2012
DOI: 10.1182/blood-2011-07-366690
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Pretreatment with CO-releasing molecules suppresses hepcidin expression during inflammation and endoplasmic reticulum stress through inhibition of the STAT3 and CREBH pathways

Abstract: The circulating peptide hormone hepcidin maintains systemic iron homeostasis. Hepcidin production increases during inflammation and as a result of endoplasmic reticulum (ER) stress. Elevated hepcidin levels decrease dietary iron absorption and promote iron sequestration in reticuloendothelial macrophages. Furthermore, increased plasma hepcidin levels cause hypoferremia and the anemia associated with chronic diseases. The signal transduction pathways that regulate hepcidin during inflammation and ER stress incl… Show more

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Cited by 38 publications
(31 citation statements)
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“…The cyclic adenosine monophosphate (cAMP) response element binding protein 3-like 3, CREB3L3 (also known as CREBH), an endoplasmic reticulum (ER) stress-associated liver-specific transcription factor 34 , up-regulates hepcidin transcription in response to exogenous and endogenous ER stressors leading to iron retention in vivo 30 (Figure 1). Hepcidin induction by CREB3L3 has been then confirmed by other studies in similar settings [35][36][37][38] . Because ER stress has been involved in a number of pathophysiological states, including inflammatory response, nutrient disorders and viral infection, it is anticipated that ER stress-driven hepcidin stimulation may cause systemic or intrahepatic iron retention in a variety of iron-unrelated disorders and thereby contribute to the pathogenesis of the underlying disease, including metabolic disorders associated with insulin resistance and activated gluconeogenesis (such as diabetes, obesity and non-alcoholic fatty liver disease, NADFD) [39][40][41][42] .…”
Section: Endoplasmic Reticulum (Er) Stressmentioning
confidence: 66%
“…The cyclic adenosine monophosphate (cAMP) response element binding protein 3-like 3, CREB3L3 (also known as CREBH), an endoplasmic reticulum (ER) stress-associated liver-specific transcription factor 34 , up-regulates hepcidin transcription in response to exogenous and endogenous ER stressors leading to iron retention in vivo 30 (Figure 1). Hepcidin induction by CREB3L3 has been then confirmed by other studies in similar settings [35][36][37][38] . Because ER stress has been involved in a number of pathophysiological states, including inflammatory response, nutrient disorders and viral infection, it is anticipated that ER stress-driven hepcidin stimulation may cause systemic or intrahepatic iron retention in a variety of iron-unrelated disorders and thereby contribute to the pathogenesis of the underlying disease, including metabolic disorders associated with insulin resistance and activated gluconeogenesis (such as diabetes, obesity and non-alcoholic fatty liver disease, NADFD) [39][40][41][42] .…”
Section: Endoplasmic Reticulum (Er) Stressmentioning
confidence: 66%
“…It has been shown that CREBH is activated by ER stress and regulates the expression of hepcidin and proinfl ammatory and acute phase response genes, linking ER stress to infl ammation and iron metabolism ( 6,17,50 ). However, subsequent studies by other investigators failed to demonstrate the activation of CREBH processing by ER stress ( 10,11 ).…”
Section: Discussionmentioning
confidence: 87%
“…We cannot exclude the possibility that other uncharacterized mechanisms contribute to CO-dependent reversal of leptin resistance, and this warrants further investigation. Recently, we (24) reported that CORM-2 treatment decreased the STAT3 phosphorylation induced by IL-6 in the hepatoma cell line HepG2. We are now reporting that CORM-2 treatment increased the STAT3 phophorylation induced by leptin in a neuronal cell line (SK-N-AS).…”
Section: Discussionmentioning
confidence: 99%