scholarly journals Chemistry and Biology of Ferritin

Metallomics ◽  
2021 ◽  
Author(s):  
Marina Plays ◽  
Sebastian Müller ◽  
Raphaël Rodriguez
Keyword(s):  
Iron Homeostasis ◽  
Cell Metabolism ◽  
Essential Element ◽  
Biological Functions ◽  
Iron Storage ◽  
Potential Biomarker ◽  
Specific Manner ◽  
Cellular Compartments ◽  
Structure And Activity ◽  
Iron Storage Protein

Abstract Iron is an essential element required by cells and has been described as a key player in ferroptosis. Ferritin operates as a fundamental iron storage protein in cells forming multimeric assemblies with crystalline iron cores. We discuss the latest findings on ferritin structure and activity and its link to cell metabolism and ferroptosis. The chemistry of iron, including its oxidations states, is important for its biological functions, its reactivity and the biology of ferritin. Ferritin can be localized in different cellular compartments and secreted by cells with a variety of functions depending on its spatial context. Here, we discuss how cellular ferritin localization is tightly linked to its function in a tissue-specific manner, and how impairment of iron homeostasis is implicated in diseases including cancer and COVID-19. Ferritin is a potential biomarker and we discuss latest research where it has been employed for imaging purposes and drug delivery.

scholarly journals Mobilization of Iron Stored in Bacterioferritin Is Required for Metabolic Homeostasis in Pseudomonas aeruginosa

Pathogens ◽  
2020 ◽  
Vol 9 (12) ◽  
pp. 980
Author(s):  
Achala N. D. Punchi Hewage ◽  
Leo Fontenot ◽  
Jessie Guidry ◽  
Thomas Weldeghiorghis ◽  
Anil K. Mehta ◽  
...  
Keyword(s):  
Iron Homeostasis ◽  
Culture Media ◽  
Acid Synthesis ◽  
Iron Limitation ◽  
Metabolic Homeostasis ◽  
Intracellular Iron ◽  
Amino Acid Synthesis ◽  
Iron Storage ◽  
Low Levels ◽  
Iron Storage Protein

Iron homeostasis offers a significant bacterial vulnerability because pathogens obtain essential iron from their mammalian hosts, but host-defenses maintain vanishingly low levels of free iron. Although pathogens have evolved mechanisms to procure host-iron, these depend on well-regulated iron homeostasis. To disrupt iron homeostasis, our work has targeted iron mobilization from the iron storage protein bacterioferritin (BfrB) by blocking a required interaction with its cognate ferredoxin partner (Bfd). The blockade of the BfrB–Bfd complex by deletion of the bfd gene (Δbfd) causes iron to irreversibly accumulate in BfrB. In this study we used mass spectrometry and NMR spectroscopy to compare the proteomic response and the levels of key intracellular metabolites between wild type (wt) and isogenic ΔbfdP. aeruginosa strains. We find that the irreversible accumulation of unusable iron in BfrB leads to acute intracellular iron limitation, even if the culture media is iron-sufficient. Importantly, the iron limitation and concomitant iron metabolism dysregulation trigger a cascade of events that lead to broader metabolic homeostasis disruption, which includes sulfur limitation, phenazine-mediated oxidative stress, suboptimal amino acid synthesis and altered carbon metabolism.

scholarly journals The pupylation machinery is involved in iron homeostasis by targeting the iron storage protein ferritin

2016 ◽  
Vol 113 (17) ◽  
pp. 4806-4811 ◽  
Author(s):  
Andreas Küberl ◽  
Tino Polen ◽  
Michael Bott
Keyword(s):  
Posttranslational Modification ◽  
Storage Protein ◽  
Iron Homeostasis ◽  
Growth Defect ◽  
Iron Release ◽  
Iron Storage ◽  
Protection Mechanism ◽  
Aaa Atpase ◽  
Iron Supply ◽  
Iron Storage Protein

