Summary
Tissue ferritins fromβ-thalassaemia/haemoglobin E heart and pancreas were characterized by native PAGE, SDS/PAGE and isoelectric focussing, and compared with those isolated from corresponding liver and spleen tissue. On PAGE; all ferritins consisted of a single band assigned to the protein monomer. Small differences in electrophoretic mobility were found between the bands. The ferritins were resolved by SDS/PAGE into two major subunits, H and L, corresponding to molecular masses of 22.5 kDa and 19 kDa, respectively. The L subunit was predominant in all cases. The isoferritin profiles of all tissue ferritins were remarkably similar; consisting of a complex pattern of bands which were appreciably more basic than those obtained for horse spleen ferritin. The subunit composition and isoferritin profiles of the four tissue ferritins almost certainly reflect the defense mechanism of the body in synthesizing in all four tissue types a more stable long-term iron-storage isoferritin in order to detoxify and store the excess iron present due to the pathological condition ofβ-thalassaemia/HbE.
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Abbreviations
- PAGE:
-
polyacrylamide gel electrophoresis
- SDS:
-
sodium dodecyl sulphate
References
Aisen P, Listowsky I (1980) Iron transport and storage proteins. Annu Rev Biochem 49:357–393
Arosio P, Adelman TG, Drysdale JW (1978) On ferritin heterogeneity. Further evidence for heteropolymers. J Biol Chem 253:4451–4458
Bhamarapravati N, Na-Nakorn S, Wasi P, Tuchinda S (1967) Pathology of abnormal hemoglobin diseases seen in Thailand. I. Pathology ofβ-thalassaemia/hemoglobin E disease. Am J Clin Pathol 47:745–758
Bomford A, Conlon-Hollingshead C, Munro HN (1981) Adaptive responses of rat tissue isoferritins to iron administration. J Biol Chem 256:948–55
Costanzo F, Santoro C, Colantuoni V, Bensi G, Raugei G, Romano V, Cortese R (1984) Cloning and sequencing of a full-length cDNA coding for a human apoferritin H chain: evidence for a multigene family. EMBO J 3:23–27
Drysdale JW, Adelman TG, Arosio P, Casareale D, Fitzpatrick P, Hazard JT, Yokota M (1977) Human isoferritins in normal and disease states. Semin Hematol 14:71–88
Harrison PM, Clegg GA, May K (1980) Ferritin structure and function. In: Jacobs A, Worwood M (eds) Iron in biochemistry and medicine II. Academic Press, London, pp 131–171
Kohgo Y, Yokota M, Drysdale JW (1980) Differential turnover of rat liver isoferritins. J Biol Chem 255:5195–5200
Lavoie DJ, Marcus DM, Ishikawa K, Listowsky I (1977) Ferritin and apoferritin from human liver: aspect of heterogeneity. In: Brown EB, Aisen P, Fielding J (eds) Proteins in iron metabolism. Grune and Stratton, New York, pp 71–78
Lawson DM, Treffry A, Artymiuk PJ, Harrison PM, Yewdall SJ, Luzzago A, Cesareni G, Levi S, Arosio P (1989) Identification of the ferroxidase centre in ferritin. FEBS Lett 254:207–210
Levi S, Luzzago A, Cesareni G, Cozzi A, Franceschinelli F, Albertini A, Arosio P (1988) Mechanism of ferritin iron uptake: activity of the H-chain and deletion mapping of the ferro-oxidase site. J Biol Chem 263:18086–18092
Massover WH (1985) Molecular size heterogeneity of ferritin in mouse liver. Biochim Biophys Acta 829:377–386
Nishi M (1985) Comparison of biochemical characteristics between human liver and spleen ferritin. Nippon Ika Daigaku Zasshi 57:165–177
Pootrakul P, Kriengkrai K, Yansukon P, Wasi P, Fucharoen S, Charoenlarp P, Brittenham G, Pippard M, Finch CA (1988) The effect of erythroid hyperplasia on iron balance. Blood 71:1124–1129
Powell LW, Alpert E, Isselbacher KJ, Drysdale JW (1974) Abnormality in tissue isoferritin distribution in idiopathic haemo-chromatosis. Nature 250:333–335
Powell LW, Alpert E, Isselbacher KJ, Drysdale JW (1975) Human isoferritins: organ-specific iron and apoferritin distribution. Br J Haematol 30:47–55
Shuler TR, Pootrakul P, Yansukon P, Nielsen FH (1990) Effect of thalassaemia/hemoglobin E disease on macro, trace and ultratrace element concentrations in human tissue. J Trace Elements Exp Med 3:31–43
St. Pierre TG, Webb J, Mann S (1989) Ferritin and hemosiderin: structural and magnetic studies of the iron core. In: Mann S, Webb J, Williams RJP (eds) Biomineralization: chemical and biochemical perspectives. VCH Verlagsgesellschaft, Weinheim, pp 295–344
Theil EC (1987) Ferritin: structure, gene regulation, and cellular function in animals, plants and microorganisms. Annu Rev Biochem 56:289–315
Tran KC, Webb J, Macey DJ, Pootrakul P, Yansukon P (1990)β-Thalassaemia/haemoglobin E tissue ferritins. I: Purification and partial characterization of liver and spleen ferritins. Biol Metals 3:222–226
Treffry A, Harrison PM (1980) Evidence for post-translational changes in rat liver ferritin. Biochim Biophys Acta 610:421–424
Treffry A, Lee PJ, Harrison PM (1984) Iron-induced changes in rat liver isoferritins. Biochem J 220:717–722
Wagstaff M, Worwood M, Jacobs A (1978) Properties of human tissue isoferritins. Biochem J 173:969–977
Wasi P (1981) Haemoglobinopathies including thalassaemia. I: Tropical Asia. Clin Hematol 10:707–729
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Tran, K.C., Webb, J., Macey, D.J. et al. β-Thalassaemia/haemoglobin E tissue ferritins. Biol Metals 3, 227–231 (1990). https://doi.org/10.1007/BF01140584
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DOI: https://doi.org/10.1007/BF01140584