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rdf:type |
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lifeskim:mentions |
umls-concept:C0287990,
umls-concept:C0441655,
umls-concept:C0450693,
umls-concept:C0851285,
umls-concept:C1258133,
umls-concept:C1418391,
umls-concept:C1418392,
umls-concept:C1538604,
umls-concept:C1549861,
umls-concept:C1556069,
umls-concept:C1709694,
umls-concept:C1741190
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pubmed:issue |
11
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pubmed:dateCreated |
2008-10-22
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pubmed:abstractText |
Hepcidin is an iron homoeostasis regulator peptide. Loss-of-function mutations cause juvenile haemochromatosis while its over-expression results in anaemia. However, the mechanism and function of preprohepcidin conversion to mature hepcidins (25, 22 and 20 amino acid C-terminal peptides) are not well known. After removal of the signal peptide, the first proteolytic cleavage occurs within the basic motif RRRRR(59)DT, suggesting the involvement of proprotein convertase (PC) family members in this process.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antimicrobial Cationic Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Cation Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Furin,
http://linkedlifedata.com/resource/pubmed/chemical/PCSK6 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Pcsk6 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Proprotein Convertase 5,
http://linkedlifedata.com/resource/pubmed/chemical/Proprotein Convertases,
http://linkedlifedata.com/resource/pubmed/chemical/SERPINA1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/alpha 1-Antitrypsin,
http://linkedlifedata.com/resource/pubmed/chemical/hepcidin,
http://linkedlifedata.com/resource/pubmed/chemical/metal transporting protein 1
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1468-3288
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
57
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1573-82
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pubmed:meshHeading |
pubmed-meshheading:18664504-Animals,
pubmed-meshheading:18664504-Antimicrobial Cationic Peptides,
pubmed-meshheading:18664504-Cation Transport Proteins,
pubmed-meshheading:18664504-Cell Line,
pubmed-meshheading:18664504-Furin,
pubmed-meshheading:18664504-Humans,
pubmed-meshheading:18664504-Liver,
pubmed-meshheading:18664504-Mice,
pubmed-meshheading:18664504-Mutagenesis, Site-Directed,
pubmed-meshheading:18664504-Neoplasms,
pubmed-meshheading:18664504-Proprotein Convertase 5,
pubmed-meshheading:18664504-Proprotein Convertases,
pubmed-meshheading:18664504-Serine Endopeptidases,
pubmed-meshheading:18664504-Transfection,
pubmed-meshheading:18664504-alpha 1-Antitrypsin
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pubmed:year |
2008
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pubmed:articleTitle |
Regulation of prohepcidin processing and activity by the subtilisin-like proprotein convertases Furin, PC5, PACE4 and PC7.
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pubmed:affiliation |
INSERM U 716/Equipe AVENIR, Institut de Génétique Moléculaire, 27 rue Juliette Dodu, 75010 Paris, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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