Alternative titles; symbols
HGNC Approved Gene Symbol: FTH1
SNOMEDCT: 1230310007;
Cytogenetic location: 11q12.3 Genomic coordinates (GRCh38): 11:61,964,285-61,967,634 (from NCBI)
| Location | Phenotype |
Phenotype MIM number |
Inheritance |
Phenotype mapping key |
|---|---|---|---|---|
| 11q12.3 | ?Hemochromatosis, type 5 | 615517 | Autosomal dominant | 3 |
| Neurodegeneration with brain iron accumulation 9 | 620669 | Autosomal dominant | 3 |
The iron storage protein ferritin is a complex of 24 ferritin light chain (FTL; 134790) and ferritin heavy chain (FTH1) subunits in ratios that vary in different cell types. FTH subunits exhibit ferroxidase activity, converting Fe(2+) to Fe(3+), so that iron may be stored in the ferritin mineral core, which prevents undesirable reactions of Fe(2+) with oxygen. FTL subunits are devoid of catalytic activity but are thought to facilitate nucleation and mineralization of the iron center (summary by Sammarco et al., 2008).
Murray et al. (1987) demonstrated that the rat has a single H-subunit gene. Near the cap region of the 5-prime untranslated region, this subunit shows a 28-nucleotide sequence that is almost totally conserved in human, bullfrog, and chicken H mRNA and is also faithfully represented in the rat and human L-subunit mRNAs. This sequence is a prime candidate for involvement in the known translational regulation of both subunits by iron, which induces synthesis of the subunits by causing latent mRNAs present in the cytosol to become polyribosome-associated and translationally active.
Hentze et al. (1986) isolated a genomic phage clone containing a full-length copy of the gene for ferritin heavy chain. The functionality of the gene was demonstrated by the fact that both transient transfectants and stable transformants of mouse fibroblasts actively transcribed human ferritin heavy-chain mRNA.
Hentze et al. (1986) determined that the FTH1 gene consists of 4 exons and spans approximately 3 kb.
From genomic analysis, using a cDNA clone, Boyd et al. (1984) concluded that the ferritin heavy chains are either encoded by a multigene family or that the gene has an unusually large number of exons.
Faniello et al. (2006) summarized the major regulatory elements of the FTH1 gene. They noted that the promoter region of FTH1 spans approximately 150 bp upstream from the transcription start site. The promoter has an A box at position -132 and a B box at position -62. The A box is a canonical GC box that is recognized by SP1 (189906). The B box is an inverted CAAT box that is recognized by the B box-binding factor (Bbf), a complex that contains the trimeric transcription factor NFY (see NFYB, 189904), EP300 (602700), and P/CAF (KAT2B; 602303).
By study of hamster-human and mouse-human hybrid cells, some with translocations involving chromosome 19, Worwood et al. (1985) concluded that light subunits of ferritin (rich in human spleen ferritin) are coded by a gene in segment 19q13.3-qter and that the gene for the heavy subunit (rich in human heart ferritin) is located on chromosome 11.
By study of DNA extracted from rodent-human cell hybrids, Cragg et al. (1985) found sequences homologous to a probe for the H subunit of human ferritin on at least 8 chromosomes: 1, 2, 3, 6p21-6cen, 11, 14, 20, and Xq23-Xqter. Only the gene on chromosome 11 appeared to be expressed in these hybrids.
Hentze et al. (1986) assigned the human FTH1 gene to chromosome 11 by analysis of genomic DNA from rodent-human cell hybrids.
Gatti et al. (1987) concluded that the heavy-subunit family includes 15 to 20 genes or pseudogenes and that the light-subunit family includes at least 3 genes. They confirmed and extended the chromosomal localization of the heavy-subunit 'genes' to chromosomes 1-6, 8, 9, 11, 13, 14, 17, and X. They identified and characterized a BamHI RFLP of FTH located on chromosome 3. Two alleles were identified and the polymorphic information content was calculated to be 0.34. Gatti et al. (1987) discussed the possibility that gene-family probes that hybridize to many discrete members of dispersed gene families might be useful in conjunction with pulsed- or inverted-field gels to screen a large number of specific genomic regions for microdeletions.
