메뉴 건너뛰기




Volumn 46, Issue 4, 2011, Pages 266-276

Cobalt uptake and binding in human red blood cells

Author keywords

A23187 kinetics; Co2+ buffering; Cobalt; Hemoglobin; Human red blood cell

Indexed keywords

ADENOSINE TRIPHOSPHATE; CALCIMYCIN; COBALT 57; EDETIC ACID; HEMOGLOBIN; MANGANESE 54;

EID: 79953677444     PISSN: 10799796     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcmd.2011.02.009     Document Type: Article
Times cited : (59)

References (50)
  • 1
    • 0030898548 scopus 로고    scopus 로고
    • Cytoplasmic calcium buffers in intact human red cells
    • Tiffert T., Lew V.L. Cytoplasmic calcium buffers in intact human red cells. J. Physiol. 1997, 500:139-154.
    • (1997) J. Physiol. , vol.500 , pp. 139-154
    • Tiffert, T.1    Lew, V.L.2
  • 2
    • 0018910543 scopus 로고
    • Magnesium buffering in intact human red blood cells measured using the ionophore A23187
    • Flatman P.W., Lew V.L. Magnesium buffering in intact human red blood cells measured using the ionophore A23187. J. Physiol. 1980, 30:13-30.
    • (1980) J. Physiol. , vol.30 , pp. 13-30
    • Flatman, P.W.1    Lew, V.L.2
  • 3
    • 0022558282 scopus 로고
    • Passive transport and binding of lead by human red blood cells
    • Simons T.B.J. Passive transport and binding of lead by human red blood cells. J. Physiol. 1986, 378:267-286.
    • (1986) J. Physiol. , vol.378 , pp. 267-286
    • Simons, T.B.J.1
  • 4
    • 0025785257 scopus 로고
    • Intracellular free zinc and zinc buffering in human red blood cells
    • Simons T.J.B. Intracellular free zinc and zinc buffering in human red blood cells. J. Membr. Biol. 1991, 123:63-71.
    • (1991) J. Membr. Biol. , vol.123 , pp. 63-71
    • Simons, T.J.B.1
  • 5
    • 0029968746 scopus 로고    scopus 로고
    • Mechanisms of manganese transport in rabbit erythroid cells
    • Chua A.C.G., Stonell L.M., Savigni D.L., Morgan E.H. Mechanisms of manganese transport in rabbit erythroid cells. J. Physiol. 1996, 493:99-112.
    • (1996) J. Physiol. , vol.493 , pp. 99-112
    • Chua, A.C.G.1    Stonell, L.M.2    Savigni, D.L.3    Morgan, E.H.4
  • 6
    • 0031921270 scopus 로고    scopus 로고
    • Transport mechanisms for iron and other transition metals in rat and rabbit erythroid cells
    • Savigni D.L., Morgan E.H. Transport mechanisms for iron and other transition metals in rat and rabbit erythroid cells. J. Physiol. 1998, 508:837-850.
    • (1998) J. Physiol. , vol.508 , pp. 837-850
    • Savigni, D.L.1    Morgan, E.H.2
  • 7
    • 0035156529 scopus 로고    scopus 로고
    • Mechanisms of iron transport into rat erythroid cells
    • Morgan E.H. Mechanisms of iron transport into rat erythroid cells. J. Cell. Physiol. 2001, 186:193-200.
    • (2001) J. Cell. Physiol. , vol.186 , pp. 193-200
    • Morgan, E.H.1
  • 8
    • 0642337436 scopus 로고    scopus 로고
    • Iron and magnesium influx via the low affinity iron transporter in rabbit erythroid cells-influx rates and the action of valinomycin, diethylstilbestrol and protein kinase inhibitors
    • Savigni D.L., Morgan E.H. Iron and magnesium influx via the low affinity iron transporter in rabbit erythroid cells-influx rates and the action of valinomycin, diethylstilbestrol and protein kinase inhibitors. Biochim. Biophys. Acta 2003, 1616:156-164.
