN analysis revealed the loss of FoxF2-associated modules (e.g., Foxf2-Bach2, Nfe2l1-Mafg), indicating impaired coordination of anti-inflammatory and regenerative pathways. In conclusion, analysis of MS white matter (WM) lesions and subsequent experimental data demonstrates that FoxF2 plays a role in regulating repair and gene networks associated with immune regulation, metabolism, and structural remodeling. - Source: PubMed
Publication date: 2026/02/26
Damsbo KarinaReyahi AzadehNik Ali MOubounyt MhanedWeber AnnaHyrlov Kirsten HKingo ChristinaFoged Maria LWaede MieBaumbach JanReynolds RichardCarlsson PeterIlles ZsoltElkjaer Maria L - The proteasome is essential for cellular protein homeostasis through selective destruction of damaged and misfolded proteins. Failure of proteasome-dependent turnover accompanied by accumulation and aggregation of aberrant proteins is a hallmark of aging and late-onset neurodegenerative diseases. SKN-1A/Nrf1, a member of the NFE2L/Nrf family of transcription factors, is a master regulator of proteasome biogenesis. Through transcriptional control of proteasome subunit gene expression, SKN-1A/Nrf1 controls homoeostatic and stress-responsive upregulation of proteasome levels in adaptation to proteasome dysfunction or protein misfolding. SKN-1A/Nrf1 acts in concert with another Nrf family transcription factor, SKN-1C/Nrf2, to regulate many aspects of physiology including stress responses, redox balance, immunity, and metabolism. Here, we demonstrate that a small deletion in the promoter of the pbs-5 gene, which encodes an essential proteasome subunit, uncouples its expression from transcriptional regulation by SKN-1A/Nrf1. This disruption leads to compensatory SKN-1A/Nrf1-dependent upregulation of other proteasome subunit genes, resulting in a homeostatic imbalance in proteasomal gene expression. This pbs-5 regulatory mutation phenocopies some, but not all, aspects of SKN-1A/Nrf1 inactivation, providing evidence that coordinated regulation of proteasomal subunit gene expression underlies a subset of SKN-1A/Nrf1's physiological roles. In comparing the effects of the pbs-5 promoter deletion with isoform-specific inactivation of SKN-1A or SKN-1C, we show that the pbs-5 promoter mutation completely abrogates multiple lifespan extension paradigms. These results reveal that coordinated homeostatic regulation of proteasome subunit gene expression is critical for longevity and healthy aging. - Source: PubMed
Publication date: 2026/02/17
Topalidou IriniLehrbach Nicolas - - Source: PubMed
Publication date: 2026/01/26
Sokolov MaximTaniguchi HiroakiWeber Jonasz Jeremiasz