Journal
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume 22, Issue 5, Pages -Publisher
MDPI
DOI: 10.3390/ijms22052650
Keywords
hepcidin; transferrin receptor; neogenin; Hjv; Tmprss6; Tfrc; Tfr2
Funding
- GACR [18-13103S]
- Charles University in Prague [PROGRES Q26]
- Ministry of Education, Youth and Sports of CR within the National Sustainability Program II [LQ1604]
- project BIOCEV [CZ.1.05/1.1.00/02.0109]
- Czech Academy of Sciences [RVO: 86652036]
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The study reveals a complex interaction between Matriptase-2 and Hemojuvelin, where the absence of one protein leads to decreased content of the other. Feeding experimental diets to mice can affect iron metabolism, and feeding iron-deficient diet can trigger stress erythropoiesis.
Matriptase-2, a serine protease expressed in hepatocytes, is a negative regulator of hepcidin expression. The purpose of the study was to investigate the interaction of matriptase-2 with hemojuvelin protein in vivo. Mice lacking the matriptase-2 proteolytic activity (mask mice) display decreased content of hemojuvelin protein. Vice versa, the absence of hemojuvelin results in decreased liver content of matriptase-2, indicating that the two proteins interact. To further characterize the role of matriptase-2, we investigated iron metabolism in mask mice fed experimental diets. Administration of iron-enriched diet increased liver iron stores as well as hepcidin expression. Treatment of iron-overloaded mask mice with erythropoietin increased hemoglobin and hematocrit, indicating that the response to erythropoietin is intact in mask mice. Feeding of an iron-deficient diet to mask mice significantly increased spleen weight as well as the splenic content of erythroferrone and transferrin receptor proteins, indicating stress erythropoiesis. Liver hepcidin expression was decreased; expression of Id1 was not changed. Overall, the results suggest a complex interaction between matriptase-2 and hemojuvelin, and demonstrate that hepcidin can to some extent be regulated even in the absence of matriptase-2 proteolytic activity.
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