Abstract
Hepcidin is an iron regulatory protein mainly synthesized by the liver. Hepatocyte production of hepcidin is responsible for serum hepcidin, is responsive to body iron stores, and is critical for maintaining iron homeostasis. Monocytes and macrophages also express hepcidin, and in contrast to the liver, hepcidin expression is primarily regulated by inflammatory mediators and infectious agents. Monocyte and macrophage hepcidin is likely to be more important on a local rather than systemic level, contributes to host defense and may modulate inflammatory processes. This review summarizes recent findings and hypotheses on the relationship of hepcidin to the mononuclear phagocyte system.
©2013 by Walter de Gruyter Berlin Boston
Articles in the same Issue
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- Masthead
- Guest Editorial
- Highlight: The physiology and dynamics of cellular microcompartments
- Highlight: The Physiology and Dynamics of Cellular Microcompartments
- Cellular microcompartments constitute general suborganellar functional units in cells
- Dynamics of bioenergetic microcompartments
- Microcompartments within the yeast plasma membrane
- Plant cell microcompartments: a redox-signaling perspective
- Microcompartments in the Drosophila heart and the mammalian brain: general features and common principles
- Minireviews
- Beyond anemia: hepcidin, monocytes and inflammation
- Melanoma resistance to photodynamic therapy: new insights
- The biosynthesis of caprazamycins and related liponucleoside antibiotics: new insights
- cCMP, cUMP, cTMP, cIMP and cXMP as possible second messengers: Development of a hypothesis based on studies with soluble guanylyl cyclase α1β1
- Research Articles/Short Communications
- Protein Structure and Function
- Degradation of channelopsin-2 in the absence of retinal and degradation resistance in certain mutants
- Cell Biology and Signaling
- Possible role of a septin, SEPT1, in spreading in squamous cell carcinoma DJM-1 cells
- Proteolysis
- ADAMTS: Novel proteases expressed by activated mast cells
- The proinflammatory cytokines interleukin-1α and tumor necrosis factor α promote the expression and secretion of proteolytically active cathepsin S from human chondrocytes
Articles in the same Issue
- Masthead
- Masthead
- Guest Editorial
- Highlight: The physiology and dynamics of cellular microcompartments
- Highlight: The Physiology and Dynamics of Cellular Microcompartments
- Cellular microcompartments constitute general suborganellar functional units in cells
- Dynamics of bioenergetic microcompartments
- Microcompartments within the yeast plasma membrane
- Plant cell microcompartments: a redox-signaling perspective
- Microcompartments in the Drosophila heart and the mammalian brain: general features and common principles
- Minireviews
- Beyond anemia: hepcidin, monocytes and inflammation
- Melanoma resistance to photodynamic therapy: new insights
- The biosynthesis of caprazamycins and related liponucleoside antibiotics: new insights
- cCMP, cUMP, cTMP, cIMP and cXMP as possible second messengers: Development of a hypothesis based on studies with soluble guanylyl cyclase α1β1
- Research Articles/Short Communications
- Protein Structure and Function
- Degradation of channelopsin-2 in the absence of retinal and degradation resistance in certain mutants
- Cell Biology and Signaling
- Possible role of a septin, SEPT1, in spreading in squamous cell carcinoma DJM-1 cells
- Proteolysis
- ADAMTS: Novel proteases expressed by activated mast cells
- The proinflammatory cytokines interleukin-1α and tumor necrosis factor α promote the expression and secretion of proteolytically active cathepsin S from human chondrocytes