Hepcidin Bound to alpha(2)-Macroglobulin Reduces Ferroportin-1 Expression and Enhances Its Activity at Reducing Serum Iron Levels

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11110%2F13%3A10189170" target="_blank" >RIV/00216208:11110/13:10189170 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00023736:_____/13:00010741

Výsledek na webu

<a href="http://dx.doi.org/10.1074/jbc.M113.471573" target="_blank" >http://dx.doi.org/10.1074/jbc.M113.471573</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1074/jbc.M113.471573" target="_blank" >10.1074/jbc.M113.471573</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Hepcidin Bound to alpha(2)-Macroglobulin Reduces Ferroportin-1 Expression and Enhances Its Activity at Reducing Serum Iron Levels

Popis výsledku v původním jazyce

Hepcidin regulates iron metabolism by down-regulating ferroportin-1 (Fpn1). We demonstrated that hepcidin is complexedto the blood transport protein, ? 2-macroglobulin (Peslova, G., Petrak, J., Kuzelova, K., Hrdy, I., Halada, P., Kuchel, P. W., Soe-Lin,S., Ponka, P., Sutak, R., Becker, E., Huang, M. L.,Suryo Rahmanto, Y., Richardson, D. R., and Vyoral, D. (2009) Blood 113, 6225-6236). However, nothing is known about the mechanism of hepcidin binding to a 2M or the effects of the ? 2M hepcidin complex in vivo. We show that decreased Fpn1 expression can be mediated by hepcidin bound to native ? 2M and also, for the first time, hepcidin bound to methylamineactivated? 2M (? M-MA). Passage of high molecular weight ? 2M_hepcidin or ? 2M-MA_hepcidin complexes (ALMOST EQUAL TO725 kDa) through a Sephadex G-25 size exclusion column retained their ability to decrease Fpn1 expression. Further studies using ultrafiltration indicated that hepcidin binding to ? 2Mand ? 2M-MA was labile, resulting in

Název v anglickém jazyce

Hepcidin Bound to alpha(2)-Macroglobulin Reduces Ferroportin-1 Expression and Enhances Its Activity at Reducing Serum Iron Levels

Popis výsledku anglicky

Hepcidin regulates iron metabolism by down-regulating ferroportin-1 (Fpn1). We demonstrated that hepcidin is complexedto the blood transport protein, ? 2-macroglobulin (Peslova, G., Petrak, J., Kuzelova, K., Hrdy, I., Halada, P., Kuchel, P. W., Soe-Lin,S., Ponka, P., Sutak, R., Becker, E., Huang, M. L.,Suryo Rahmanto, Y., Richardson, D. R., and Vyoral, D. (2009) Blood 113, 6225-6236). However, nothing is known about the mechanism of hepcidin binding to a 2M or the effects of the ? 2M hepcidin complex in vivo. We show that decreased Fpn1 expression can be mediated by hepcidin bound to native ? 2M and also, for the first time, hepcidin bound to methylamineactivated? 2M (? M-MA). Passage of high molecular weight ? 2M_hepcidin or ? 2M-MA_hepcidin complexes (ALMOST EQUAL TO725 kDa) through a Sephadex G-25 size exclusion column retained their ability to decrease Fpn1 expression. Further studies using ultrafiltration indicated that hepcidin binding to ? 2Mand ? 2M-MA was labile, resulting in

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2013

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of Biological Chemistry

ISSN

0021-9258

e-ISSN

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Svazek periodika

288

Číslo periodika v rámci svazku

35

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

16

Strana od-do

25450-25465

Kód UT WoS článku

000330619000041

EID výsledku v databázi Scopus

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