Using in situ hybridization, Yachou et al. (1991) demonstrated that mouse ferritin H-related sequences map to murine chromosomes 3, 6, and 19. Syntenic homology suggested that the chromosome 19 sequence corresponds to the structural H gene. Yachou et al. (1991) demonstrated that ferritin H represents a multigene family, that it is polymorphic, and that there is a single multiallelic functional gene on mouse chromosome 19 in a region of conserved synteny with human chromosome 11q. Richard et al. (1991) described a high resolution radiation hybrid map of 11q12-q13, which placed FTH1 between the PGA cluster (see 169710) and COX8 (123870). In pulsed field gel electrophoresis studies, Gailani et al. (1991) found that C1NH (606860) and FTH1 lie in the same DNA fragment that is less than or equal to 48 kb. Papadopoulos et al. (1992) identified a second ferritin heavy chain gene on chromosome 11, FTH2, which in situ hybridization indicated lies close to FTH1. Whether this is a functional gene remained to be determined.
Courseaux et al. (1996) used a combination of methods to refine maps of an approximately 5-Mb region of 11q13. They proposed the following gene order: cen--PGA--FTH1--UGB--AHNAK--ROM1--MDU1--CHRM1--COX8--EMK1--FKBP2--PLCB3--[PYGM, ZFM1]--FAU--CAPN1--[MLK3, RELA]--FOSL1--SEA--CFL1--tel.
Wu et al. (1999) demonstrated that c-myc (190080) represses the expression of ferritin-H.
Pham et al. (2004) identified FTH1, the primary iron storage factor, as an essential mediator of the antioxidant and protective activities of nuclear factor kappa-B (NFKB; see 164011). They determined that FTH1 is induced downstream of NFKB and is required to prevent sustained JNK (see 601158) activation and, thereby, apoptosis triggered by tumor necrosis factor (TNF; 191160). FTH1-mediated inhibition of JNK signaling depended on suppressing reactive oxygen species accumulation and was achieved through iron sequestration.
Human ferritins expressed in yeast normally contain little iron, which led Shi et al. (2008) to hypothesize that yeast, which do not express ferritins, might also lack the requisite iron chaperones needed for delivery of iron to ferritin. In a genetic screen to identify human genes that, when expressed in yeast, could increase the amount of iron loaded into ferritin, Shi et al. (2008) identified poly(rC) binding protein-1 (PCBP1; 601209). PCBP1 bound to ferritin in vivo and bound iron and facilitated iron loading into ferritin in vitro. Depletion of PCBP1 in human cells inhibited ferritin iron loading and increased cytosolic iron pools. Thus, Shi et al. (2008) concluded that PCBP1 can function as a cytosolic iron chaperone in the delivery of iron to ferritin.
Ferritin made up of only FHC can circulate and bind specifically and saturably to various cell types. Using expression cloning and protein interaction assays, Li et al. (2010) found that transferrin receptor-1 (TFR1; 190010) bound directly to FHC, but not FTL. Binding of FHC to TFR1 on the cell surface resulted in endocytosis and transfer of FHC to endosomes and lysosomes. The FHC-TFR1 interaction was partially inhibited by diferric transferrin, but it was not inhibited by HFE (613609). Inhibitory antibodies that blocked binding of FHC to TFR1 revealed that TFR1 accounted for most binding of FHC to cells, including mitogen-activated lymphocytes and circulating reticulocytes.
Mancias et al. (2014) used quantitative proteomics to identify a cohort of novel and known autophagosome-enriched proteins, including cargo receptors, in human cells. Like known cargo receptors, nuclear receptor coactivator-4 (NCOA4; 601984) was highly enriched in autophagosomes, and associated with autophagy-8 (ATG8)-related proteins that recruit cargo-receptor complexes into autophagosomes (see, e.g., GABARAPL2, 607452). Unbiased identification of NCOA4-associated proteins revealed FTH1 and ferritin light chain (FTL; 134790), components of an iron-filled cage structure that protects cells from reactive iron species but is degraded via autophagy to release iron. Mancias et al. (2014) found that delivery of ferritin to lysosomes required NCOA4, and an inability of NCOA4-deficient cells to degrade ferritin led to decreased bioavailable intracellular iron. Mancias et al. (2014) concluded that their work identified NCOA4 as a selective cargo receptor for autophagic turnover of ferritin (ferritinophagy), which is critical for iron homeostasis, and provided a resource for further dissection of autophagosomal cargo-receptor connectivity.
For a review of the ferritins, including their molecular properties, iron storage function, and cellular regulation, see Harrison and Arosio (1996).