The balance of sufficient iron supply and avoidance of iron toxicity by iron homeostasis is a prerequisite for cellular metabolism and growth. Here we provide evidence that, in Actinobacteria, pupylation plays a crucial role in this process. Pupylation is a posttranslational modification in which the prokaryotic ubiquitin-like protein Pup is covalently attached to a lysine residue in target proteins, thus resembling ubiquitination in eukaryotes. Pupylated proteins are recognized and unfolded by a dedicated AAA+ ATPase (Mycobacteriumproteasomal AAA+ ATPase; ATPase forming ring-shaped complexes). In Mycobacteria, degradation of pupylated proteins by the proteasome serves as a protection mechanism against several stress conditions. Other bacterial genera capable of pupylation such asCorynebacteriumlack a proteasome, and the fate of pupylated proteins is unknown. We discovered thatCorynebacterium glutamicummutants lacking components of the pupylation machinery show a strong growth defect under iron limitation, which was caused by the absence of pupylation and unfolding of the iron storage protein ferritin. Genetic and biochemical data support a model in which the pupylation machinery is responsible for iron release from ferritin independent of degradation.

scholarly journals Peran Ferritin pada Stroke Iskemik Akut

2021 ◽  
Vol 10 (2) ◽  
pp. 127-132
Author(s):  
Lisda Amalia ◽  
Keyword(s):  
Oxidative Stress ◽  
Ischemic Stroke ◽  
Iron Homeostasis ◽  
Cell Damage ◽  
The Body ◽  
Neurological Deficits ◽  
Iron Storage ◽  
The Central Nervous System ◽  
Focal Injury ◽  
Iron Storage Protein

Stroke is a neurological deficit that occurs due to acute focal injury to the central nervous system that occurs solely due to vascular disorders, including cerebral infarction or bleeding. Ferritin is an intracellular and extracellular iron storage protein which is essential for iron homeostasis in the body. Ferritin is expressed in microglia and macrophages, and also in neurons. If there is cell damage due to ischemic stroke, ferritin will leave the cells and enter the serum. The hypoxia-ischemic state in stroke induces the expression of ferritin in oligodendrocytes and microglia. When there is oxidative stress, ferritin formation will increase. The function of ferritin in times of oxidative stress is still controversial. Ferritin in this condition can act as a scavenger and as a donor for free iron ions. Ischemic stroke patients with larger lesions and more severe neurological deficits showed higher serum ferritin levels and a higher likelihood of complications of bleeding transformation.

scholarly journals Structure and function of a 9.6 megadalton bacterial iron storage compartment

2019 ◽  
Author(s):  
T. W. Giessen ◽  
B. J. Orlando ◽  
A. A. Verdegaal ◽  
M. G. Chambers ◽  
J. Gardener ◽  
...  
Keyword(s):  
Iron Homeostasis ◽  
Storage Proteins ◽  
Essential Element ◽  
Redox Balance ◽  
Intracellular Iron ◽  
Iron Storage ◽  
Storage Compartment ◽  
X Ray Crystallography ◽  
Iron Storage Proteins ◽  
Assembly Principles

AbstractIron storage proteins are essential for maintaining intracellular iron homeostasis and redox balance. Iron is generally stored in a soluble and bioavailable form inside ferritin protein compartments. However, some organisms do not encode ferritins and thus rely on alternative storage strategies. Encapsulins, a class of protein-based organelles, have recently been implicated in microbial iron and redox metabolism. Here, we report the structural and mechanistic characterization of a 42 nm two-component encapsulin-based iron storage compartment from Quasibacillus thermotolerans. Using cryo-electron microscopy and x-ray crystallography, we reveal the assembly principles of a thermostable T = 4 shell topology and its catalytic ferroxidase cargo. We show that the cargo-loaded compartment has an exceptionally large iron storage capacity storing over 23,000 iron atoms. These results form the basis for understanding alternate microbial strategies for dealing with the essential element iron.

scholarly journals Ferritin: An Inflammatory Player Keeping Iron at the Core of Pathogen-Host Interactions

2020 ◽  
Vol 8 (4) ◽  
pp. 589 ◽  
Author(s):  
Ana C. Moreira ◽  
Gonçalo Mesquita ◽  
Maria Salomé Gomes
Keyword(s):  
Inflammatory Diseases ◽  
Essential Element ◽  
Basic Research ◽  
Cell Types ◽  
Acid Synthesis ◽  
Organ Damage ◽  
Iron Storage ◽  
Host Interactions ◽  
Cellular Iron ◽  
Iron Storage Protein

Iron is an essential element for virtually all cell types due to its role in energy metabolism, nucleic acid synthesis and cell proliferation. Nevertheless, if free, iron induces cellular and organ damage through the formation of free radicals. Thus, iron levels must be firmly controlled. During infection, both host and microbe need to access iron and avoid its toxicity. Alterations in serum and cellular iron have been reported as important markers of pathology. In this regard, ferritin, first discovered as an iron storage protein, has emerged as a biomarker not only in iron-related disorders but also in inflammatory diseases, or diseases in which inflammation has a central role such as cancer, neurodegeneration or infection. The basic research on ferritin identification and functions, as well as its role in diseases with an inflammatory component and its potential as a target in host-directed therapies, are the main considerations of this review.

