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Volumn 26, Issue 5, 2015, Pages 532-540

Bioavailability of iron from plant and animal ferritins

Author keywords

Bioavailability; Digestion; Ferritin; Iron; Stability

Indexed keywords

DODECYL SULFATE SODIUM; FERRITIN; IRON;

EID: 84928301319     PISSN: 09552863     EISSN: 18734847     Source Type: Journal    
DOI: 10.1016/j.jnutbio.2014.12.006     Document Type: Article
Times cited : (44)

References (47)
  • 1
    • 0035237534 scopus 로고    scopus 로고
    • Iron deficiency anemia
    • Leung A.K., Chan K.W. Iron deficiency anemia. Adv Pediatr 2000, 48:385-408.
    • (2000) Adv Pediatr , vol.48 , pp. 385-408
    • Leung, A.K.1    Chan, K.W.2
  • 2
    • 0036616441 scopus 로고    scopus 로고
    • Do side-effects reduce compliance to iron supplementation? A study of daily and weekly-dose regimens in pregnancy
    • Hyder S.M., Persson L.Å., Chowdhury A.M., Ekström E.C. Do side-effects reduce compliance to iron supplementation? A study of daily and weekly-dose regimens in pregnancy. J Health Popul Nutr 2002, 20:175-179.
    • (2002) J Health Popul Nutr , vol.20 , pp. 175-179
    • Hyder, S.M.1    Persson, L.Å.2    Chowdhury, A.M.3    Ekström, E.C.4
  • 3
    • 0036846243 scopus 로고    scopus 로고
    • Iron supplementation affects growth and morbidity of breast-fed infants: results of a randomized trial in Sweden and Honduras
    • Dewey K.G., Domellöf M., Cohen R.J., Landa R.L., Hernell O., Lönnerdal B. Iron supplementation affects growth and morbidity of breast-fed infants: results of a randomized trial in Sweden and Honduras. J Nutr 2002, 132:3249-3255.
    • (2002) J Nutr , vol.132 , pp. 3249-3255
    • Dewey, K.G.1    Domellöf, M.2    Cohen, R.J.3    Landa, R.L.4    Hernell, O.5    Lönnerdal, B.6
  • 4
    • 77953811022 scopus 로고
    • Phytoferritin and its implications for human health and nutrition
    • Zhao G. Phytoferritin and its implications for human health and nutrition. Biochim Biophys Acta 1800, 2010:815-823.
    • (1800) Biochim Biophys Acta , vol.2010 , pp. 815-823
    • Zhao, G.1
  • 5
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: molecular properties, iron storage function and cellular regulation
    • Harrison P.M., Arosio P. The ferritins: molecular properties, iron storage function and cellular regulation. Biochim Biophys Acta 1996, 1275:161-203.
    • (1996) Biochim Biophys Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 6
    • 3142781945 scopus 로고    scopus 로고
    • Iron, ferritin, and nutrition
    • Theil E.C. Iron, ferritin, and nutrition. Annu Rev Nutr 2004, 24:327-343.
    • (2004) Annu Rev Nutr , vol.24 , pp. 327-343
    • Theil, E.C.1
  • 7
    • 65549136658 scopus 로고    scopus 로고
    • Soybean ferritin: implications for iron status of vegetarians
    • Lönnerdal B. Soybean ferritin: implications for iron status of vegetarians. Am J Clin Nutr 2009, 89:1680S-1685S.
    • (2009) Am J Clin Nutr , vol.89 , pp. 1680S-1685S
    • Lönnerdal, B.1
  • 8
    • 0030071285 scopus 로고    scopus 로고
    • Purified ferritin and soybean meal can be sources of iron for treating iron deficiency in rats
    • Beard J.L., Burton J.W., Theil E.C. Purified ferritin and soybean meal can be sources of iron for treating iron deficiency in rats. J Nutr 1996, 126:154-160.
    • (1996) J Nutr , vol.126 , pp. 154-160
    • Beard, J.L.1    Burton, J.W.2    Theil, E.C.3
  • 11
    • 0035379652 scopus 로고    scopus 로고
    • A novel plant ferritin subunit from soybean that is related to a mechanism in iron release
    • Masuda T., Goto F., Yoshihara T. A novel plant ferritin subunit from soybean that is related to a mechanism in iron release. J Biol Chem 2001, 276:19575-19579.
