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Ferritin, heavy polypeptide 1

apoferritin, FTH1, FTH
This gene encodes the heavy subunit of ferritin, the major intracellular iron storage protein in prokaryotes and eukaryotes. It is composed of 24 subunits of the heavy and light ferritin chains. Variation in ferritin subunit composition may affect the rates of iron uptake and release in different tissues. A major function of ferritin is the storage of iron in a soluble and nontoxic state. Defects in ferritin proteins are associated with several neurodegenerative diseases. This gene has multiple pseudogenes. Several alternatively spliced transcript variants have been observed, but their biological validity has not been determined. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, ACID, HAD, Ceruloplasmin, V1a
Papers on apoferritin
Obesity is associated with gene expression and imaging markers of iron accumulation in skeletal muscle.
New
Fernández-Real et al., Girona, Spain. In J Clin Endocrinol Metab, Feb 2016
Design, setting, patients and outcome measures: Markers of iron accumulation were measured in 3 different territories: Iron gene markers (TFRC1, TF, SLC11A2, FTL, FTH1 and SLC40A1) were studied in abdominal rectus abdominis (cohort 1, n=26) and quadriceps (cohort 2, n= 13) muscle using real time PCR, while paravertebral muscle R2* signal (as surrogate of iron content) (cohort 3, n=43) was evaluated by means of MRI.
WO3 Nanofiber-Based Biomarker Detectors Enabled by Protein-Encapsulated Catalyst Self-Assembled on Polystyrene Colloid Templates.
New
Kim et al., Taejŏn, South Korea. In Small, Feb 2016
The metallic NPs, composed of Au, Pd, or Pt, are encapsulated within a protein cage, i.e., apoferritin, to form unagglomerated monodispersed particles with diameters of less than 5 nm.
Whole genome and normalized mRNA sequencing reveal genetic status of TK6, WTK1, and NH32 human B-lymphoblastoid cell lines.
New
Dobrovolsky et al., United States. In Mutat Res Genet Toxicol Environ Mutagen, Feb 2016
These include a single base deletion mutation in the ferritin heavy chain gene (FTH1) resulting in a frame shift and protein truncation in TK6 that impairs iron metabolism.
Hierarchical Organization of Organic Dyes and Protein Cages into Photoactive Crystals.
New
Kostiainen et al., Finland. In Acs Nano, Jan 2016
Toward this end, a hierarchical organization process has been designed in which (a) a supramolecular complex is formed between octacationic zinc Pc (1) and a tetraanionic pyrene (2) derivatives, driven by electrostatic and π-π interactions, and (b) the resulting tetracationic complex acts as a molecular glue that binds to the outer surface anionic patches of the apoferritin (aFt) protein cage, inducing cocrystallization.
Coaxial electrospinning of WO3 nanotubes functionalized with bio-inspired Pd catalysts and their superior hydrogen sensing performance.
New
Kim et al., Taejŏn, South Korea. In Nanoscale, Jan 2016
In addition, catalytic Pd nanoparticles (NPs) were synthesized using bio-inspired protein cages, i.e., apoferritin, and uniformly dispersed within the shell solution and subsequently on the WO3 NTs.
Electron microscopy: Ultrastable gold substrates for electron cryomicroscopy.
Impact
Passmore et al., Cambridge, United Kingdom. In Science, 2015
With this improvement, we determine the structure of apoferritin, a smooth octahedral shell of α-helical subunits that is particularly difficult to solve by electron microscopy.
Plant ferritin--a source of iron to prevent its deficiency.
Review
Zielińska-Dawidziak, Poznań, Poland. In Nutrients, 2014
This protein captures huge amounts of iron ions inside the apoferritin shell and isolates them from the environment.
Selective VPS34 inhibitor blocks autophagy and uncovers a role for NCOA4 in ferritin degradation and iron homeostasis in vivo.
Impact
Murphy et al., Cambridge, United States. In Nat Cell Biol, 2014
NCOA4 directly binds ferritin heavy chain-1 (FTH1) to target the iron-binding ferritin complex with a relative molecular mass of 450,000 to autolysosomes following starvation or iron depletion.
Coupling heme and iron metabolism via ferritin H chain.