Hemochromatosis 5
Synthesis of both the H- and L-ferritin subunits is controlled by a common cytosolic protein, iron regulatory protein (IRP), which binds to the iron-responsive element (IRE) in the 5-prime untranslated region of the H- and L-ferritin mRNAs (Leibold and Munro, 1988; Eisenstein, 2000). In 4 of 7 members of a Japanese family affected by dominantly inherited iron overload consistent with hemochromatosis (HFE5; 615517), Kato et al. (2001) identified a heterozygous single point mutation (134770.0001) in the IRE motif of H-ferritin mRNA. Gel-shift mobility assay and Scatchard-plot analysis revealed that a mutated IRE probe had a higher binding affinity to IRP than did the wildtype probe. When mutated H subunit was overexpressed in COS-1 cells, suppression of H-subunit synthesis and of the increment of radiolabeled iron uptake were observed. These data suggested that the point mutation in the IRE of H-subunit is responsible for tissue iron deposition and is a novel cause of hereditary iron overload, most likely related to impairment of the ferroxidase activity generated by H subunit.
Neurodegeneration With Brain Iron Accumulation 9
In 5 unrelated patients with neurodegeneration with brain iron accumulation-9 (NBIA9; 620669), Shieh et al. (2023) identified de novo heterozygous truncating mutations in the last exon (exon 4) of the FTH1 gene. One patient carried an S164X mutation (134770.0002) and the 4 other patients carried an F171X mutation (134770.0003). The mutations, which were found by whole-exome sequencing, were not present in the gnomAD database. Studies of patient fibroblasts showed that both mutations escaped nonsense-mediated mRNA decay and produced a C-terminally truncated protein with a likely dominant-negative effect. Molecular modeling predicted that the mutations would disrupt the ferritin E-helix, alter the pore region that is important for iron retention, and thus likely diminish iron-storage capacity. Patient fibroblasts showed elevated FTH1 and FTL (134790) protein levels, abnormal accumulation of cytoplasmic ferritin aggregates, increased susceptibility to iron accumulation, and evidence of increased oxidation and oxidative stress compared to controls. Targeted knockdown of the mutant S164X FTH1 transcript using antisense oligonucleotides (ASOs) in vitro partially rescued the abnormal cellular phenotype.
Polymorphisms
Using single-strand conformation polymorphism analysis, Faniello et al. (2006) analyzed peripheral blood lymphocyte DNA fragments from the promoter region of the FTH1 gene from 100 healthy Southern Italian individuals. They identified 3 unrelated individuals carrying 1 allele of a -69G-T SNP. Two of these individuals were married, and their descendant carried T on both alleles. Reporter gene assays showed reduced expression from the ferritin promoter in samples with the T allele compared with the G allele. The -69G allele was significantly more efficient in competing with the -69T allele for binding to the Bbf complex in cross-competition assays. Real-time PCR analysis of -69TT, -69GT, and -69GG samples revealed a dose-dependent decrease in steady-state amount of H-ferritin mRNA with increasing dose of the T allele.
Ferreira et al. (2000) disrupted the H-ferritin gene in mice by homologous recombination. Heterozygous mice were healthy, fertile, and did not differ significantly from their control littermates. However, Fth -/- embryos died between 3.5 and 9.5 days of development, suggesting that there is no functional redundancy between the 2 ferritin subunits and that, in the absence of H subunits, L-ferritin homopolymers are not able to maintain iron in a bioavailable and nontoxic form. The pattern of expression of the wildtype Fth gene in 9.5-day embryos is restricted to the developing heart and central nervous system.
The results of an analysis of H-ferritin knockout mice by Ferreira et al. (2001) raised the possibility that reduced H-ferritin expression may be responsible for unexplained human cases of hyperferritinemia in the absence of iron overload where the hereditary hyperferritinemia-cataract syndrome (600886) has been excluded. Heterozygous H-ferritin knockout mice had slightly elevated tissue L-ferritin content and 7- to 10-fold more L-ferritin in the serum than normal mice, but their serum iron remained unchanged. H-ferritin synthesis from the remaining allele was not upregulated.
Hasegawa et al. (2013) created transgenic mice expressing human H-ferritin (HF-tg). HF-tg mice were viable and reproduced normally, but they exhibited growth retardation and a temporary hairless phenotype. HF-tg mice eventually achieved normal weight, and their serum iron concentration and blood parameters, such as hemoglobin and red blood cell counts, were comparable to wildtype. Temporary hair loss in HF-tg mice began at 3 to 5 weeks of age, with loss of coat hair on the trunk, but not the head or face. Although initial hair development was normal and epidermal differentiation was largely unaltered, HF-tg skin showed hyperplasia with hyperkeratosis, dilated hair follicles, bended hair shafts, and keratinous debris during the hairless period, which lasted approximately 1 to 2 weeks.