    • (2003) Biochim. Biophys. Acta , vol.1616 , pp. 156-164
    • Savigni, D.L.1    Morgan, E.H.2
  • 9
    • 33645234539 scopus 로고    scopus 로고
    • The clinical significance of metal ion release from cobalt-chromium metal-on-metal hip joint arthroplasty
    • Cobb A.G., Schmalzreid T.P. The clinical significance of metal ion release from cobalt-chromium metal-on-metal hip joint arthroplasty. J Eng. Med 2006, 220-H:385-398.
    • (2006) J Eng. Med , pp. 385-398
    • Cobb, A.G.1    Schmalzreid, T.P.2
  • 10
    • 34547506619 scopus 로고    scopus 로고
    • The validity of serum levels as a surrogate measure of systemic exposure to metal ions in hip replacement
    • Daniel J., Ziaee H., Pynsent P.B., McMinn D.J.W. The validity of serum levels as a surrogate measure of systemic exposure to metal ions in hip replacement. J. Bone Joint Surg. Br. 2007, 89-B:736-741.
    • (2007) J. Bone Joint Surg. Br. , pp. 736-741
    • Daniel, J.1    Ziaee, H.2    Pynsent, P.B.3    McMinn, D.J.W.4
  • 11
    • 67651243835 scopus 로고    scopus 로고
    • Erythropoietin over-expression protects against diet-induced obesity in mice through increased fat oxidation in muscles
    • Hojman P., Brolin C., Gissel H., Brandt C., Zerahn B., Pedersen B.K. Erythropoietin over-expression protects against diet-induced obesity in mice through increased fat oxidation in muscles. PLoS ONE 2009, 4(6):e5894.
    • (2009) PLoS ONE , vol.4 , Issue.6
    • Hojman, P.1    Brolin, C.2    Gissel, H.3    Brandt, C.4    Zerahn, B.5    Pedersen, B.K.6
  • 12
    • 3142523739 scopus 로고    scopus 로고
    • HIF-1. An oxygen and metal responsive transcription factor
    • Maxwell P., Salnikow K. HIF-1. An oxygen and metal responsive transcription factor. Cancer Biol. Ther. 2004, 3:29-35.
    • (2004) Cancer Biol. Ther. , vol.3 , pp. 29-35
    • Maxwell, P.1    Salnikow, K.2
  • 13
    • 33751169387 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1 (HIF-1)
    • Ke Q., Costa M. Hypoxia-inducible factor-1 (HIF-1). Mol. Pharmacol. 2006, 70:1469-1480.
    • (2006) Mol. Pharmacol. , vol.70 , pp. 1469-1480
    • Ke, Q.1    Costa, M.2
  • 14
    • 33748902441 scopus 로고    scopus 로고
    • Hypoxia-induced erythropoietin production: a paradigm for oxygen-regulated gene expression
    • Stockmann C., Fandrey J. Hypoxia-induced erythropoietin production: a paradigm for oxygen-regulated gene expression. Clin. Exp. Pharmacol. Physiol. 2006, 33:968-979.
    • (2006) Clin. Exp. Pharmacol. Physiol. , vol.33 , pp. 968-979
    • Stockmann, C.1    Fandrey, J.2
  • 15
    • 33846963814 scopus 로고    scopus 로고
    • Erythropoietin after a century of research: younger than ever
    • Jelkmann W. Erythropoietin after a century of research: younger than ever. Eur. J. Haematol. 2007, 78:183-205.
    • (2007) Eur. J. Haematol. , vol.78 , pp. 183-205
    • Jelkmann, W.1
  • 16
    • 35148828429 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1 (HIF-1) pathway
    • Semenza G.L. Hypoxia-inducible factor 1 (HIF-1) pathway. Sci. STKE 2007, 407:cm8.
    • (2007) Sci. STKE , vol.407
    • Semenza, G.L.1
  • 17
    • 43649093915 scopus 로고    scopus 로고
    • Oxygen sensing by metazoans: the central role of the HIF hydroxylase pathway
    • Kaelin W.G., Ratcliffe P.J. Oxygen sensing by metazoans: the central role of the HIF hydroxylase pathway. Mol. Cell 2008, 30:393-402.