scholarly journals The Adaptive Mechanism of Plants to Iron Deficiency via Iron Uptake, Transport, and Homeostasis

2019 ◽  
Vol 20 (10) ◽  
pp. 2424 ◽  
Author(s):  
Xinxin Zhang ◽  
Di Zhang ◽  
Wei Sun ◽  
Tianzuo Wang
Keyword(s):  
Iron Deficiency ◽  
Iron Uptake ◽  
Iron Homeostasis ◽  
Iron Acquisition ◽  
Essential Element ◽  
Transport Mechanisms ◽  
Iron Storage ◽  
Iron Deficient ◽  
Dicotyledonous Plants ◽  
Shed Light

Iron is an essential element for plant growth and development. While abundant in soil, the available Fe in soil is limited. In this regard, plants have evolved a series of mechanisms for efficient iron uptake, allowing plants to better adapt to iron deficient conditions. These mechanisms include iron acquisition from soil, iron transport from roots to shoots, and iron storage in cells. The mobilization of Fe in plants often occurs via chelating with phytosiderophores, citrate, nicotianamine, mugineic acid, or in the form of free iron ions. Recent work further elucidates that these genes’ response to iron deficiency are tightly controlled at transcriptional and posttranscriptional levels to maintain iron homeostasis. Moreover, increasing evidences shed light on certain factors that are identified to be interconnected and integrated to adjust iron deficiency. In this review, we highlight the molecular and physiological bases of iron acquisition from soil to plants and transport mechanisms for tolerating iron deficiency in dicotyledonous plants and rice.

scholarly journals FTH1 Pseudogenes in Cancer and Cell Metabolism

Cells ◽  
2020 ◽  
Vol 9 (12) ◽  
pp. 2554
Author(s):  
Maddalena Di Sanzo ◽  
Barbara Quaresima ◽  
Flavia Biamonte ◽  
Camillo Palmieri ◽  
Maria Concetta Faniello
Keyword(s):  
Gene Expression ◽  
Cell Metabolism ◽  
Structural Features ◽  
Intracellular Iron ◽  
Iron Storage ◽  
Master Regulators ◽  
Detailed Classification ◽  
Ferritin Gene ◽  
Complex Regulatory Network ◽  
Iron Storage Protein

Ferritin, the principal intracellular iron-storage protein localized in the cytoplasm, nucleus, and mitochondria, plays a major role in iron metabolism. The encoding ferritin genes are members of a multigene family that includes some pseudogenes. Even though pseudogenes have been initially considered as relics of ancient genes or junk DNA devoid of function, their role in controlling gene expression in normal and transformed cells has recently been re-evaluated. Numerous studies have revealed that some pseudogenes compete with their parental gene for binding to the microRNAs (miRNAs), while others generate small interference RNAs (siRNAs) to decrease functional gene expression, and still others encode functional mutated proteins. Consequently, pseudogenes can be considered as actual master regulators of numerous biological processes. Here, we provide a detailed classification and description of the structural features of the ferritin pseudogenes known to date and review the recent evidence on their mutual interrelation within the complex regulatory network of the ferritin gene family.

Polygonal profiles of ferritin molecules

1983 ◽  
Vol 41 ◽  
pp. 600-601
Author(s):  
William H. Massover
Keyword(s):  
Axial Ratio ◽  
X Ray Diffraction ◽  
Rhombic Dodecahedron ◽  
Apparent Contradiction ◽  
Iron Storage ◽  
X Ray ◽  
Hexagonal Shape ◽  
Axes Of Symmetry ◽  
Apparent Conflict ◽  
Iron Storage Protein

The molecular structure of the iron-storage protein, ferritin, is becoming known in ever finer detail. The 24 apoferritin subunits (MW ca. 20,000) have a 2:1 axial ratio and are polymerized with 4:3:2 symmetry to form an outer shell surrounding a variable amount of microcrystalline iron, Recent x-ray diffraction results indicate that the projected outline of the native molecule has a quasi-hexagonal shape when viewed down the 3-fold axes of symmetry, and a quasi-square shape when looking down the 4-fold axes. To date, no electron microscope study has reported observing anything other than circular profiles, which would indicate that ferritin is strictly spherical. The apparent conflict between the "hollow sphere" of electron microscopy (E.M.) and the "truncated rhombic dodecahedron" of x-ray diffraction could reflect the poorer effective resolution of E.M. coming from radiation damage, staining, drying, etc. The present study investigates the detailed shape of individual ferritin molecules in order to search for the predicted aspherical profiles and to interpret the nature of this apparent contradiction.