Ferritin of liver and spleen contains mostly L subunits. Antibodies to liver or spleen ferritin are not likely to detect ferritin containing only H subunits. This may explain the conclusion of Caskey et al. (1983) that both subunits are coded by chromosome 19. Heart ferritin contains a preponderance of H subunits. (According to Costanzo et al. (1986), the 2 types of apoferritin subunits were designated H and L for heart and liver, respectively.) Contrary to the earlier impression that both the heavy and light chains of ferritin are encoded by chromosome 19, McGill et al. (1984) by in situ hybridization localized the L gene to 19 (as previously) and the H gene to 1p.
Using a heavy chain probe of Boyd et al. (1984), Youssoufian et al. (1988) concluded that one FTH gene is in the segment 1q32.3-q42.3. In a patient with deletion of this segment, a reduced hybridization signal with the FTH probe was observed. The gene may be nonfunctional (i.e., a pseudogene).
Kato et al. (2001) studied a Japanese family segregating autosomal dominant primary iron overload (HFE5; 615517). The proband was a 56-year-old woman who was incidentally found to have iron overload. A brother, 2 sisters, and a daughter of 1 of the sisters were affected. The father of the 3 affected sibs was deceased; the mother was apparently unaffected. After excluding other causes of iron overload, they sequenced H- and L-ferritin cDNAs. In the sequence of H subunit mRNA, they found a heterozygous single A-to-U conversion at position 49 from the transcription start site, in the second residue of the 5-base IRE loop sequence. The mutation was found in the genomic DNA of the 4 affected members of the family but not in 42 unrelated normal subjects.
In a 13-year-old girl of Indian descent (P1) with neurodegeneration with brain iron accumulation-9 (NBIA9; 620669), Shieh et al. (2023) identified a de novo heterozygous 4-bp duplication (c.487_490dupGAAT, NM_002032) in the last exon (exon 4) of the FTH1 gene, resulting in premature termination (ser164 to ter, S164X) in the C terminus, deleting the E-helix region. The mutation, which was found by whole-exome sequencing, was not present in the gnomAD database. Patient fibroblasts showed mildly decreased FTH1 mRNA compared to controls, although mutant-specific transcripts were detectable, indicating escape from nonsense-mediated mRNA decay. Patient fibroblasts showed increased protein levels of both FTH1 and FTL (134790) compared to controls. Patient fibroblasts showed increased iron accumulation compared to controls at 7 days after iron exposure; patient cells also showed increased levels of oxidized proteins and peroxidized lipids, suggesting that the mutation resulted in increased susceptibility to oxidative stress. Molecular modeling predicted that the mutation would disrupt the ferritin E-helix, alter the pore region that is important for iron retention, and thus likely diminish iron-storage capacity. The findings were consistent with a dominant-negative effect. Targeted knockdown of the mutant FTH1 transcript using antisense oligonucleotides (ASOs) in vitro partially rescued the abnormal cellular phenotype. The patient also carried a heterozygous missense variant of uncertain significance (R253W) in the TOE1 gene (613931) that was inherited from the unaffected father.
In 4 unrelated patients (P2-P5) with neurodegeneration with brain iron accumulation-9 (NBIA9; 620669), Shieh et al. (2023) identified a de novo heterozygous 2-bp deletion (c.512_513delTT, NM_002032) in the last exon (exon 4) of the FTH1 gene, resulting in premature termination (phe171 to ter, F171X) in the E-helix region of the C terminus. The mutation, which was found by whole-exome sequencing, was not present in the gnomAD database. Patient fibroblasts showed mildly decreased FTH1 mRNA compared to controls, although mutant-specific transcripts were detectable, indicating escape from nonsense-mediated mRNA decay. Patient cells showed increased protein levels of both FTH1 and FTL (134790) compared to controls. Immunostaining of patient cells showed the presence of abnormal FTH1-positive cytoplasmic aggregates that were not observed in control cells, and these aggregates increased in the presence of iron. Although iron content did not differ between patient cells and controls up to 7 days after iron exposure, patient fibroblasts showed increased levels of oxidized proteins and peroxidized lipids, suggesting that the mutation resulted in increased susceptibility to oxidative stress. Molecular modeling predicted that the mutation would disrupt the ferritin E-helix, alter the pore region that is important for iron retention, and thus likely diminish iron-storage capacity. The findings were consistent with a dominant-negative effect.
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