    • (2008) Mol. Cell , vol.30 , pp. 393-402
    • Kaelin, W.G.1    Ratcliffe, P.J.2
  • 19
    • 0028946946 scopus 로고
    • Human exposure to toxic metals: factors influencing interpretation of biomonitoring results
    • Christensen J.M. Human exposure to toxic metals: factors influencing interpretation of biomonitoring results. Sci. Total Environ. 1995, 166:89-135.
    • (1995) Sci. Total Environ. , vol.166 , pp. 89-135
    • Christensen, J.M.1
  • 20
    • 34250754537 scopus 로고    scopus 로고
    • Orthopaedic metals and their potential toxicity in the arthroplasty patient
    • Keegan G.M., Learmonth I.D., Case C.P. Orthopaedic metals and their potential toxicity in the arthroplasty patient. J. Bone Joint Surg. Br. 2007, 89-B:567-573.
    • (2007) J. Bone Joint Surg. Br. , pp. 567-573
    • Keegan, G.M.1    Learmonth, I.D.2    Case, C.P.3
  • 21
    • 84984499541 scopus 로고
    • Autoradiographic study of distribution patterns of metals which occur as corrosion products from dental restorations
    • Söremark R., Diab M., Arvidson K. Autoradiographic study of distribution patterns of metals which occur as corrosion products from dental restorations. Scand. J. Dent. Res. 1979, 87:450-458.
    • (1979) Scand. J. Dent. Res. , vol.87 , pp. 450-458
    • Söremark, R.1    Diab, M.2    Arvidson, K.3
  • 22
    • 0020773546 scopus 로고
    • The distribution in mice of radioactive cobalt administered by two different methods
    • Stenberg T. The distribution in mice of radioactive cobalt administered by two different methods. Acta Odontol. Scand. 1983, 41:143-148.
    • (1983) Acta Odontol. Scand. , vol.41 , pp. 143-148
    • Stenberg, T.1
  • 23
    • 27644552637 scopus 로고    scopus 로고
    • Cobalt chloride administration in athletes: a new perspective in blood doping?
    • Lippi G., Franchini M., Guidi G.C. Cobalt chloride administration in athletes: a new perspective in blood doping?. Br. J. Sports Med. 2005, 39:872-873.
    • (2005) Br. J. Sports Med. , vol.39 , pp. 872-873
    • Lippi, G.1    Franchini, M.2    Guidi, G.C.3
  • 24
    • 34248223079 scopus 로고    scopus 로고
    • Blood doping by cobalt. Should we measure cobalt in athletes?
    • Lippi G., Franchini M., Guidi G.C. Blood doping by cobalt. Should we measure cobalt in athletes?. J. Occup. Med. Toxicol. 2006, 1:18-20.
    • (2006) J. Occup. Med. Toxicol. , vol.1 , pp. 18-20
    • Lippi, G.1    Franchini, M.2    Guidi, G.C.3
  • 25
    • 0034530294 scopus 로고    scopus 로고
    • Improved cardiac contractile functions in hypoxia-reoxygenation in rats treated with low concentration Co2+
    • Endoh H., Kaneko T., Nakamura H., Doi K., Takahashi E. Improved cardiac contractile functions in hypoxia-reoxygenation in rats treated with low concentration Co2+. Am. J. Physiol. Heart Circ. Physiol. 2000, 279:H2713-H2719.
    • (2000) Am. J. Physiol. Heart Circ. Physiol. , vol.279
    • Endoh, H.1    Kaneko, T.2    Nakamura, H.3    Doi, K.4    Takahashi, E.5
  • 26
    • 0036825379 scopus 로고    scopus 로고
    • Microvascular remodelling after endurance training with Co2+ treatment in the rat diaphragm and hind-leg muscles
    • Suzuki J. Microvascular remodelling after endurance training with Co2+ treatment in the rat diaphragm and hind-leg muscles. Jpn J. Physiol. 2002, 52:409-419.