scholarly journals Effect of Intense Exercise on Plasma Macrominerals and Trace Elements in Lidia Bulls

2021 ◽  
Vol 8 (6) ◽  
pp. 97
Author(s):  
Francisco Escalera-Valente ◽  
Marta E. Alonso ◽  
Juan M. Lomillos ◽  
Vicente R. Gaudioso ◽  
Ángel J. Alonso ◽  
...  
Keyword(s):  
Cell Metabolism ◽  
Sweat Glands ◽  
Stressful Situation ◽  
Biological Functions ◽  
Intense Exercise ◽  
Physical Effort ◽  
Mean Values ◽  
Inorganic Substances ◽  
Body Tissues ◽  
Icp Ms

Minerals are inorganic substances present in all body tissues and fluids that directly or indirectly influence the maintenance of multiple metabolic processes and, therefore, are essential for the development of various biological functions. The Lidia bull breed may be considered an athlete, as during a bull fight it displays considerable physical effort of great intensity and short duration in a highly stressful situation. The objective of this study was to assess plasma minerals concentration (macro- and microminerals) in Lidia bulls after intense physical exercise during a bull fight. Plasma Ca, Mg, P, K, Na, Fe, Cr, Co, Ni, Cu, Zn, Se and Mo concentrations were measured in 438 male Lidia bulls. Ca, P and Mg were measured using a Cobas Integra autoanalyzer, while Na and K were determined by ICP-AES, and Fe, Cr, Co, Ni, Cu, Zn, Se and Mo were measured by ICP-MS. All macrominerals, (Ca: 2.96 ± 0.31, Mg: 1.27 ± 0.17, P: 3.78 ± 0.65, K: 7.50 ± 1.58, Na: 150.15 ± 19.59 in mmol/L), and Cr (1.24 ± 0.58), Ni (0.249 ± 1.07), Cu (22.63 ± 4.84) and Zn (24.14 ± 5.59, in μmol/L) showed greater mean values than the reported reference values in the published literature, while Co (0.041 ± 0.07), Se (0.886 ± 0.21) and Mo (0.111 ± 0.08, in μmol/L) values were lower than those reported for other bovine breeds. These increased concentrations could be justified mainly by muscle cell metabolism, hepatic need to provide energy, and intense dehydration and hemoconcentration by losses through sweat glands or urination.

scholarly journals Trafficking of Stretch-Regulated TRPV2 and TRPV4 Channels Inferred Through Interactomics

Biomolecules ◽  
2019 ◽  
Vol 9 (12) ◽  
pp. 791
Author(s):  
Pau Doñate-Macián ◽  
Jennifer Enrich-Bengoa ◽  
Irene R. Dégano ◽  
David G. Quintana ◽  
Alex Perálvarez-Marín
Keyword(s):  
Protein Interactions ◽  
Transient Receptor Potential ◽  
Cell Structure ◽  
Receptor Potential ◽  
Transient Receptor Potential Vanilloid ◽  
Protein Protein Interactions ◽  
Phosphoinositide Signaling ◽  
Transient Receptor ◽  
Cellular Compartments ◽  
Structure And Activity

Transient receptor potential cation channels are emerging as important physiological and therapeutic targets. Within the vanilloid subfamily, transient receptor potential vanilloid 2 (TRPV2) and 4 (TRPV4) are osmo- and mechanosensors becoming critical determinants in cell structure and activity. However, knowledge is scarce regarding how TRPV2 and TRPV4 are trafficked to the plasma membrane or specific organelles to undergo quality controls through processes such as biosynthesis, anterograde/retrograde trafficking, and recycling. This revision lists and reviews a subset of protein–protein interactions from the TRPV2 and TRPV4 interactomes, which is related to trafficking processes such as lipid metabolism, phosphoinositide signaling, vesicle-mediated transport, and synaptic-related exocytosis. Identifying the protein and lipid players involved in trafficking will improve the knowledge on how these stretch-related channels reach specific cellular compartments.

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