    • (2001) J Biol Chem , vol.276 , pp. 19575-19579
    • Masuda, T.1    Goto, F.2    Yoshihara, T.3
  • 12
    • 58849146095 scopus 로고    scopus 로고
    • Two different H-type subunits from pea seed (Pisum sativum) ferritin that are responsible for fast Fe(II) oxidation
    • Li C., Hu X., Zhao G. Two different H-type subunits from pea seed (Pisum sativum) ferritin that are responsible for fast Fe(II) oxidation. Biochimie 2009, 91:230-239.
    • (2009) Biochimie , vol.91 , pp. 230-239
    • Li, C.1    Hu, X.2    Zhao, G.3
  • 13
    • 0024977973 scopus 로고
    • Mechanism of the transition from plant ferritin to phytosiderin
    • Laulhere J.P., Laboure A.M., Briat J.F. Mechanism of the transition from plant ferritin to phytosiderin. J Biol Chem 1989, 264:3629-3635.
    • (1989) J Biol Chem , vol.264 , pp. 3629-3635
    • Laulhere, J.P.1    Laboure, A.M.2    Briat, J.F.3
  • 14
    • 34249021014 scopus 로고    scopus 로고
    • Gastric digestion of pea ferritin and modulation of its iron bioavailability by ascorbic and phytic acids in Caco-2 cells
    • Bejjani S., Pullakhandam R., Punjal R., Nair K.M. Gastric digestion of pea ferritin and modulation of its iron bioavailability by ascorbic and phytic acids in Caco-2 cells. World J Gastroenterol 2007, 13:2083-2088.
    • (2007) World J Gastroenterol , vol.13 , pp. 2083-2088
    • Bejjani, S.1    Pullakhandam, R.2    Punjal, R.3    Nair, K.M.4
  • 15
    • 30844451636 scopus 로고    scopus 로고
    • Regional postprandial differences in pH within the stomach and gastroesophageal junction
    • Simonian H.P., Vo L., Doma S., Fisher R.S., Parkman H.P. Regional postprandial differences in pH within the stomach and gastroesophageal junction. Dig Dis Sci 2005, 50:2276-2285.
    • (2005) Dig Dis Sci , vol.50 , pp. 2276-2285
    • Simonian, H.P.1    Vo, L.2    Doma, S.3    Fisher, R.S.4    Parkman, H.P.5
  • 16
    • 32244434196 scopus 로고    scopus 로고
    • Characterization of the human upper gastrointestinal contents under conditions simulating bioavailability/bioequivalence studies
    • Kalantzi L., Goumas K., Kalioras V., Abrahamsson B., Dressman J.B., Reppas C. Characterization of the human upper gastrointestinal contents under conditions simulating bioavailability/bioequivalence studies. Pharm Res 2006, 23:165-176.
    • (2006) Pharm Res , vol.23 , pp. 165-176
    • Kalantzi, L.1    Goumas, K.2    Kalioras, V.3    Abrahamsson, B.4    Dressman, J.B.5    Reppas, C.6
  • 17
    • 33644869600 scopus 로고    scopus 로고
    • Iron absorption from soybean ferritin in nonanemic women
    • Lönnerdal B., Bryant A., Liu X., Theil E.C. Iron absorption from soybean ferritin in nonanemic women. Am J Clin Nutr 2006, 83:103-107.
    • (2006) Am J Clin Nutr , vol.83 , pp. 103-107
    • Lönnerdal, B.1    Bryant, A.2    Liu, X.3    Theil, E.C.4
  • 18
    • 5144224375 scopus 로고    scopus 로고
    • Iron in ferritin or in salts (ferrous sulfate) is equally bioavailable in nonanemic women
    • Davila-Hicks P., Theil E.C., Lönnerdal B. Iron in ferritin or in salts (ferrous sulfate) is equally bioavailable in nonanemic women. Am J Clin Nutr 2004, 80:936-940.
    • (2004) Am J Clin Nutr , vol.80 , pp. 936-940
    • Davila-Hicks, P.1    Theil, E.C.2    Lönnerdal, B.3
  • 22
    • 41549147443 scopus 로고    scopus 로고
    • Caco-2 intestinal epithelial cells absorb soybean ferritin by μ2 subunit (AP2)-dependent endocytosis
    • San Martin C.D., Garri C., Pizarro F., Walter T., Theil E.C., Núñez M.T. Caco-2 intestinal epithelial cells absorb soybean ferritin by μ2 subunit (AP2)-dependent endocytosis. J Nutr 2008, 138:659-666.