    • (2002) Jpn J. Physiol. , vol.52 , pp. 409-419
    • Suzuki, J.1
  • 27
    • 3042511599 scopus 로고    scopus 로고
    • Time-course changes in VEGF expression and capillarity in the early stages of exercise training with Co2+ treatment in rat skeletal muscles
    • Suzuki J. Time-course changes in VEGF expression and capillarity in the early stages of exercise training with Co2+ treatment in rat skeletal muscles. Acta Physiol. Scand. 2004, 181:225-232.
    • (2004) Acta Physiol. Scand. , vol.181 , pp. 225-232
    • Suzuki, J.1
  • 28
    • 0343547055 scopus 로고
    • Intracellular cobalt buffering by intact human red cells-evidence for time-dependent and metabolism-dependent changes
    • Brown A.M., Simonsen L.O. Intracellular cobalt buffering by intact human red cells-evidence for time-dependent and metabolism-dependent changes. J. Physiol. 1985, 361:26P.
    • (1985) J. Physiol. , vol.361
    • Brown, A.M.1    Simonsen, L.O.2
  • 29
    • 0020644375 scopus 로고
    • The effect of intracellular calcium on the sodium pump of human red cells
    • Brown A.M., Lew V.L. The effect of intracellular calcium on the sodium pump of human red cells. J. Physiol. 1983, 343:455-493.
    • (1983) J. Physiol. , vol.343 , pp. 455-493
    • Brown, A.M.1    Lew, V.L.2
  • 30
    • 0024459224 scopus 로고
    • Measurement and control of intracellular calcium in intact red cells
    • Academic Press, San Diego, CA, USA
    • Lew V.L., Garcia-Sancho J. Measurement and control of intracellular calcium in intact red cells. Methods in Enzymology 1989, Vol. 173:100-112. Academic Press, San Diego, CA, USA.
    • (1989) Methods in Enzymology , vol.173 , pp. 100-112
    • Lew, V.L.1    Garcia-Sancho, J.2
  • 31
    • 0015070760 scopus 로고
    • On the ATP dependence of the Ca2+-induced increase in K+ permeability observed in human red cells
    • Lew V.L. On the ATP dependence of the Ca2+-induced increase in K+ permeability observed in human red cells. Biochim. Biophys. Acta 1971, 233:827-830.
    • (1971) Biochim. Biophys. Acta , vol.233 , pp. 827-830
    • Lew, V.L.1
  • 32
    • 79957574728 scopus 로고
    • Calcium transport and the properties of a calcium-activated potassium channel in red cell membranes
    • Academic Press, London
    • Lew V.L., Ferreira H.G. Calcium transport and the properties of a calcium-activated potassium channel in red cell membranes. Current Topics in Membranes and Transport 1978, Vol. 10:217-277. Academic Press, London.
    • (1978) Current Topics in Membranes and Transport , vol.10 , pp. 217-277
    • Lew, V.L.1    Ferreira, H.G.2
  • 33
    • 1642297295 scopus 로고    scopus 로고
    • Voltage activation and hysteresis of the non-selective voltage-dependent channel in the intact human red cell
    • Bennekou P., Barksmann T.L., Jensen L.R., Kristensen B.I., Christophersen P. Voltage activation and hysteresis of the non-selective voltage-dependent channel in the intact human red cell. Bioelectrochemistry 2004, 62:181-185.
    • (2004) Bioelectrochemistry , vol.62 , pp. 181-185
    • Bennekou, P.1    Barksmann, T.L.2    Jensen, L.R.3    Kristensen, B.I.4    Christophersen, P.5
  • 34
    • 0021241536 scopus 로고
    • Irreversible ATP depletion caused by low concentrations of formaldehyde and of calcium-chelator esters in intact human red cells
    • Tiffert T., Garcia-Sancho J., Lew V.L. Irreversible ATP depletion caused by low concentrations of formaldehyde and of calcium-chelator esters in intact human red cells. Biochim. Biophys. Acta 1984, 773:43-156.
    • (1984) Biochim. Biophys. Acta , vol.773 , pp. 43-156
    • Tiffert, T.1    Garcia-Sancho, J.2    Lew, V.L.3
  • 35
    • 0024211677 scopus 로고
    • Maximal calcium extrusion capacity and stoichiometry of the human red cell calcium pump
    • Dagher G., Lew V.L. Maximal calcium extrusion capacity and stoichiometry of the human red cell calcium pump. J. Physiol. 1988, 407:569-586.
