메뉴 건너뛰기




Volumn 14, Issue 4, 2010, Pages 245-252

Effects of ATP and ADP on iron uptake in rat heart mitochondria

Author keywords

ADP; ATP; Divalent metal ion; Heart mitochondria; Iron uptake

Indexed keywords

RATTUS;

EID: 79957651230     PISSN: 19768354     EISSN: 21512485     Source Type: Journal    
DOI: 10.1080/19768354.2010.525836     Document Type: Article
Times cited : (2)

References (40)
  • 2
    • 0036024973 scopus 로고    scopus 로고
    • In vivo and in organello assessment of oxphos activities
    • Barrientos A. 2002. In vivo and in organello assessment of oxphos activities. Methods. 26:307-316.
    • (2002) Methods , vol.26 , pp. 307-316
    • Barrientos, A.1
  • 3
    • 0025055329 scopus 로고
    • The cationically selective state of the mitochondrial outer membrane pore: A study with intact mitochondria and reconstituted mitochondrial porin
    • Benz R, Kottke M, Brdiczka D. 1990. The cationically selective state of the mitochondrial outer membrane pore: a study with intact mitochondria and reconstituted mitochondrial porin. Biochim Biophys Acta. 1022:311-318.
    • (1990) Biochim Biophys Acta , vol.1022 , pp. 311-318
    • Benz, R.1    Kottke, M.2    Brdiczka, D.3
  • 4
    • 0342669907 scopus 로고
    • Sideroblastic anaemia, mitochondria and erythroblastic iron
    • Bessis MC, Jensen WN. 1965. Sideroblastic anaemia, mitochondria and erythroblastic iron. Br J Haematol. 11: 49-51.
    • (1965) Br J Haematol , vol.11 , pp. 49-51
    • Bessis, M.C.1    Jensen, W.N.2
  • 5
    • 0016593950 scopus 로고
    • 2+ uptake supported by hydrolysis of endogenous ATP in rat liver mitochondria
    • 2+ uptake supported by hydrolysis of endogenous ATP in rat liver mitochondria. J Biol Chem. 250:7958-7960.
    • (1975) J Biol Chem , vol.250 , pp. 7958-7960
    • Brand, M.D.1    Lehninger, A.L.2
  • 6
    • 0015523308 scopus 로고
    • Binding of iron and copper to bovine heart mitochondria. II. Effect of mitochondrial metabolism
    • Cederbaum AI, Wainio WW. 1972. Binding of iron and copper to bovine heart mitochondria. II. Effect of mitochondrial metabolism. J Biol Chem. 247:4604-4614.
    • (1972) J Biol Chem , vol.247 , pp. 4604-4614
    • Cederbaum, A.I.1    Wainio, W.W.2
  • 7
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • Chance B, Sies H, Boveris A. 1979. Hydroperoxide metabolism in mammalian organs. Physiol Rev. 59:527-605.
    • (1979) Physiol Rev , vol.59 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 9
    • 0026519544 scopus 로고
    • Transmembrane arrangement of mitochondrial porin or voltage-dependent anion channel (VDAC)
    • De Pinto VD, Palmieri F. 1992. Transmembrane arrangement of mitochondrial porin or voltage-dependent anion channel (VDAC). J Bioenerg Biomembr. 24:21-26.
    • (1992) J Bioenerg Biomembr , vol.24 , pp. 21-26
    • de Pinto, V.D.1    Palmieri, F.2
  • 11
    • 0022558529 scopus 로고
    • Lipid enrichment and fusion of mitochondrial inner membranes
    • Hackenbrock CR, Chazotte B. 1986. Lipid enrichment and fusion of mitochondrial inner membranes. Methods Enzymol. 125:35-43.
    • (1986) Methods Enzymol , vol.125 , pp. 35-43
    • Hackenbrock, C.R.1    Chazotte, B.2
  • 12
    • 0021294830 scopus 로고
    • Role of iron in oxygen radical reactions
    • Halliwell B, Gutteridge JM. 1984. Role of iron in oxygen radical reactions. Methods Enzymol. 105:47-56.
    • (1984) Methods Enzymol , vol.105 , pp. 47-56
    • Halliwell, B.1    Gutteridge, J.M.2
  • 13
    • 77049308856 scopus 로고
    • Aging: A theory based on free radical and radiation chemistry
    • Harman D. 1956. Aging: a theory based on free radical and radiation chemistry. J Gerontol. 11:298-300.
    • (1956) J Gerontol , vol.11 , pp. 298-300
    • Harman, D.1
  • 14
    • 0015319592 scopus 로고
    • A biologic clock: The mitochondria?
    • Harman D. 1972. A biologic clock: the mitochondria? J Am Geriat Soc. 20:145-147.
    • (1972) J Am Geriat Soc , vol.20 , pp. 145-147
    • Harman, D.1
  • 15
    • 0034014265 scopus 로고    scopus 로고
    • Control of the mitochondrial permeability transition pore by high-affinity ADP binding at the ADP/ATP translocase in permeabilized mitochondria
