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Hepcidin antimicrobial peptide

Hepcidin, hepcidin-25
The product encoded by this gene is involved in the maintenance of iron homeostasis, and it is necessary for the regulation of iron storage in macrophages, and for intestinal iron absorption. The preproprotein is post-translationally cleaved into mature peptides of 20, 22 and 25 amino acids, and these active peptides are rich in cysteines, which form intramolecular bonds that stabilize their beta-sheet structures. These peptides exhibit antimicrobial activity. Mutations in this gene cause hemochromatosis type 2B, also known as juvenile hemochromatosis, a disease caused by severe iron overload that results in cardiomyopathy, cirrhosis, and endocrine failure. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Transferrin, Interleukin-6, CAN, HAD, HFE
Papers on Hepcidin
Targeted disruption of hepcidin in the liver recapitulates the hemochromatotic phenotype.
Peyssonnaux et al., Paris, France. In Blood, Jul 2014
Hepcidin is a 25-amino-acid peptide demonstrated to be the iron regulatory hormone capable of blocking iron absorption from the duodenum and iron release from macrophages.
Hepcidin and the iron enigma in HCV infection.
Mamalaki et al., Athens, Greece. In Virulence, Jun 2014
Hepcidin is a 25-aa peptide, present in human serum and urine and represents the key peptide hormone, which modulates iron homeostasis in the body.
Turbot (Scophthalmus maximus) hepcidin-1 and hepcidin-2 possess antimicrobial activity and promote resistance against bacterial and viral infection.
Sun et al., Qingdao, China. In Fish Shellfish Immunol, May 2014
Hepcidin is an antimicrobial peptide and a regulator of iron homeostasis.
Modulation of hepcidin as therapy for primary and secondary iron overload disorders: preclinical models and approaches.
Fleming et al., Boston, United States. In Hematol Oncol Clin North Am, Apr 2014
In this article, the authors discuss new approaches to treating iron overload diseases using hepcidin mimetics or by modulating endogenous hepcidin expression.
Lipopolysaccharides Upregulate Hepcidin in Neuron via Microglia and the IL-6/STAT3 Signaling Pathway.
Ke et al., Shanghai, China. In Mol Neurobiol, Apr 2014
Our previous study demonstrated that lipopolysaccharides (LPS) can regulate expression of iron-regulatory peptide hepcidin; however, the mechanism is undefined.
Immunoassay-Based Serum Hepcidin Reference Range Measurements in Healthy Children: Differences Among Age Groups.
Kossiva et al., Athens, Greece. In J Clin Lab Anal, Apr 2014
BACKGROUND: Hepcidin is a peptide hormone that plays a key role in regulating iron absorption from the small intestine and body iron distribution.
A78: urine biomarkers role in predicting the future development of renal functional loss with lupus nephritis in children and adults.
Rovin et al., Cincinnati, United States. In Arthritis Rheumatol, Mar 2014
The biomarker candidates studies were liver-type fatty acid binding protein (L-FABP), albumin (Alb), monocyte chemoattractant protein 1 (MCP-1), Uromodulin, Transferrin and Hepcidin.
Iron status and the acute post-exercise hepcidin response in athletes.
Trinder et al., Australia. In Plos One, Dec 2013
Venous blood samples were collected pre-, post- and 3 h post-exercise, and were analysed for serum ferritin, iron, interleukin-6 (IL-6) and hepcidin-25.
Systemic iron homeostasis.
Ganz, In Physiol Rev, Oct 2013
The iron hormone hepcidin and its receptor and cellular iron exporter ferroportin control the major fluxes of iron into blood plasma: intestinal iron absorption, the delivery of recycled iron from macrophages, and the release of stored iron from hepatocytes.
Hepcidin and its role in inflammatory bowel disease.
Poniewierka et al., Wrocław, Poland. In Adv Clin Exp Med, Jul 2013
Hepcidin, discovered in the year 2000, is an endogenous peptide responsible for iron homeostasis.
Hepcidin and HFE protein: Iron metabolism as a target for the anemia of chronic kidney disease.
Valenti et al., Milano, Italy. In World J Nephrol, 2013
The anemia of chronic kidney disease and hemodialysis is characterized by chronic inflammation and release of cytokines, resulting in the upregulation of the iron hormone hepcidin, also increased by iron therapy and reduced glomerular filtration, with consequent reduction in iron absorption, recycling, and availability to the erythron.
Hepcidin and the iron-infection axis.
Prentice et al., Oxford, United Kingdom. In Science, 2012
Hepcidin, an antimicrobial-like peptide hormone, has emerged as the master regulator of iron metabolism.
Efficient oxidative folding and site-specific labeling of human hepcidin to study its interaction with receptor ferroportin.
Guo et al., Shanghai, China. In Febs J, 2012
labeled hepcidin was also a suitable tool to visualize internalization of overexpressed or even endogenously expressed ferroportin without tags
Induction of activin B by inflammatory stimuli up-regulates expression of the iron-regulatory peptide hepcidin through Smad1/5/8 signaling.
Coppin et al., Toulouse, France. In Blood, 2012
There is a dramatic induction of Inhbb mRNA, encoding the activin beta(B)-subunit, in liver challenged with lipopolysaccharide, slightly preceding an increase in Smad1/5/8 phosphorylation and Hamp mRNA.
Molecular mechanism of hepcidin-mediated ferroportin internalization requires ferroportin lysines, not tyrosines or JAK-STAT.
Arvedson et al., Thousand Oaks, United States. In Cell Metab, 2012
Hepcidin-induced ferroportin internalization did not require JAK2 or phosphorylation of ferroportin residues 302 and 303
Hepcidin-induced endocytosis of ferroportin is dependent on ferroportin ubiquitination.
Nemeth et al., Los Angeles, United States. In Cell Metab, 2012
ubiquitination is the functionally relevant signal for hepcidin-induced ferroportin endocytosis
[Hepcidin and diabetic anemia: is there an association?].
Elias et al., Israel. In Harefuah, 2012
Based on the results of this small study, hepcidin was not associated with diabetic anemia
Intestinal ferritin H is required for an accurate control of iron absorption.
Kühn et al., Lausanne, Switzerland. In Cell Metab, 2010
To maintain appropriate body iron levels, iron absorption by the proximal duodenum is thought to be controlled by hepcidin, a polypeptide secreted by hepatocytes in response to high serum iron.
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