    • (1988) J. Physiol. , vol.407 , pp. 569-586
    • Dagher, G.1    Lew, V.L.2
  • 36
    • 0020431472 scopus 로고
    • Effects of divalent metal ions on the calcium pump and membrane phosphorylation in human red cells
    • Enyedi A., Sarkadi B., Nyers A., Gárdos G. Effects of divalent metal ions on the calcium pump and membrane phosphorylation in human red cells. Biochim. Biophys. Acta 1982, 690:41-49.
    • (1982) Biochim. Biophys. Acta , vol.690 , pp. 41-49
    • Enyedi, A.1    Sarkadi, B.2    Nyers, A.3    Gárdos, G.4
  • 37
    • 0001989630 scopus 로고
    • The plasma membrane calcium pump of erythrocytes and other animal cells
    • Academic Press, New York, E. Carafoli (Ed.)
    • Schatzmann H.J. The plasma membrane calcium pump of erythrocytes and other animal cells. Membrane Transport of Calcium 1982, 41-108. Academic Press, New York. E. Carafoli (Ed.).
    • (1982) Membrane Transport of Calcium , pp. 41-108
    • Schatzmann, H.J.1
  • 38
    • 0020376604 scopus 로고
    • Uniform ionophore A23187 distribution and cytoplasmic calcium buffering in intact human red cells
    • Simonsen L.O., Gomme J., Lew V.L. Uniform ionophore A23187 distribution and cytoplasmic calcium buffering in intact human red cells. Biochim. Biophys. Acta 1982, 692:431-440.
    • (1982) Biochim. Biophys. Acta , vol.692 , pp. 431-440
    • Simonsen, L.O.1    Gomme, J.2    Lew, V.L.3
  • 39
    • 0034565124 scopus 로고    scopus 로고
    • The non-selective voltage-activated cation channel in the human red blood cell membrane: reconciliation between two conflicting reports and further characterisation
    • Kaestner L., Christophersen P., Bernhardt I., Bennekou P. The non-selective voltage-activated cation channel in the human red blood cell membrane: reconciliation between two conflicting reports and further characterisation. Bioelectrochemistry 2000, 52:117-125.
    • (2000) Bioelectrochemistry , vol.52 , pp. 117-125
    • Kaestner, L.1    Christophersen, P.2    Bernhardt, I.3    Bennekou, P.4
  • 40
    • 0141428833 scopus 로고    scopus 로고
    • The human red cell voltage-regulated cation channel. The interplay with the chloride conductance, the Ca2+-activated K+ channel and the Ca2+ pump
    • Bennekou P., Kristensen B.I., Christophersen P. The human red cell voltage-regulated cation channel. The interplay with the chloride conductance, the Ca2+-activated K+ channel and the Ca2+ pump. J. Membr. Biol. 2003, 195:1-8.
    • (2003) J. Membr. Biol. , vol.195 , pp. 1-8
    • Bennekou, P.1    Kristensen, B.I.2    Christophersen, P.3
  • 41
    • 0018908733 scopus 로고
    • The effect of buffer composition and deoxygenation on the concentration of ionized magnesium inside human red blood cells
    • Flatman P.W. The effect of buffer composition and deoxygenation on the concentration of ionized magnesium inside human red blood cells. J. Physiol. 1980, 300:19-30.
    • (1980) J. Physiol. , vol.300 , pp. 19-30
    • Flatman, P.W.1
  • 42
    • 0014670580 scopus 로고
    • The chromium, manganese, and cobalt complexes of transferrin
    • Aisen P., Aasa R., Redfield A.G. The chromium, manganese, and cobalt complexes of transferrin. J. Biol. Chem. 1969, 244:4628-4633.
