Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P02794 (ferritin)
 17,525 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

242 members of 43 families with idiopathic haemochromatosis were investigated for increased body-iron stores in order to assess the value of serum-ferritin determination as a screening-test to detect preclinical disease. The serum-iron concentration was elevated in only 76% of relatives with increased iron stores, and it was also elevated in 10% of relatives with normal iron stores. The percentage saturation of transferrin was elevated in all relatives with increased iron stores but also in 33% of relatives with normal iron stores. Serum-ferritin was raised in 98% of relatives with increased iron stores and in only 3 (1.8%) of those with normal iron stores. These 3 subjects consumed alcohol in excess of 100 g ethanol per day, and their serum-ferritin levels fluctuated widely. Increased iron stores were reflected in increased serum-ferritin concentrations in subjects as young as 14 years in whom the liver-iron concentration was twice the normal upper limit and before there was any evidence of architectural damage to the liver. The serum-ferritin concentration is a useful non-invasive screening test for precirrhotic haemochromatosis.
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PMID:Serum-ferritin in diagnosis of haemochromatosis. A study of 43 families. 7 45

To determine the frequency of HLA histocompatibility antigens in persons with idiopathic hemochromatosis and their usefulness as genetic markers of the disease, HLA typing for the A, B and C loci was carried out. HLA-A3 was found in 61% of 18 unrelated individuals with idiopathic hemochromatosis compared with 25% of 253 randomly chosen control subjects (P less than 0.001), and HLA-B7 was found in 50% and 22% respectively (P less than 0.025). Eighty-six members of seven families with idiopathic hemochromatosis were screened for abnormalities in iron metabolism with tests for serum iron concentration, transferrin saturation, serum ferritin concentration and iron content of the hepatocytes. Of the 14 persons selected for liver biopsy because of abnormalities detected by these tests, 8 had increased amounts of stainable iron in the hepatocytes. Body iron overload was subsequently demonstrated in six of the seven, who had undergone repeated phlebotomy. In sibships having one member with hemochromatosis, only 1 of 22 members had two haplotypes in common with the proband, whereas in sibships having more than 1 member with the disease 4 of 5 affected members had two haplotypes in common. HLA typing in families with hemochromatosis may provide a means of identifying persons at risk of acquiring the disease.
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PMID:Histocompatibility antigens as markers of abnormal iron metabolism in idiopathic hemochromatosis. 8 5

A study of 18 unrelated families with idiopathic haemochromatosis (I.H.C.) was undertaken to define the relative values of HLA typing and serum-ferritin estimation in the early detection of the disease. Sharing of both HLA haplotypes with the proband indicated a high risk of I.H.C. in siblings; but HLA typing was of limited value in detecting affected offspring. Non-identical HLA indicated a low risk of I.H.C. in both siblings and offspring. The presence of HLA A3 was not clinically useful as a marker for I.H.C., since this antigen was also present in 40% of unaffected relatives. In contrast, the serum-ferritin concentration was elevated in 96% of patients with I.H.C. and in only 5% of unaffected relatives. HLA typing provides some indication of the risk of I.H.C. in first-degree relatives, but the combination of serum-ferritin, serum-iron, and transferrin saturation remains the most reliable screening regimen for early diagnosis of I.H.C.
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PMID:Early detection of idiopathic haemochromatosis: relative value of serum-ferritin and HLA typing. 8 15

Serogroups of N. meningitidis were characterized as virulent or avirulent according to their capacity to establish meningococcal infection in mice. An agar plate diffusion technique demonstrated that iron had a definite growth-supporting role for both of these meningococcal types. The avirulent strains could use ionic or chelated iron as well as the virulent strains. Iron-reversible growth inhibition occurred to the same extent for both bacterial types in the presence of the synthetic iron-chelating agents Desferal and ethylenediamine-di-orthohydroxy phenylacetic acid. A difference in response was demonstrated for these bacterial types when grown in the presence of various iron-binding proteins from animal body fluids and tissues. The growth of the avirulent strain was inhibited to a greater degree by egg white conalbumin. The humoral iron-binding protein transferrin showed a significant inhibitory capacity only when used in conjunction with bicarbonate. Under conditions of increased iron saturation of this protein, the avirulent strain was inhibited to the furthest extent. In the presence of ferritin, the cellular iron-binding protein, which had been reduced, inhibition of the growth of either strain type did not occur on iron-poor media (less than 5 micrograms/100 ml). However, with the incorporation of iron into the media, the inhibitory effect of the protein became evident. As the concentration of iron increased, the inhibition increased to a certain level and subsequently declined. A substantial difference in the ability of the avirulent type to grow in the presence of reduced horse spleen ferritin was observed. For this microorganism, a correlation appears to exist between the capacity to grow by utilizing the available iron in the presence of reduced ferritin and the ability to establish infection. The host protein ferritin, in the reduced state, apart from simply being a storage protein for iron, can prevent the growth of a procaryotic organism. Our experiments suggest a role for ferritin in the prevention of emningococcal disease. A cehmotherapeutic potential for Desferal is also implied.
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PMID:Inhibition of the growth of Neisseria meningitidis by reduced ferritin and other iron-binding agents. 11 92

