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Glial ferritin maintains self-renewal and proliferation of neural stem cells by supplying iron in Drosophila

ABSTRACT: Glial ferritin maintains self-renewal and proliferation of neural stem cells by supplying iron in Drosophila

PROVIDER: PRJNA994013 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR25244738_1.fastq.gz	Fastqsanger.gz
	SRR25244738_2.fastq.gz	Fastqsanger.gz
	SRR25244739_1.fastq.gz	Fastqsanger.gz
	SRR25244739_2.fastq.gz	Fastqsanger.gz
	SRR25244740_1.fastq.gz	Fastqsanger.gz

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Glial ferritin maintains self-renewal and proliferation of neural stem cells by supplying iron in Drosophila

Project description:Stem cell niche is critical for regulating the behavior of stem cells. Drosophila neural stem cells (Neuroblasts, NBs) are encased by glial niche cells closely, but it still remains unclear whether glial niche cells can regulate the self-renewal and differentiation of NBs. Here we show that ferritin produced by glia, cooperates with Zip13 to transport iron into NBs for the energy production, which is essential to the self-renewal and proliferation of NBs. The knockdown of glial ferritin encoding genes causes energy shortage in NBs, which leads to the low proliferation and premature differentiation of NBs. Moreover, the level of glial ferritin production is affected by the status of NBs, establishing a bicellular iron homeostasis. In this study, we demonstrate that glial cells are indispensable to maintain the self-renewal of NBs, unveiling a novel role of the NB glial niche during brain development.

2024-07-15 | GSE237124 | GEO

The Hyphal Associated Adhesin and Invasin Als3 of Candida albicans Mediates Iron Acquisition from Host Ferritin

Project description:Iron sequestration by host iron-binding proteins is an important mechanism of resistance to microbial infections. Inside oral epithelial cells, iron is stored within the ferritin, and is therefore usually not accessible to pathogenic microbes. We observed that the ferritin concentration within oral epithelial cells was directly related to their susceptibility to damage by the human pathogenic fungus Candida albicans. Thus, we hypothesized that host ferritin may be used as an iron source by this organism. A screen of C. albicans mutants lacking components of each of the three iron acquisition systems revealed that only the reductive pathway is involved in iron utilization from ferritin by this organism. Transcriptional profiling of wild-type and hyphal-defective C. albicans strains suggested that the C. albicans invasin-like protein Als3 plays a role in ferritin binding.

2008-05-20 | GSE11490 | GEO

Critical Role of Ferritin-Mediated Iron Homeostasis in the Maintenance of Hematopoietic Stem Cells and Leukemia Stem Cells

Project description:Iron metabolism has emerged as a critical factor in cell viability, both in normal and pathological contexts. However, the intricate relationship between iron metabolism and the maintenance of adult stem cells and cancer stem cells remains incompletely understood. The ferritin complex, responsible for intracellular iron storage and buffering, plays a pivotal role in this process. Our research provides insights into the regulatory role of ferritin-mediated iron homeostasis in hematopoietic stem cells (HSCs).

2024-04-17 | GSE240742 | GEO

Masison2022 - Cellular ferritin iron storage

Project description:This is a small model of ferritin iron sequestration kinetics. The model’s parameter values were determined from published kinetic and binding experiments and the model was validated against independent data not used in its construction. Beyond its utility to investigate properties of ferritin iron sequestration itself, we propose this model to be used as a building block for larger models of iron metabolism in a variety of specific cell types.