Review
Soares et al., Portugal. In Antioxid Redox Signal, 2014
While heme catabolism by heme oxygenase-1 (HO-1) prevents programmed cell death, this cytoprotective effect requires the co-expression of ferritin H (heart/heavy) chain (FTH), which controls the pro-oxidant effect of labile Fe released from the protoporphyrin IX ring of heme.
Problems in obtaining perfect images by single-particle electron cryomicroscopy of biological structures in amorphous ice.
Review
McMullan et al., Cambridge, United Kingdom. In Microscopy (oxf), 2013
In this review, we compare the contrast of experimental electron cryomicroscopy images of two smaller molecular assemblies, namely apoferritin and beta-galactosidase, with that expected from perfect simulated images calculated from their known X-ray structures.
GAPDH in anesthesia.
Review
Seidler, Kansas City, United States. In Adv Exp Med Biol, 2012
The binding site of inhaled anesthetics is described from literature reports on model proteins, such as human serum albumin and apoferritin.
Survivin inhibition by an interacting recombinant peptide, derived from the human ferritin heavy chain, impedes tumor cell growth.
GeneRIF
Groner et al., Frankfurt am Main, Germany. In J Cancer Res Clin Oncol, 2012
Survivin inhibition by an interacting recombinant peptide, derived from the human ferritin heavy chain, impedes tumor cell growth
The use of highly expressed FTH1 as carrier protein for cytosolic targeting in Hansenula polymorpha.
GeneRIF
Suckow et al., Langenfeld, Germany. In J Biotechnol, 2012
To study whether the human ferritin heavy chain (FTH1) can be expressed in Hansenula polymorpha, we integrated an expression cassette for FTH1, analyzed the protein expression, and also designed a FTH1-PTH fusion protein.
Ferritin heavy chain is the host factor responsible for HCV-induced inhibition of apoB-100 production and is required for efficient viral infection.
GeneRIF
Tripodi et al., Roma, Italy. In J Proteome Res, 2012
Induction of ferritin heavy chain expression results in severe inhibition of apoB-100 secretion from hepatoma cells during HCV infection.
Discovery of Novel General Anesthetics Using Apoferritin as a Surrogate System
Review
Maloney et al., Bethesda, United States. In Unknown Journal, 2012
A surrogate approach was recently developed, where the iron-binding protein apoferritin, was demonstrated to possess not only strong binding capacity for many general anesthetics, but also to have a structural architecture highly resembling that of the GABAA receptor transmembrane region.
Regulation of iron-related molecules in the rat hippocampus: sex- and age-associated differences.
GeneRIF
Wang et al., Huntington, United States. In Ann Clin Lab Sci, 2011
The expression of HO1, FTH, and IRP1 mRNAs is higher in the female hippocampus than that observed in male rats.
Elevated serum ferritin and soluble transferrin receptor in infants with congenital hypothyroidism.
GeneRIF
Zhao et al., Hangzhou, China. In J Pediatr Endocrinol Metab, 2011
Elevated serum ferrin in infants is associated with congenital hypothyroidism.
Computational studies on the interactions of inhalational anesthetics with proteins.
Review
Impact
Klein et al., Chennai, India. In Acc Chem Res, 2010
However, later experiments with lipid-free globular proteins, such as luciferase and apoferritin, shifted the focus of anesthetic action to proteins.
Nanoparticulate assemblies of amphiphiles and diagnostically active materials for multimodality imaging.
Impact
Nicolay et al., New York City, United States. In Acc Chem Res, 2009
Moreover, natural nanoparticles, such as viruses, lipoproteins, or apoferritin, as well as hybrid nanostructures composed of inorganic and natural nanoparticles, have been applied broadly.
Pushing the sensitivity envelope of lanthanide-based magnetic resonance imaging (MRI) contrast agents for molecular imaging applications.
Review
Impact
Terreno et al., Torino, Italy. In Acc Chem Res, 2009
For Gd-based agents, high sensitivities can be attained by exploiting a range of nanosized carriers (micelles, liposomes, microemulsions, and the like, as well as biological structures such as apoferritin and lipoproteins) properly loaded with Gd-based chelates.
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