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Table 1 Expression, regulation and action of brain hepcidin

From: Hepcidin, an emerging and important player in brain iron homeostasis

Methods Study conditions Main results References
Expression measured with RT-PCR from human tissues Physiological conditions mRNA of hepcidin present in brain tissue Krause et al. [31]
Expression measured with RT-PCR from human tissues Physiological conditions mRNA of hepcidin present in spinal cord Pigeon et al. [1]
Expression measured with RT-PCR, in situ hybridization, immunohistochemistry in murine brain Physiological conditions Hepcidin expression detected with RT-PCR and in situ hybridization
Immunohistochemistry showed a wide distribution of the protein across the brain tissue compared to narrow distribution of mRNA of hepcidin measured by in situ hybridization
Zechel et al. [32]
Expression measured with RT-PCR and in situ hybridization, while protein levels were measured with western blotting and immunohistochemistry (rat brain samples) Physiological conditions Hepcidin expression was low with highest signal detected in choroidal plexus and to a lesser extent in blood vessels
Protein levels were abundant, especially in blood vessels, choroidal plexus and cortical astrocytes in close proximity to blood vessels
Raha-Chowdhury et al. [33]
Protein levels measured with western blotting and immunohistochemistry (mouse brain samples) Physiological conditions Abundant protein levels of hepcidin across the brain tissue Raha et al. [35]
Expression measured with RT-PCR, while protein levels were measured with western blotting (mouse brain and cell cultures) Physiological and stimulated conditions Hepcidin expression was abundant but still in low levels
Hepcidin induced FPN downregulation in mouse brain
Hepcidin decreases iron-release in cultured neurons due to FPN downregulation
Wang et al. [34]
Expression measured with RT-PCR (human brain samples) Physiological conditions HJV mRNA was not observed
Hepcidin, neogenin, TFR2, HFE mRNA was present
Hänninen et al. [69]
Expression measured with RT-PCR, while protein levels were measured with western blotting (mouse brain) Different stimulated conditions TFR2 loss does not affect brain hepcidin protein levels Pellegrino et al. [73]
Expression measured with RT-PCR, while protein levels were measured with western blotting and immunohistochemistry (rat cultured cells) Inflammation Microglia react to LPS by producing IL-6
Astrocytes produce hepcidin in response to IL-6 secreted by microglia
Hepcidin increases iron-load in neurons
Inflammation has hepcidin-independent actions in reducing iron-export and enhancing iron-import in neurons
You et al. [54]
Expression measured with RT-PCR, while protein levels were measured by western blotting and immunohistochemistry (rat cultured cells) Inflammation and iron-stimulation TNF-α, IL-6 and LPS increase cellular iron content in neurons
TNF-α, IL-6 and LPS do not affect cellular iron content in astrocytes
TNF-α, IL-6 and LPS increase cellular iron content in microglia
TNF-α, IL-6 and LPS cause DMT1↑ and FPN↓ (protein levels) in neurons
TNF-α, IL-6 and LPS cause DMT1↑ (protein levels) in astrocytes
TNF-α, IL-6 and LPS cause DMT1↑ (protein levels) in microglia
TNF-α, IL-6 and LPS cause DMT1↑ (mRNA) in neurons
TNF-α, IL-6 and LPS cause DMT1↑ (mRNA), while LPS causes FPN↓ in astrocytes
TNF-α, IL-6 and LPS cause DMT1↑ (mRNA), while TNF-α and LPS cause FPN↓ (mRNA) in microglia
TNF-α, IL-6, LPS and FeNTA cause hepcidin↑(mRNA) in astrocytes and microglia but not in neurons
Urrutia et al. [56]
Protein levels measured with western blotting and ELISA in rat cultured cells Inflammation LPS increases hepcidin expression in rat brain
LPS increases IL-6 production from microglia
IL-6 from microglia induces hepcidin production in neurons (via STAT3 pathway)
No observed hepcidin↑ in neurons without co-cultured microglia due to LPS stimulation
Qian et al. [55]
Expression measured with RT-PCR, while protein levels were measured with western blotting and immunohistochemistry (rat brain and cultured cells) Iron-overload Hepcidin↑ in rat brain and cultured cells
Hepcidin mRNA↑ in cultured neurons in response to iron-overload
Sun et al. [64]
Expression measured with RT-PCR, while protein levels were measured with western blotting and ELISA in rat brain and cultured cells Iron-overload Hepcidin reduces iron-load in rat brains
Hepcidin induces TFR1↓, DMT1↓ and FPN↓ in BMEC
Hepcidin induces TFR1↓, DMT1↓ and FPN↓ in neurons
Du et al. [59]
Expression measured with RT-PCR, while protein levels were measured with western blotting and ELISA in rat brain and cultured cells Physiological conditions Hepcidin induces TFR1↓, DMT1↓ and FPN↓ in astrocytes
TFR1↓ is realized through AMPK pathway
Du et al. [58]
Expression measured by RT-PCR, while levels of chemicals were measured with ELISA Inflammation induced by Aβ aggregates Hepcidin pre-treatment reduces expression and secretion of IL-6 and TNF-α in astrocytes and microglia Urrutia et al. [65]
  1. amyloid beta, AMPK AMP-activated protein kinase, BMEC brain microvascular endothelial cells, DMT1 divalent metal transporter 1, ELISA enzyme-linked immunosorbent assay, FeNTA ferric nitrilotriacetate, FPN ferroportin, HFE hemochromatosis protein, HJV hemojuvelin, IL-6 interleukin 6, LPS lipopolysaccharide, RT-PCR reverse transcription polymerase chain reaction, STAT3 signal transducer and activator of transcription 3, TFR transferrin receptor, TNF-α tumor necrosis factor-alpha