2023-02-07 | MODEL2211030001 | BioModels

Gene Expression by array after Ferritin Knockdown in Preferential Iron Trafficking Characterizes Glioblastoma Stem-like Cells

Project description:Glioblastomas display hierarchies with self-renewing cancer stem-like cells (CSCs). RNA sequencing and enhancer mapping revealed regulatory programs unique to CSCs causing upregulation of the iron transporter transferrin, the top differentially expressed gene compared to tissue-specific progenitors. Direct interrogation of iron uptake demonstrated CSCs potently extract iron from the microenvironment more effectively than other tumor cells. Systematic interrogation of iron flux determined that CSCs preferentially require transferrin receptor and ferritin - two core iron regulators - to propagate and form tumors in vivo. Depleting ferritin disrupted CSC mitotic progression, through the STAT3-FoxM1 regulatory axis, revealing an iron-regulated CSC pathway. Iron is a unique, primordial metal fundamental for earliest life forms, and on which CSCs have an epigenetically programmed, targetable dependence.

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Id1 maintains embryonic stem cell self-renewal by upregulation of Nanog and repression of Brachyury expression

Project description:Understanding the mechanism by which embryonic stem (ES) cells self-renew is critical for the realization of their therapeutic potential. Previously it had been shown that in combination with LIF, Id proteins were sufficient to maintain mouse ES cells in a self-renewing state. Here we investigate the requirement for Id1 in maintaing ES cell self-renewal and blocking differentiation. We find that Id1-/- ES cells have a propensity to differentiate and a decreased capacity to self-renew. Chronic or acute loss of Id1 leads to a down-regulation of Nanog, a critical regulator of self-renewal. In addition, in the absence of Id1, ES cells express elevated levels of Brachyury, a marker of mesendoderm differentiation. We find that loss of both Nanog and Id1 is required for the up-regulation of Brachyury, and Id1 maintains Nanog expression by blocking the expression of Zeb1, a repressor of Nanog transcription. These results identify Id1 as an important factor in the maintenance of ES cell self-renewal and suggest a plausible mechanism for its control of lineage commitment. Wild type and Id1-/- ES cells were grown on gelatin under normal self-renewing conditions (in the presence of serum and LIF).

2011-11-01 | E-GEOD-19144 | biostudies-arrayexpress

Transtriptome analysis of bone marrow-derived neutrophils after ferritin injection

Project description:How ferritin regulates neutrophil leukocyte function remains unknown. To address this question, we injected mice with ferritin. bone marrow-derived neutrophils (BMDN) were isolated by density gradient centrifugation. Then we displayed RNA-seq of isolated BMDNs.

2021-07-09 | GSE179679 | GEO

Masison2022 - Liver Iron Metabolism with updated ferritin

Project description:This is a new version of a liver iron model (original from Mitchell 2013 BIOMD0000000498) with updated kinetics of ferritin iron storage. It uses MODEL2211030001 as a substitute for the original ferritin reactions.

2023-02-07 | MODEL2211030002 | BioModels

CHD2 maintains spermatogonial self-renewal by promoting chromatin activity and mRNA stability

Project description:CHD2 maintains spermatogonial self-renewal by promoting chromatin activity and mRNA stability

| PRJNA816070 | ENA

Ferritin-mediated iron detoxification mediates hypothermia survival in Caenorhabditis elegans and murine neurons.

Project description:How animals rewire cellular programs to survive cold is a fascinating problem with potential biomedical implications, ranging from emergency medicine to space travel. Studying a hibernation-like response in the free-living nematode Caenorhabditis elegans, we uncovered a regulatory axis that enhances the natural resistance of nematodes to severe cold. This axis involves conserved transcription factors, DAF-16/FoxO and PQM-1, which jointly promote cold survival by upregulating FTN-1, a protein related to mammalian ferritin heavy chain (FTH1). Moreover, we show that inducing expression of FTH1 also promotes cold survival of mammalian neurons, a cell type particularly sensitive to deterioration in hypothermia. Our findings in both animals and cells suggest that FTN-1/FTH1 facilitates cold survival by detoxifying ROS-generating iron species. We finally show that mimicking the effects of FTN-1/FTH1 with drugs protects neurons from cold-induced degeneration, opening a potential avenue to improved treatments of hypothermia.

2022-10-14 | PXD034794 | Pride

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