    • (2008) J Nutr , vol.138 , pp. 659-666
    • San Martin, C.D.1    Garri, C.2    Pizarro, F.3    Walter, T.4    Theil, E.C.5    Núñez, M.T.6
  • 23
    • 61749102565 scopus 로고    scopus 로고
    • Receptor-mediated uptake of ferritin-bound iron by human intestinal Caco-2 cells
    • Kalgaonkar S., Lönnerdal B. Receptor-mediated uptake of ferritin-bound iron by human intestinal Caco-2 cells. J Nutr Biochem 2009, 20:304-311.
    • (2009) J Nutr Biochem , vol.20 , pp. 304-311
    • Kalgaonkar, S.1    Lönnerdal, B.2
  • 24
    • 35448945259 scopus 로고    scopus 로고
    • Construction of homo- and heteropolymers of plant ferritin subunits using an in vitro protein expression system
    • Masuda T., Goto F., Yoshihara T., Ezure T., Takashi S., Kobayashi S., et al. Construction of homo- and heteropolymers of plant ferritin subunits using an in vitro protein expression system. Protein Expr Purif 2007, 56:237-246.
    • (2007) Protein Expr Purif , vol.56 , pp. 237-246
    • Masuda, T.1    Goto, F.2    Yoshihara, T.3    Ezure, T.4    Takashi, S.5    Kobayashi, S.6
  • 26
    • 84900331071 scopus 로고    scopus 로고
    • Effects of different industrial heating processes of milk on site-specific protein modifications and their relation to in vitro and in vivo digestibility
    • Wada Y., Lönnerdal B. Effects of different industrial heating processes of milk on site-specific protein modifications and their relation to in vitro and in vivo digestibility. J Agric Food Chem 2014, 62:4175-4185.
    • (2014) J Agric Food Chem , vol.62 , pp. 4175-4185
    • Wada, Y.1    Lönnerdal, B.2
  • 27
    • 84859607981 scopus 로고    scopus 로고
    • Biofortification of rice with zinc: assessment of the relative bioavailability of zinc in a Caco-2 cell model and suckling rat pups
    • Jou M.Y., Du X., Hotz C., Lönnerdal B. Biofortification of rice with zinc: assessment of the relative bioavailability of zinc in a Caco-2 cell model and suckling rat pups. J Agric Food Chem 2012, 60:3650-3657.
    • (2012) J Agric Food Chem , vol.60 , pp. 3650-3657
    • Jou, M.Y.1    Du, X.2    Hotz, C.3    Lönnerdal, B.4
  • 28
    • 0020556943 scopus 로고
    • An experimental model for studies of zinc bioavailability from milk and infant formulas using extrinsic labeling
    • Sandström B., Keen C.L., Lönnerdal B. An experimental model for studies of zinc bioavailability from milk and infant formulas using extrinsic labeling. Am J Clin Nutr 1983, 38:420-428.
    • (1983) Am J Clin Nutr , vol.38 , pp. 420-428
    • Sandström, B.1    Keen, C.L.2    Lönnerdal, B.3
  • 29
    • 79955697326 scopus 로고    scopus 로고
    • Zinc absorption from low phytic acid genotypes of maize (Zea mays L.), barley (Hordeum vulgare L.), and rice (Oryza sativa L.) assessed in a suckling rat pup model
    • Lönnerdal B., Mendoza C., Brown K.H., Rutger J.N., Raboy V. Zinc absorption from low phytic acid genotypes of maize (Zea mays L.), barley (Hordeum vulgare L.), and rice (Oryza sativa L.) assessed in a suckling rat pup model. J Agric Food Chem 2011, 59:4755-4762.
    • (2011) J Agric Food Chem , vol.59 , pp. 4755-4762
    • Lönnerdal, B.1    Mendoza, C.2    Brown, K.H.3    Rutger, J.N.4    Raboy, V.5
  • 30
    • 84896535550 scopus 로고    scopus 로고
    • Encapsulation of anthocyanin molecules within a ferritin nanocage increases their stability and cell uptake efficiency
    • Zhang T., Lv C., Chen L., Bai G., Zhao G., Xu C. Encapsulation of anthocyanin molecules within a ferritin nanocage increases their stability and cell uptake efficiency. Food Res Int 2014, 6:183-192.