    • Haworth RA, Hunter DR. 2000. Control of the mitochondrial permeability transition pore by high-affinity ADP binding at the ADP/ATP translocase in permeabilized mitochondria. J Bioenerg Biomembr. 32:91-96.
    • (2000) J Bioenerg Biomembr , vol.32 , pp. 91-96
    • Haworth, R.A.1    Hunter, D.R.2
  • 16
    • 0018140977 scopus 로고
    • Relation between high energy phosphate and lethal injury in myocardial ischemia in the dog
    • Jennings RB, Hawkins HK, Lowe JE, Hill ML, Klotman S, Reimer KA. 1978. Relation between high energy phosphate and lethal injury in myocardial ischemia in the dog. Am J Pathol. 92:187-214.
    • (1978) Am J Pathol , vol.92 , pp. 187-214
    • Jennings, R.B.1    Hawkins, H.K.2    Lowe, J.E.3    Hill, M.L.4    Klotman, S.5    Reimer, K.A.6
  • 17
    • 0021894480 scopus 로고
    • Nucleotide metabolism and cellular damage in myocardial ischemia
    • Jennings RB, Steenbergen C Jr. 1985. Nucleotide metabolism and cellular damage in myocardial ischemia. Annu Rev Physiol. 47:727-749.
    • (1985) Annu Rev Physiol , vol.47 , pp. 727-749
    • Jennings, R.B.1    Steenbergen Jr., C.2
  • 18
    • 40549117465 scopus 로고    scopus 로고
    • Increased expression of the F1F0 ATP synthase in response to iron in heart mitochondria
    • Kim M, Kim J, Cheon C-I, Cho DH, Park JH, Kim KI, Lee K-H, Song E. 2008. Increased expression of the F1F0 ATP synthase in response to iron in heart mitochondria. BMB Rep. 2:153-157.
    • (2008) BMB Rep , vol.2 , pp. 153-157
    • Kim, M.1    Kim, J.2    Cheon, C.-I.3    Cho, D.H.4    Park, J.H.5    Kim, K.I.6    Lee, K.-H.7    Song, E.8
  • 19
    • 77649191099 scopus 로고    scopus 로고
    • Iron transport by proteolipoosomes containing mitochondrial F1Fo ATP synthase isolated from rat heart
    • Kim M, Song E. 2010. Iron transport by proteolipoosomes containing mitochondrial F1Fo ATP synthase isolated from rat heart. Biochimie 92:333-342.
    • (2010) Biochimie , vol.92 , pp. 333-342
    • Kim, M.1    Song, E.2
  • 20
    • 52049113898 scopus 로고    scopus 로고
    • The ADP and ATP transport in mitochondria and its carrier
    • Klingenberg M. 2008. The ADP and ATP transport in mitochondria and its carrier. Biochim Biophys Acta. 1778:1978-2021.
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 1978-2021
    • Klingenberg, M.1
  • 21
    • 0037809232 scopus 로고    scopus 로고
    • Mitochondrial ATP synthasome. Cristae-enriched membranes and a multiwell detergent screening assay yield dispersed single complexes containing the ATP synthase and carriers for Pi and ADP/ATP
    • Ko YH, Delannoy M, Hullihen J, Chiu W, Pedersen PL. 2003. Mitochondrial ATP synthasome. Cristae-enriched membranes and a multiwell detergent screening assay yield dispersed single complexes containing the ATP synthase and carriers for Pi and ADP/ATP. J Biol Chem. 278:12305-12309.
    • (2003) J Biol Chem , vol.278 , pp. 12305-12309
    • Ko, Y.H.1    Delannoy, M.2    Hullihen, J.3    Chiu, W.4    Pedersen, P.L.5
  • 22
    • 0033516467 scopus 로고    scopus 로고
    • Mechanism of iron transport to the site of heme synthesis inside yeast mitochondria
    • Lange H, Kispal G, Lill R. 1999. Mechanism of iron transport to the site of heme synthesis inside yeast mitochondria. J Biol Chem. 274:18989-18996.
    • (1999) J Biol Chem , vol.274 , pp. 18989-18996
    • Lange, H.1    Kispal, G.2    Lill, R.3
  • 23
    • 67349165712 scopus 로고    scopus 로고
    • The role of iron in mitochondrial function
    • Levi S, Rovida E. 2009. The role of iron in mitochondrial function. Biochim Biophys Acta. 1790:629-636.
    • (2009) Biochim Biophys Acta , vol.1790 , pp. 629-636
    • Levi, S.1    Rovida, E.2
  • 25
    • 0024336003 scopus 로고
    • Fluorescent indicators for cytosolic calcium based on rhodamine and fluorescein chromophores
    • Minta A, Kao JPY, Tsien RY. 1989. Fluorescent indicators for cytosolic calcium based on rhodamine and fluorescein chromophores. J Biol Chem. 264:8171-8178.
    • (1989) J Biol Chem , vol.264 , pp. 8171-8178
