Literature DB >> 7848299

Hepatic molecular conversion and detoxification of ferritin iron in adult lampreys (Geotria australis), following natural and induced iron loading.

L R Harris1, D J Macey, I C Potter, M H Cake.   

Abstract

Weekly intramuscular injections of 3 mg of iron as horse spleen ferritin into adult Geotria australis over 10 weeks, resulted in a progressive increase in that form of iron in the serum. However, as with control animals, the ferritin in the liver of injected lampreys consisted of one subunit type, whose M(r) (20,300) differed from those of the two subunit types of horse spleen ferritin. Thus, lampreys had converted horse spleen ferritin iron into endogenous ferritin iron, presumably in their liver. Marked rises in hepatic non-haem iron during the first 2 weeks and between weeks 8 and 10 of iron injections were accompanied by pronounced increases in superoxide dismutase (SOD) activity. This rise, which parallels the rise in SOD activity that occurs as iron increases during the very protracted upstream migration of G. australis, is consistent with the view that SOD protects against iron-mediated damage by removing the superoxide radical, which facilitates the formation of the highly toxic hydroxyl radical. A levelling off of the iron concentration between weeks 2 and 8 was accompanied by a decline in SOD activity, even though nonhaem iron levels were well above those of control animals. Enhanced SOD activity may therefore only be required when there is an elevated flux of iron in the liver through low-molecular-mass intermediates. A small amount of ferritin iron was converted into the more inert haemosiderin iron.

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Year:  1995        PMID: 7848299      PMCID: PMC1136353          DOI: 10.1042/bj3050975

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  19 in total

1.  Studies on intermediary iron metabolism. XII. Measurement of the iron derived from water soluble and water insoluble non-haem compounds (ferritin and haemosiderin iron) in liver and spleen.

Authors:  I KALDOR
Journal:  Aust J Exp Biol Med Sci       Date:  1958-04

2.  A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.

Authors:  M M Bradford
Journal:  Anal Biochem       Date:  1976-05-07       Impact factor: 3.365

3.  Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein).

Authors:  J M McCord; I Fridovich
Journal:  J Biol Chem       Date:  1969-11-25       Impact factor: 5.157

4.  Changes in the amount of nonhaem iron in the plasma, whole body, and selected organs during the postlarval life of the lamprey Geotria australis.

Authors:  S R Smalley; D J Macey; I C Potter
Journal:  J Exp Zool       Date:  1986-02

5.  Adaptive responses of rat tissue isoferritins to iron administration. Changes in subunit synthesis, isoferritin abundance, and capacity for iron storage.

Authors:  A Bomford; C Conlon-Hollingshead; H N Munro
Journal:  J Biol Chem       Date:  1981-01-25       Impact factor: 5.157

6.  On ferritin heterogeneity. Further evidence for heteropolymers.

Authors:  P Arosio; T G Adelman; J W Drysdale
Journal:  J Biol Chem       Date:  1978-06-25       Impact factor: 5.157

7.  Superoxide-dependent and -independent mechanisms of iron mobilization from ferritin by xanthine oxidase. Implications for oxygen-free-radical-induced tissue destruction during ischaemia and inflammation.

Authors:  P Biemond; A J Swaak; C M Beindorff; J F Koster
Journal:  Biochem J       Date:  1986-10-01       Impact factor: 3.857

8.  Studies on the concentration and intracellular localization of iron proteins in liver biopsy specimens from patients with iron overload with special reference to their role in lysosomal disruption.

Authors:  C Selden; M Owen; J M Hopkins; T J Peters
Journal:  Br J Haematol       Date:  1980-04       Impact factor: 6.998

9.  Differential turnover of rat liver isoferritins.

Authors:  Y Kohgo; M Yokota; J W Drysdale
Journal:  J Biol Chem       Date:  1980-06-10       Impact factor: 5.157

10.  Formation of hydroxyl radicals in the presence of ferritin and haemosiderin. Is haemosiderin formation a biological protective mechanism?

Authors:  M O'Connell; B Halliwell; C P Moorhouse; O I Aruoma; H Baum; T J Peters
Journal:  Biochem J       Date:  1986-03-15       Impact factor: 3.857

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