کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9137558 | 1162483 | 2005 | 5 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Recombinant human hepcidin expressed in Escherichia coli isolates as an iron containing protein
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شناسی مولکولی
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چکیده انگلیسی
Hepcidin is a small peptide that acts as a regulator of systemic iron homeostasis. To study some of its functional properties, a synthetic cDNA for the minimal, 20-amino-acid, form of human hepcidin was cloned into different constructs for expression in Escherichia coli. The fusion ferritin-hepcidin produced molecules retaining most of ferritin structural and functional properties, including ferroxidase and iron incorporation activities. However, it showed spectroscopic properties compatible with the presence of iron-sulfur complexes on the hepcidin moiety, which was buried into protein cavity. Similar complexes were reconstituted by in vitro incubation of the iron-free protein with iron and sulfide salts. Two other unrelated fusion products were constructed, which, when expressed in E. coli, formed insoluble aggregates retaining a large proportion of total bacterial iron. Analysis of the solubilized preparations showed them to contain iron-sulfur complexes. We concluded that the cysteine-rich hepcidin acts as an iron-sequestering molecule during expression in E. coli. This may have implications for the biological functions of this key protein of iron metabolism.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Blood Cells, Molecules, and Diseases - Volume 35, Issue 2, SeptemberâOctober 2005, Pages 177-181
Journal: Blood Cells, Molecules, and Diseases - Volume 35, Issue 2, SeptemberâOctober 2005, Pages 177-181
نویسندگان
Gianmario Gerardi, Giorgio Biasiotto, Paolo Santambrogio, Isabella Zanella, Rosaria Ingrassia, Marcella Corrado, Patrizia Cavadini, Manuela Derosas, Sonia Levi, Paolo Arosio,