Ferritin has been purified from normal full-term human placentae and its antigenic and molecular characteristics compared with adult liver ferritin. Placental ferritin is composed predominantly of a single subunit type, co-migrating with a liver ferritin standard on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. Comparison of dose-response curves in an immunoradiometric assay indicated some tissue-specific antigenicity for placental ferritin. This was supported by immunofluorescence studies on cryostat sections of human placentae by using antibodies to placental and spleen ferritin. Specific staining for placental ferritin was demonstrated within placental syncytiotrophoblast, particularly localized towards the microvillus plasma membrane. Ferritin has also been shown by electrophoretic and antigenic analysis to be present in protein fractions solubilized from isolated human syncytiotrophoblast microvillus plasma-membrane preparations, suggesting that ferritin may play an active role in the transfer of iron from maternal transferrin across the syncytiotrophoblast plasma membrane.
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PMID:Characterization and localization of human placental ferritin. 11 99

We studied 12 members of a family with precirrhotic hemochromatosis to define the physiologic abnormalities in the asymptomatic phase of the disease. Six of 12 had increased iron stores; the mode of inheritance was consistent with an autosomal dominant trait. Serum ferritin levels were no more predictive of tissue iron levels than measurements of serum iron, transferrin saturation or chelatable iron excretion. In three affected family members intestinal iron content was normal. Liver proline hydroxylase activity and urinary hydroxyproline excretion did not correlate with tissue iron content, suggesting that, in addition to the possible role of tissue iron, hepatic fibrosis may involve other factors. "Borderline diabetes mellitus" was present in three affected family members, but extensive studies revealed that pituitary dysfunction is uncommon in early hemochromatosis. Increased levels of liver iron proved to be the most reliable marker for the disease.
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PMID:Familial hemochromatosis. Physiologic studies in the precirrhotic stage of the disease. 19 51

The mechanism of tumor localization of gallium-67 (67Ga) is not known with certainty, although much information has been derived regarding the biodistribution and subcellular fate of 67Ga in a variety of tumors and other tissues from experimental animals. After intravenous administration, 67Ga is bound to transferrin in the blood, and distributed to liver, lacrimal glands, salivary glands, and soft tissue tumors. Within the cells of the liver and tumors, gallium is found in lysosomes, and rough endoplasmic reticulum. Within these organelles, 67Ga is bound to a variety of macromolecules, including transferrin, ferritin, and a 45,000 molecular weight glycoprotein. Recent studies of tumor cells growing in tissue culture suggest an important role for transferrin in 67Ga tumor uptake. This uptake is mediated by a transferrin specific cellular receptor.
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PMID:Mechanisms of localization of gallium-67 in tumors. 21 49

On account of its easy access in aqueous solution to the two states ferrous (FeII) and ferric (FeIII), iron is ideally suited for the activation of molecular oxygen. It is, therefore, logical to seek links between the normal and pathological metabolism of iron and oxygen activation. The pathways of intracellular iron metabolism require changes in the oxidation state of iron both in its deposition in the storage form, ferritin, and in its mobilization from the storage form and use in the cell. Evidence is presented which shows that iron oxidation and deposition in ferritin involves activation of molecular oxygen with formation of a stable peroxo-complex as an intermediate in which the oxygen is bound between two iron atoms attached to adjacent polypeptide chains. The release of iron from ferritin is thought to involve reduction by a flavin, which is associated with the protein, and serves as a cofactor being alternately reduced by NADH or NADPH and oxidized by iron(III). The nature of the low-molecular-weight iron complex which serves to transfer storage iron to transferrin and to supply iron for intracellular use remains to be established. The consequence of excessive iron overload can be rationalized on the basis of oxidative free-radical reactions which provoke lesions typical of deregulated oxygen activation. In some cases these pathological defects can be reversed by iron chelators. Progress in the development of chelation therapy for iron overload are reviewed.
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PMID:Interactions between iron metabolism and oxygen activation. 25 65

The duodenal mucosa of genotypically normal iron replete and iron deficient mice and mice with sex-linked (sla) and microcytic anemias (mk) was examined for the presence of iron-binding proteins. Following continuous, 15 or 120 minute, in vivo intraenteric exposure of a closed duodenal loop to 59Fe, a high speed supernatant of homogenized mucosal tissue was chromatographed on G-200 Sephadex. Two major peaks of 59Fe activity were observed. The molecular weight, and immunological properties of peak I were similar to ferritin whilst those of peak II were similar to transferrin. The distribution of 59Fe between peaks I and II in mk/mk animals was similar to that in genotypically normal iron deficient animals indicating that the intramucosal mechanisms for iron transport were reacting appropriately to the iron deficient state of mice with microcytic anemia. In contrast, the distribution of 59Fe between peaks I and II in sla/Y animals was the reverse of that found in genotypically normal iron deficient animals suggesting the possibility of an intramucosal iron binding protein defect in sex-linked anemia.
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PMID:Mucosal iron binding proteins in sex-linked anemia and microcytic anemia of the mouse. 28 79

In the present paper we apply the "ecotaxis hypothesis" to the analysis of lymphocyte distribution in Hodgkin's disease and other forms of lymphoid malignancy. The results lead us to consider the possiblity that metal-binding proteins, namely ferritin, transferrin and lactoferrin, play a role in lymphocyte ecotaxopahty. It is suggested that in Hodgkin's disease, a failure of lymph node and spleen monocytes to handle iron normally could explain most of the hematologic, immunologic, pathologic, and epidemiologic features of the disease.
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PMID:Suggested models of ecotaxopathy in lymphoreticular malignancy. A role for iron-binding proteins in the control of lymphoid cell migration. 30 76


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