Microheterogeneity of horse spleen ferritin and apoferritin

Urushizaki, I; Niitsu, Yoshiro; Ishitani, Kunihiko; Matsuda, Mikihito; Fukuda, M

doi:10.1016/0005-2795(71)90075-4

Cited by 51 publications

(25 citation statements)

References 8 publications

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“…The mucosal ferritin is clearly different from the ferritins of liver and spleen. Despite reports in the literature of microheterogeneity of rat and other ferritins [25,26] as revealed by isoelectric focusing we have found no evidence for such heterogeneity under our conditions. Recent reports [28 -301 of lower molecular weight components in horse and rat ferritins have not been confirmed in the present study.…”

Section: General Conclusioncontrasting

confidence: 98%

Isolation and Characterization of Iron‐Binding Proteins from Rat Intestinal Mucosa

Huebers

Rummel

et al. 1976

European Journal of Biochemistry

107

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Two iron-binding proteins were isolated from rat intestinal mucosa. From determination of their molecular weights, their electrophoretic and iron-binding properties it was established that one was a mucosal ferritin and the other a mucosal transferrin.The mucosal ferritin is compared in its molecular weight, isoelectric point, amino acid composition and tryptic peptide pattern with the ferritins of rat spleen and liver. All three ferritins are distinctly different from one another. In addition the iron content of mucosal ferritin was found to be much lower than that of liver and spleen ferritins.Mucosal transferrin was separated into two components by isoelectric focusing, as was plasma transferrin. The plasma and mucosal transferrins differ in their isoelectric points and in their amino acid compositions. Differences were also found in vitro in the iron-binding of mucosal transferrin as compared with plasma transferrin. The role of these mucosal proteins in the absorption of iron is briefly discussed.

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Section: General Conclusioncontrasting

confidence: 98%

Isolation and Characterization of Iron‐Binding Proteins from Rat Intestinal Mucosa

Huebers

Rummel

et al. 1976

European Journal of Biochemistry

107

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“…Many tissue ferritins have been resolved into multiple isoferritins by the technique of isoelectric focusing (Drysdale, 1970;Urushizaki et al, 1971;Drysdale, 1974;Powell et al, 1975). These isoferritins do not represent differences in aggregation or iron content of the protein but intrinsically different apoferritin shells (Drysdale, 1970;1974).…”

mentioning

confidence: 99%

Alterations in tissue ferritins in iron storage disorders.

Powell¹,

McKeering²,

Halliday³

1975

Gut

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SUMMARY Purified tissue ferritins isolated from Bantu subjects with gross haemosiderosis, from a patient with idiopathic haemochromatosis ( HC) treated by phlebotomy, and from rats with experimental iron overload were studied in order to determine the significance of the abnormality previously demonstrated in tissue isoferritins in patients with IHC. The isoferritin profile of the tissues from the Bantu subjects and the iron-loaded rats showed a similar abnormality to that previously found in patients with untreated IHC-that is, an abnormally uniform distribution of iron-containing isoferritins with an increase in the more basic isoferritins and an apparent absence of the more acidic ones. In contrast, tissues from the patient with treated IHC, who was iron depleted at the time of death, showed the normal organ-specific isoferritin distribution. These findings strongly suggest that the abnormal distribution of tissue isoferritins in IHC is an acquired phenomenon and unlikely to be related to an underlying genetic defect in ferritin or iron metabolism.Ferritin is the major iron storage protein in mammalian tissues and is found, or may be induced by iron administration, in most organs (Granick, 1951;Munro and Drysdale, 1970). Many tissue ferritins have been resolved into multiple isoferritins by the technique of isoelectric focusing Urushizaki et al., 1971;Drysdale, 1974;Powell et al., 1975). These isoferritins do not represent differences in aggregation or iron content of the protein but intrinsically different apoferritin shells 1974). Each tissue appears to have a characteristic isoferritin composition (Drysdale, 1974;Powell et al., 1975). This organ-specific isoferritin profile has recently been shown to be markedly abnormal in patients with untreated primary idiopathic haemochromatosis . The present study was designed to determine whether the abnormality in tissue isoferritins in idiopathic haemochromatosis is directly related to the genetic defect in iron metabolism or the result of long-standing iron overload. Methods HUMAN TISSUESNecropsy tissues were obtained from a normal adult male accident victim and also from a patient with classical familial idiopathic haemochromatosis whose case history and family history have been documented previously (Powell, 1965). This patient Received for publication 18 September 1975. had been treated by repeated phlebotomy for 11 years and was in a state of marginal iron deficiency at the time of his death at the age of 74 years. Histological examination showed no stainable iron in any of the tissues examined. Tissues from two Bantu patients with gross haemosiderosis were kindly provided by Professor R. Charlton of Johannesburg. ANIMAL STUDIESTen male Sprague Dawley rats weighing 250 to 300 g were each given 1 g/kg body weight of iron as irondextran by intramuscular injection over a period of two weeks. The rats were maintained on a normal diet tor three months and then killed by exsanguination from the dorsal aorta under ether anaesthesia. The carcasses were then perfuse...

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“…All of Dr Richter's arguments suggesting that the multiple forms arc coiitamiiiaiits or artifacts resulting froin aggregates or ampholytc binding have already been fully answered in the past few years (Drysdale, 1970(Drysdale, , 1974Urushizaki et al, 1971Urushizaki et al, , 1973.…”

Section: Dr Drysdale and Rolkagircs Reply Asfo/lowsmentioning

confidence: 99%

“…They do iiot represent differences in iron content or aggregate size since monomeric, i.e. single shell, apoferritiii gives cssentially the same pattern (Drysdalc, 1970;Urushizaki et al, 1971). Finally, since a similar lieterogencity may be observed by ioii cxchaiige chromatography (Urusliizaki et al, 1973 ;Drysdalc, 1974;Marcus & Ziinberg, 1974), arguments about ampholyte binding, or any other possible artifact of electrofocusiiig, become irrelevant.…”

Section: Dr Drysdale and Rolkagircs Reply Asfo/lowsmentioning

confidence: 99%