    • (1969) J. Biol. Chem. , vol.244 , pp. 4628-4633
    • Aisen, P.1    Aasa, R.2    Redfield, A.G.3
  • 43
    • 0015841510 scopus 로고
    • The labilization of haemoglobin by cobalt. Its effect on globin synthesis in reticulocytes
    • Schulman H.M., Martinez-Medellin J., Sidloi R. The labilization of haemoglobin by cobalt. Its effect on globin synthesis in reticulocytes. Eur. J. Biochem. 1973, 37:178-184.
    • (1973) Eur. J. Biochem. , vol.37 , pp. 178-184
    • Schulman, H.M.1    Martinez-Medellin, J.2    Sidloi, R.3
  • 44
    • 0027410304 scopus 로고
    • Inhibition of the calcium pump by high cytosolic Ca2+ in intact human red blood cells
    • Pereira A.C., Samellas D., Tiffert T., Lew V.L. Inhibition of the calcium pump by high cytosolic Ca2+ in intact human red blood cells. J. Physiol. 1993, 461:63-73.
    • (1993) J. Physiol. , vol.461 , pp. 63-73
    • Pereira, A.C.1    Samellas, D.2    Tiffert, T.3    Lew, V.L.4
  • 45
    • 0018119413 scopus 로고
    • Magnetic resonance studies of the binding of ATP and cations to human haemoglobin
    • Gupta R.K., Benovic J.L., Rose Z.B. Magnetic resonance studies of the binding of ATP and cations to human haemoglobin. J. Biol. Chem. 1978, 253:6165-6171.
    • (1978) J. Biol. Chem. , vol.253 , pp. 6165-6171
    • Gupta, R.K.1    Benovic, J.L.2    Rose, Z.B.3
  • 46
    • 0034633283 scopus 로고    scopus 로고
    • Application of native-state electrospray mass spectrometry to identify zinc-binding sites of engineered hemoglobin
    • Lippincott J., Fattor T.J., Lemon D.D., Apostol I. Application of native-state electrospray mass spectrometry to identify zinc-binding sites of engineered hemoglobin. Anal. Biochem. 2000, 284:247-255.
    • (2000) Anal. Biochem. , vol.284 , pp. 247-255
    • Lippincott, J.1    Fattor, T.J.2    Lemon, D.D.3    Apostol, I.4
  • 47
    • 0029905132 scopus 로고    scopus 로고
    • Ionophore 4-BrA23187 transports Zn2+ and Mn2+ with high selectivity over Ca2+
    • Erdahl W.L., Chapman C.J., Wang E., Taylor R.W., Pfeiffer D.R. Ionophore 4-BrA23187 transports Zn2+ and Mn2+ with high selectivity over Ca2+. Biochemistry 1996, 35:13817-13825.
    • (1996) Biochemistry , vol.35 , pp. 13817-13825
    • Erdahl, W.L.1    Chapman, C.J.2    Wang, E.3    Taylor, R.W.4    Pfeiffer, D.R.5
  • 48
    • 0022996803 scopus 로고
    • Delayed activation of calcium pump during transient increases in cellular Ca2+ concentration and K+ conductance in hyperpolarizing human red cells
    • Scharff O., Foder B. Delayed activation of calcium pump during transient increases in cellular Ca2+ concentration and K+ conductance in hyperpolarizing human red cells. Biochim. Biophys. Acta 1986, 861:471-479.
    • (1986) Biochim. Biophys. Acta , vol.861 , pp. 471-479
    • Scharff, O.1    Foder, B.2
  • 49
    • 0002577019 scopus 로고
    • Binding of ionophore A23187 by bovine plasma albumin
    • Simonsen L.O. Binding of ionophore A23187 by bovine plasma albumin. J. Physiol. 1981, 331:34P-35P.
    • (1981) J. Physiol. , vol.331
    • Simonsen, L.O.1
  • 50
    • 0021792016 scopus 로고
    • Near-normal circulatory survival of rabbit red cells exposed to high levels of Ca and ionophore in vitro
    • Bookchin R.M., Roth E.F., Lew V.L. Near-normal circulatory survival of rabbit red cells exposed to high levels of Ca and ionophore in vitro. Blood 1985, 66:220-223.
    • (1985) Blood , vol.66 , pp. 220-223
    • Bookchin, R.M.1    Roth, E.F.2    Lew, V.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.