The effect of isoferritins on granulopoiesis

Sala, G; Worwood, Mark; Jacobs, A.

doi:10.1182/blood.v67.2.436.bloodjournal672436

Cited by 11 publications

(3 citation statements)

References 22 publications

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“…This supports the hypothesis that the increased presence of morphologically abnormal erythroblasts leads to a lower PI range for erythrocyte ferritin. Quite recently (3 yr after the initial diagnosis), the patient's hematological status deteriorated and pancytopenia developed, which may indicate an inhibitory effect of acidic ferritins on hemopoietic progenitors (28,29), although this effect is not completely accepted (30).…”

Section: Discussionmentioning

confidence: 99%

Quantitative and qualitative studies of red cell ferritin in refractory anemia of myelodysplastic syndrome

Ohhara

1993

European J of Haematology

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The red cell ferritin (rFt) level in 10 patients with refractory anemia (RA) was measured and analyzed by column isoelectric focusing (IEF). The levels in 9 of the 10 patients (90.0%) were higher than the upper limit in healthy controls (MV ± SD: male 14.3 ± 10.3 ag/cell, female 7.5 ± 3.6 ag/cell). The isoelectric point (pI) of rFt determined by IEF in healthy subjects ranged from 5.1 to 5.7. However, the pI ranges for RA patients varied widely; the pI value was thought to correlate with the severity of the morphological abnormalities of bone marrow (BM) erythroblasts. That is, the greater the proportion of morphologically abnormal erythroblasts with respect to all erythroid precursors, the lower the pI range for rFt. The rFt content was not related to serum iron, transferrin saturation, serum ferritin, reticulocyte count, red cell iron content, or BM erythroblast count. These data suggest that rFt synthesis in RA patients is influenced by factor(s) other than iron; this is considered an essential feature of erythropoiesis in myelodysplastic syndrome (MDS).

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Section: Discussionmentioning

confidence: 99%

Quantitative and qualitative studies of red cell ferritin in refractory anemia of myelodysplastic syndrome

Ohhara

1993

European J of Haematology

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“…A more controversial role for ferritin is the proposal that acidic isoferritins released from leukaemic cells may suppress normal myelopoiesis (119; reviewed in 78). As with the related proposal for lactoferrin (see above), the primary mechanism of ferritin action remains unclear, and contrary results have been reported (120). An immunosuppressive role for ferritin has also been proposed, based on !ts ability to inhibit mitogen-stimulated lymphocyte proliferation ( 121,122).…”

Section: Function Of Ferritinmentioning

confidence: 95%

Iron‐binding Proteins

Brock

1989

Acta Paediatrica

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Brock, J. H. (Department of Bacteriology and Immunology, Western Infirmary, Glasgow, UK). Iron‐binding proteins. The structure and properties of the iron‐binding proteins transferrin, lactoferrin and transferrin are reviewed. Transferrin and lactoferrin are structurally similar, consisting of a single polypetide chain and reversibly binding two iron atoms per molecule. Transferrin is found mainly in serum, whereas lactoferrin is found in neutrophils and in external secretions. Transferrin functions mainly as a donor of iron to cells, but there is no established iron‐transport role for lactoferrin. Both these proteins may have antimicrobial activity as a result of their ability to sequester iron. Lactoferrin may act principally as a scavenger of iron in conditions where transferrin may not bind iron well, e.g. at low pH. Ferritin is a multisubunit protein capable of binding up to 4 000 iron atoms and serves principally as an iron‐storage protein, though it may also serve to detoxify iron. In iron‐rich tissues ferritin is largely degraded and the iron is converted to haemosiderin.

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“…AIF suppresses colony formation of in vitro myeloid progenitors (CFU-gm, BFUe, CFU-gemm) from normal donors [188-1941 but not from patients or mice with leukemia [188,190,1951, which led to suggestions that abnormalities in AIFtarget cell interactions might be associated with a growth advantage for leukemia cells [188,190]. Some evidence exists for an in vim action for AIF [1%], but others have questioned this role [197,1981. Moreover, the cDNAs coding for the two subunits of ferritin have been cloned in vectors for overproduction of E. coli [199,2001.…”

Section: "Suppressor" Moleculesmentioning

confidence: 99%

Biomolecule‐cell interactions and the regulation of myelopoiesis

Broxmeyer

1986

The International Journal of Cell Cloning

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The regulation of myelopoiesis in vivo most likely entails a complex set of interactions between cell-derived biomolecules and their target cells. Much of what we currently know of these interactions has been derived from studies in vitro utilizing techniques for the purification of both the biomolecules and the cells producing and responding to these factors. Stimulating and suppressing influences have been uncovered, and with the cloning and purification of biologically active factors, studies assessing the actions of these molecules in vivo have begun. From studies in vitro it is apparent that many of the purified molecules can have move than one action and that different molecules can collaborate in a synergistic manner to enhance or suppress functional endpoints.

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The effect of isoferritins on granulopoiesis

Cited by 11 publications

References 22 publications

Quantitative and qualitative studies of red cell ferritin in refractory anemia of myelodysplastic syndrome

Quantitative and qualitative studies of red cell ferritin in refractory anemia of myelodysplastic syndrome

Iron‐binding Proteins

Biomolecule‐cell interactions and the regulation of myelopoiesis

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