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Hepcidin, the Hormone of Iron Metabolism, is Bound Specifically to a-2-Macroglobulin
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SYSNO ASEP 0338673 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Hepcidin, the Hormone of Iron Metabolism, is Bound Specifically to a-2-Macroglobulin Author(s) Pešlová, G. (CZ)
Petrák, J. (CZ)
Kuželová, K. (CZ)
Hrdý, I. (CZ)
Halada, Petr (MBU-M) RID, ORCID
Kuchel, P. W. (AU)
Soe-Lin, S. (CA)
Ponka, P. (CA)
Šuták, R. (CA)
Becker, E. (AU)
Huang, M. L.-H. (AU)
Rahmanto, Y. S. (AU)
Richardson, D. R. (AU)
Vyoral, D. (CZ)Source Title Blood. - : American Society of Hematology - ISSN 0006-4971
Roč. 113, č. 24 (2009), s. 6225-6236Number of pages 12 s. Language eng - English Country US - United States Keywords RECEPTOR-RELATED PROTEIN ; GROWTH-FACTOR-BETA ; BINDING-PROTEIN Subject RIV CE - Biochemistry R&D Projects GD204/03/H066 GA ČR - Czech Science Foundation (CSF) LC07017 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) CEZ AV0Z50200510 - MBU-M (2005-2011) UT WOS 000267147100027 DOI 10.1182/blood-2009-01-201590 Annotation Hepcidin is a major regulator of iron metabolism. Hepcidin-based therapeutics/diagnostics could play roles in hematology in the future, and thus, hepcidin transport is crucial to understand. In this study, we identify alpha2-macroglobulin (alpha2-M) as the specific hepcidin-binding molecule in blood. Interaction of 125I-hepcidin with alpha2-M was identified using fractionation of plasma proteins followed by native gradient polyacrylamide gel electrophoresis and mass spectrometry. Hepcidin binding to nonactivated alpha2-M displays high affinity , whereas hepcidin binding to albumin was nonspecific and displayed nonsaturable kinetics Workplace Institute of Microbiology Contact Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Year of Publishing 2010
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