    • (2014) Food Res Int , vol.6 , pp. 183-192
    • Zhang, T.1    Lv, C.2    Chen, L.3    Bai, G.4    Zhao, G.5    Xu, C.6
  • 31
    • 84898885409 scopus 로고    scopus 로고
    • Four-fold channels are involved in iron diffusion into the inner cavity of plant ferritin
    • Lv C., Zhang S., Zang J., Zhao G., Xu C. Four-fold channels are involved in iron diffusion into the inner cavity of plant ferritin. Biochemistry 2014, 53:2232-2241.
    • (2014) Biochemistry , vol.53 , pp. 2232-2241
    • Lv, C.1    Zhang, S.2    Zang, J.3    Zhao, G.4    Xu, C.5
  • 32
    • 23944512213 scopus 로고    scopus 로고
    • μ-1, 2-Peroxo diferric complex formation in horse spleen ferritin. A mixed H/L-subunit heteropolymer
    • Zhao G., Su M., Chasteen N.D. μ-1, 2-Peroxo diferric complex formation in horse spleen ferritin. A mixed H/L-subunit heteropolymer. J Mol Biol 2005, 352:467-477.
    • (2005) J Mol Biol , vol.352 , pp. 467-477
    • Zhao, G.1    Su, M.2    Chasteen, N.D.3
  • 33
    • 77952778704 scopus 로고    scopus 로고
    • A novel EP-involved pathway for iron release from soya bean seed ferritin
    • Fu X., Deng J., Yang H., Masuda T., Goto F., Yoshihara T., et al. A novel EP-involved pathway for iron release from soya bean seed ferritin. Biochem J 2010, 427:313-321.
    • (2010) Biochem J , vol.427 , pp. 313-321
    • Fu, X.1    Deng, J.2    Yang, H.3    Masuda, T.4    Goto, F.5    Yoshihara, T.6
  • 34
    • 84873742396 scopus 로고    scopus 로고
    • Stability and iron oxidation properties of a novel homopolymeric plant ferritin from adzuki bean seeds: a comparative analysis with recombinant soybean seed H-1 chain ferritin
    • Li M., Yun S., Yang X., Zhao G. Stability and iron oxidation properties of a novel homopolymeric plant ferritin from adzuki bean seeds: a comparative analysis with recombinant soybean seed H-1 chain ferritin. Biochim Biophys Acta (BBA) Gen Subj 2013, 1830:2946-2953.
    • (2013) Biochim Biophys Acta (BBA) Gen Subj , vol.1830 , pp. 2946-2953
    • Li, M.1    Yun, S.2    Yang, X.3    Zhao, G.4
  • 35
    • 42449088037 scopus 로고    scopus 로고
    • Ferritin-iron is released during boiling and in vitro gastric digestion
    • Hoppler M., Schönbächler A., Meile L., Hurrell R.F., Walczyk T. Ferritin-iron is released during boiling and in vitro gastric digestion. J Nutr 2008, 138:878-884.
    • (2008) J Nutr , vol.138 , pp. 878-884
    • Hoppler, M.1    Schönbächler, A.2    Meile, L.3    Hurrell, R.F.4    Walczyk, T.5
  • 36
    • 0020713656 scopus 로고
    • Kinetic studies of in vivo digestion of bovine unheated skim-milk proteins in the rat stomach
    • Miranda G., Pelissier J.P. Kinetic studies of in vivo digestion of bovine unheated skim-milk proteins in the rat stomach. J Dairy Res 1983, 50:27-36.
    • (1983) J Dairy Res , vol.50 , pp. 27-36
    • Miranda, G.1    Pelissier, J.P.2
  • 37
    • 36749079917 scopus 로고    scopus 로고
    • Effects of dietary factors on iron uptake from ferritin by Caco-2 cells
    • Kalgaonkar S., Lönnerdal B. Effects of dietary factors on iron uptake from ferritin by Caco-2 cells. J Nutr Biochem 2008, 19:33-39.
    • (2008) J Nutr Biochem , vol.19 , pp. 33-39
    • Kalgaonkar, S.1    Lönnerdal, B.2
  • 39
    • 33751103909 scopus 로고    scopus 로고
    • Ferroportin-mediated mobilization of ferritin iron precedes ferritin degradation by the proteasome
    • De Domenico I., Vaughn M.B., Li L., Bagley D., Musci G., Ward D.M., et al. Ferroportin-mediated mobilization of ferritin iron precedes ferritin degradation by the proteasome. EMBO J 2006, 25:5396-5404.
