Work

Endoplasmic reticulum stress controls iron metabolism through TMPRSS6 repression and hepcidin mRNA stabilization by RNA-binding protein HuR

Year: 2020
Type: article
Abstract: The liver hormone hepcidin controls the main inflows of iron into plasma by binding to and inducing the degradation or the occlusion of the iron export activity of ferroportin, the only known cellular exporter of iron. When hepcidin concentrations are high, iron is trapped in enterocytes of the duodenum, hepatocytes, and macrophages. Hepcidin production by the hepatocytes is induced by a number of stimuli, most notably iron, through the BMP-SMAD signaling pathway, and inflammatory signals, through the IL-6/ STAT3 signaling axis. In addition, hepcidin has also been reported to respond to intracellular stress, namely endoplasmic reticulum (ER) stress which is involved in a number of pathophysiological states, including the inflammatory response, nutrient disorders and viral infection. A previous study has suggested that hepcidin induction by ER stress is controlled by the BMP-SMAD pathway,5 but the exact mechanism is still uncertain
Language: English
Subfield: Hematology
Field: Medicine
Open Access status: gold
Estimated APC paid: $379
OpenAlex ID: W3043839133
FWCI: 1.549
Cites: 16
Cited by: 12
Related to: 10