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ERYTHROFERRONE; ERFE

ERYTHROFERRONE; ERFE

Alternative titles; symbolsFAMILY WITH SEQUENCE SIMILARITY 132, MEMBER B; FAM132BC1q- AND TUMOR NECROSIS FACTOR-RELATED PROTEIN 15; CIQTNF15; CTRP15MYONECTINHGNC...

Alternative titles; symbols

  • FAMILY WITH SEQUENCE SIMILARITY 132, MEMBER B; FAM132B
  • C1q- AND TUMOR NECROSIS FACTOR-RELATED PROTEIN 15; CIQTNF15; CTRP15
  • MYONECTIN

HGNC Approved Gene Symbol: ERFE

Cytogenetic location: 2q37.3 Genomic coordinates (GRCh38): 2:238,158,969-238,168,889 (from NCBI)

▼ Description
ERFE is a stress hormone that elevates erythropoiesis following blood loss (Kautz et al., 2014).

▼ Cloning and Expression
Seldin et al. (2012) cloned mouse Fam132b, which they called myonectin. The deduced 340-amino acid protein has an N-terminal signal sequence, followed by N-terminal domain-1 (NTD1), a short collagen domain with 6 gly-X-Y repeats, NTD2, and a C-terminal C1q (see 120550)- and TNF (191160)-like domain. It also has 4 cysteines and 4 potential N-glycosylation sites. Highest myonectin expression was detected in mouse skeletal muscle, with much lower expression in heart, brain, lung, kidney, eye, and smooth muscle, and little to no expression in other tissues examined. Myonectin expression was higher in soleus, a predominantly slow-twitch, oxidative muscle fiber type, than in plantaris, a predominantly fast-twitch, glycolytic muscle fiber type. Glycosidase treatment reduced the apparent molecular mass of myonectin, suggesting that is glycosylated.

By 5-prime RACE of human fetal liver erythroblasts, Kautz et al. (2014) cloned human ERFE. The deduced 354-amino acid protein has a C-terminal TNF-like domain. ERFE shares 71% amino acid identity with the 340-amino acid mouse protein, with highest identity in the C-terminal region. Quantitative RT-PCR detected Erfe expression in mouse colon, duodenum, testis, muscle, and bone marrow, with lower expression in brain, eye, heart, lung, and thymus, and little to no expression in other tissues examined. Erfe was also expressed in mouse bone marrow erythroid precursors.

▼ Mapping
Hartz (2013) mapped the FAM132B gene to chromosome 2q37.3 based on an alignment of the FAM132B sequence (GenBank AK094353) with the genomic sequence (GRCh37).

Seldin et al. (2012) mapped the mouse Fam132b gene to chromosome 1.

▼ Gene Function
Skeletal muscles secrete cytokines and growth factors (collectively termed myokines) that can act as autocrine, paracrine, and/or endocrine factors. Seldin et al. (2012) found that mouse myonectin formed dimers via intermolecular disulfide bonds following expression in HEK293 cells. Myonectin also formed heterodimers with CTRP2 (ADIPOQ; 605441), and CTRP12 (C1QTNF12; 616593), and to a lesser extent with CTRP5 (C1QTNF5; 608752) and CTRP10 (C1QL2; 614330), but not with other CTRPs tested. Expression and secretion of myonectin in mice was highly responsive to acute nutritional and metabolic changes (e.g., fasting/refeeding cycles and exercise), as well as chronic alteration in the energy state of the animals (e.g., diet-induced obesity). Increased intracellular cAMP or calcium increased myonectin expression in mouse myotubes in culture, but insulin (INS; 176730) and 5-aminoimidazole-4-carboxamide ribonucleoside, an AMP-activated protein kinase activator, had no effect. In starved myotubes, addition of glucose or free fatty acids induced myonectin mRNA expression. Similar results were obtained with overnight-fasted mice gavaged with a bolus of glucose or lipid. Stimulation of adipocytes with a combination of insulin and myonectin did not show additive effects, and both enhanced expression of genes involved in lipid metabolism, suggesting that insulin and myonectin function in the same metabolic pathway.

Using quantitative RT-PCR, Kautz et al. (2014) found that expression of Erfe was induced in mouse bone marrow and spleen by phlebotomy or treatment with recombinant human erythropoietin (EPO; 133170). Erfe expression was also induced by phlebotomy in mouse erythroid precursors. The authors identified multiple putative Stat5 (STAT5A; 601511)-binding sites in the ERFE promoter region, and inhibition of Stat5 inhibited EPO-stimulated Erfe mRNA expression. Injection of mice with recombinant mouse Erfe or overexpression of Erfe via a lentivirus vector reduced hepcidin (HAMP; 606464) mRNA, suggesting that Erfe enhances erythropoiesis in part by increasing iron availability. Treatment of primary hepatocytes with ERFE confirmed that ERFE directly suppressed hepcidin activity.

▼ Animal Model
Kautz et al. (2014) reported that Fam132b -/- mice were viable and fertile and showed no abnormal phenotype. Fam132b -/- newborns showed mildly delayed hemoglobin and mean corpuscular hemoglobin concentrations compared with age-matched controls. After phlebotomy, Fam132b -/- mice failed to suppress hepcidin, in contrast with wildtype mice, and exhibited delayed recovery from hemorrhage. Fam132b +/- mice presented an intermediate response.

Tags: 2q37.3