    • (2006) EMBO J , vol.25 , pp. 5396-5404
    • De Domenico, I.1    Vaughn, M.B.2    Li, L.3    Bagley, D.4    Musci, G.5    Ward, D.M.6
  • 40
    • 0028338934 scopus 로고
    • Identification and characterization of a receptor for tissue ferritin on activated rat lipocytes
    • Ramm G.A., Britton R.S., O'Neill R., Bacon B.R. Identification and characterization of a receptor for tissue ferritin on activated rat lipocytes. J Clin Invest 1994, 94:9-15.
    • (1994) J Clin Invest , vol.94 , pp. 9-15
    • Ramm, G.A.1    Britton, R.S.2    O'Neill, R.3    Bacon, B.R.4
  • 41
    • 0029919416 scopus 로고    scopus 로고
    • Ferritin uptake by human erythroid precursors is a regulated iron uptake pathway
    • Gelvan D., Fibach E., Meyron-Holtz E.G., Konijn A.M. Ferritin uptake by human erythroid precursors is a regulated iron uptake pathway. Blood 1996, 88:3200-3207.
    • (1996) Blood , vol.88 , pp. 3200-3207
    • Gelvan, D.1    Fibach, E.2    Meyron-Holtz, E.G.3    Konijn, A.M.4
  • 42
    • 0033137124 scopus 로고    scopus 로고
    • Distribution of transferrin and ferritin binding in normal and multiple sclerotic human brains
    • Hulet S.W., Powers S., Connor J.R. Distribution of transferrin and ferritin binding in normal and multiple sclerotic human brains. J Neurol Sci 1999, 165:48-55.
    • (1999) J Neurol Sci , vol.165 , pp. 48-55
    • Hulet, S.W.1    Powers, S.2    Connor, J.R.3
  • 43
    • 0023813241 scopus 로고
    • Isolation of a human hepatic ferritin receptor
    • Adams P.C., Powell L.W., Halliday J.W. Isolation of a human hepatic ferritin receptor. Hepatology 1988, 8:719-721.
    • (1988) Hepatology , vol.8 , pp. 719-721
    • Adams, P.C.1    Powell, L.W.2    Halliday, J.W.3
  • 44
    • 0034891444 scopus 로고    scopus 로고
    • Expression of ferritin receptor in placental microvilli membrane in pregnant women with different iron status at mid-term gestation
    • Liao Q.K., Kong P.A., Gao J., Li F.Y., Qian Z.M. Expression of ferritin receptor in placental microvilli membrane in pregnant women with different iron status at mid-term gestation. Eur J Clin Nutr 2001, 55:651-656.
    • (2001) Eur J Clin Nutr , vol.55 , pp. 651-656
    • Liao, Q.K.1    Kong, P.A.2    Gao, J.3    Li, F.Y.4    Qian, Z.M.5
  • 45
    • 77957819609 scopus 로고    scopus 로고
    • Role of H-1 and H-2 subunits of soybean seed ferritin in oxidative deposition of iron in protein
    • Deng J., Liao X., Yang H., Zhang X., Hua Z., Masuda T., et al. Role of H-1 and H-2 subunits of soybean seed ferritin in oxidative deposition of iron in protein. J Biol Chem 2010, 285:32075-32086.
    • (2010) J Biol Chem , vol.285 , pp. 32075-32086
    • Deng, J.1    Liao, X.2    Yang, H.3    Zhang, X.4    Hua, Z.5    Masuda, T.6
  • 46
    • 77957371888 scopus 로고    scopus 로고
    • Altered ferritin subunit composition: change in iron metabolism in lens epithelial cells and downstream effects on glutathione levels and VEGF secretion
    • Harned J., Ferrell J., Lall M.M., Fleisher L.N., Nagar S., Goralska M., et al. Altered ferritin subunit composition: change in iron metabolism in lens epithelial cells and downstream effects on glutathione levels and VEGF secretion. Invest Ophthalmol Vis Sci 2010, 51:4437-4446.
    • (2010) Invest Ophthalmol Vis Sci , vol.51 , pp. 4437-4446
    • Harned, J.1    Ferrell, J.2    Lall, M.M.3    Fleisher, L.N.4    Nagar, S.5    Goralska, M.6


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