Literature DB >> 2400627

The valency state of absorbed iron appearing in the portal blood and ceruloplasmin substitution.

P Wollenberg1, R Mahlberg, W Rummel.   

Abstract

(1) Attempts to determine the redox-state of the absorbed iron, which appeared in the portal blood when the free iron-binding capacity was previously saturated, indicate that about 30-90% of this iron was in the ferrous state. This effect was particularly prominent after luminal administration of ferrous iron, but was also seen when iron was given in the ferric state. (2) Total iron absorption is significantly higher in ceruloplasmin-substituted copper-deficient animals as compared to copper-deficient controls. (3) The appearance rate of absorbed iron in the portal blood of copper-deficient animals increased several times immediately after the intravenous infusion of ceruloplasmin. (5) The distribution of absorbed iron was changed due to the ceruloplasmin substitution: it was increased in the reticulocytes (+66%), plasma (+400%) and the body (+112%), whereas in the liver it was decreased by about 78%. (5) In iron-deficient rats intravenously injected ceruloplasmin did not increase iron absorption. (6) The conclusion was drawn that, as for the entrance into the mucosa from the luminal side, also for the release at the contraluminal side into the portal blood, the ferrous state of iron is favoured and that ceruloplasmin accelerates the release into the portal blood by catalyzing the oxidation of ferrous iron due to its high Fe(II): oxygen oxidoreductase (EC 1.16.3.1) activity.

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Year:  1990        PMID: 2400627     DOI: 10.1007/bf01141169

Source DB:  PubMed          Journal:  Biol Met        ISSN: 0933-5854


  30 in total

1.  ACTIVE TRANSPORT OF IRON BY INTESTINE: MUCOSAL IRON POOLS.

Authors:  J MANIS; D SCHACHTER
Journal:  Am J Physiol       Date:  1964-10

2.  Studies on copper metabolism. IV. The influence of copper on the absorption of iron.

Authors:  M S CHASE; C J GUBLER; G E CARTWRIGHT; M M WINTROBE
Journal:  J Biol Chem       Date:  1952-12       Impact factor: 5.157

3.  [Influence of blood flow on the absorption of urea, methanol and ethanol from the rat jejunum].

Authors:  D Winne; J Remischovsky
Journal:  Naunyn Schmiedebergs Arch Pharmakol       Date:  1971

4.  Role of iron in the oxidase activity of ceruloplasmin.

Authors:  J A McDermott; C T Huber; S Osaki; E Frieden
Journal:  Biochim Biophys Acta       Date:  1968-03-25

5.  Binding of iron to a non-ferritin protein in the mucosal cells of normal and iron-deficient rats during absorption.

Authors:  H Huebers; E Huebers; W Forth; W Rummel
Journal:  Life Sci I       Date:  1971-10-15

6.  Mobilization of liver iron by ferroxidase (ceruloplasmin).

Authors:  S Osaki; D A Johnson
Journal:  J Biol Chem       Date:  1969-10-25       Impact factor: 5.157

7.  Measurement of ceruloplasmin from its oxidase activity in serum by use of o-dianisidine dihydrochloride.

Authors:  K H Schosinsky; H P Lehmann; M F Beeler
Journal:  Clin Chem       Date:  1974-12       Impact factor: 8.327

8.  The possible significance of the ferrous oxidase activity of ceruloplasmin in normal human serum.

Authors:  S Osaki; D A Johnson; E Frieden
Journal:  J Biol Chem       Date:  1966-06-25       Impact factor: 5.157

9.  Caeruloplasmin: a multi-functional metalloprotein of vertebrate plasma.

Authors:  E Frieden
Journal:  Ciba Found Symp       Date:  1980

10.  Conjugation of 1-naphthol and transport of 1-naphthol-conjugates in the vascularly perfused small intestine of the mouse.

Authors:  P Wollenberg; V Ullrich; W Rummel
Journal:  Biochem Pharmacol       Date:  1983-07-01       Impact factor: 5.858

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  2 in total

1.  Serum ceruloplasmin protein expression and activity increases in iron-deficient rats and is further enhanced by higher dietary copper intake.

Authors:  Perungavur N Ranganathan; Yan Lu; Lingli Jiang; Changae Kim; James F Collins
Journal:  Blood       Date:  2011-07-18       Impact factor: 22.113

2.  Menkes Copper ATPase (Atp7a) is a novel metal-responsive gene in rat duodenum, and immunoreactive protein is present on brush-border and basolateral membrane domains.

Authors:  Jennifer J Ravia; Renu M Stephen; Fayez K Ghishan; James F Collins
Journal:  J Biol Chem       Date:  2005-08-04       Impact factor: 5.157

  2 in total

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