    • Minta, A.1    Kao, J.P.Y.2    Tsien, R.Y.3
  • 26
    • 44349138089 scopus 로고    scopus 로고
    • 2+ uniporter involves proton flux through the ATP synthase
    • 2+ uniporter involves proton flux through the ATP synthase. Curr Biol. 18:855-859.
    • (2008) Curr Biol , vol.18 , pp. 855-859
    • Moreau, B.1    Parekh, A.B.2
  • 27
    • 0020491332 scopus 로고
    • Regulation of mitochondrial malate dehydrogenase. Evidence for an allosteric citrate-binding site
    • Mullinax TR, Mock JN, McEvily AJ, Harrison JH. 1982. Regulation of mitochondrial malate dehydrogenase. Evidence for an allosteric citrate-binding site. J Biol Chem. 257:13233-13239.
    • (1982) J Biol Chem , vol.257 , pp. 13233-13239
    • Mullinax, T.R.1    Mock, J.N.2    McEvily, A.J.3    Harrison, J.H.4
  • 28
    • 14944387002 scopus 로고    scopus 로고
    • Iron trafficking in the mitochondrion: Novel pathways revealed by disease
    • Napier I, Ponka P, Richardson DR. 2005. Iron trafficking in the mitochondrion: novel pathways revealed by disease. Blood. 105:1867-1874.
    • (2005) Blood , vol.105 , pp. 1867-1874
    • Napier, I.1    Ponka, P.2    Richardson, D.R.3
  • 29
    • 0015238979 scopus 로고
    • Reversible inhibition of mitochondrial adenosine diphosphate phosphorylation by long chain acyl coenzyme A esters
    • Pande SV, Blanchaer MC. 1971. Reversible inhibition of mitochondrial adenosine diphosphate phosphorylation by long chain acyl coenzyme A esters. J Biol Chem. 246:402-411.
    • (1971) J Biol Chem , vol.246 , pp. 402-411
    • Pande, S.V.1    Blanchaer, M.C.2
  • 30
    • 34248640533 scopus 로고    scopus 로고
    • Metal Ion availability in mitochondria
    • Pierrel F, Cobine PA, Winge DR. 2007. Metal Ion availability in mitochondria. Biometals. 20:675-682.
    • (2007) Biometals , vol.20 , pp. 675-682
    • Pierrel, F.1    Cobine, P.A.2    Winge, D.R.3
  • 32
    • 0016661023 scopus 로고
    • Energy-dependent accumulation of iron by isolated rat liver mitochondria. IV. Relationship to the energy state of the mitochondria
    • Romslo I. 1975. Energy-dependent accumulation of iron by isolated rat liver mitochondria. IV. Relationship to the energy state of the mitochondria. Biochim Biophys Acta. 387:69-79.
    • (1975) Biochim Biophys Acta , vol.387 , pp. 69-79
    • Romslo, I.1
  • 34
    • 0016167211 scopus 로고
    • Energy-dependent accumulation of iron by isolated rat liver mitochondria. 3. Submitochondrial localization of the iron accumulated
    • Romslo I, Flatmark T. 1974. Energy-dependent accumulation of iron by isolated rat liver mitochondria. 3. Submitochondrial localization of the iron accumulated. Biochim Biophys Acta. 347:160-167.
    • (1974) Biochim Biophys Acta , vol.347 , pp. 160-167
    • Romslo, I.1    Flatmark, T.2
  • 35
    • 0016366597 scopus 로고
    • Adenylate kinase in human tissue. I. Organ specificity of adenylate kinase isoenzymes
    • Russell PJ Jr, Horenstein JM, Goins L, Jones D, Laver M. 1974. Adenylate kinase in human tissue. I. Organ specificity of adenylate kinase isoenzymes. J Biol Chem. 249:1874-1879.
    • (1974) J Biol Chem , vol.249 , pp. 1874-1879
    • Russell Jr., P.J.1    Horenstein, J.M.2    Goins, L.3    Jones, D.4    Laver, M.5
  • 38
    • 17144417734 scopus 로고    scopus 로고
    • A historical review of cellular calcium handling with emphasis on mitochondria
    • Saris NE, Carafoli E. 2005. A historical review of cellular calcium handling with emphasis on mitochondria. Biochemistry (Mosc) 70:187-194.
    • (2005) Biochemistry (Mosc) , vol.70 , pp. 187-194
    • Saris, N.E.1    Carafoli, E.2
  • 39
    • 0023547633 scopus 로고
    • Radical-driven Fenton reactions: Studies with paraquat, adriamycin, and anthraquinone 6-sulfonate and citrate, ATP, ADP, and pyrophosphate iron chelates
    • Vile GF, Winterbourn CC, Sutton HC. 1987. Radical-driven Fenton reactions: studies with paraquat, adriamycin, and anthraquinone 6-sulfonate and citrate, ATP, ADP, and pyrophosphate iron chelates. Arch Biochem Biophys. 259:616-626.
    • (1987) Arch Biochem Biophys , vol.259 , pp. 616-626
    • Vile, G.F.1    Winterbourn, C.C.2    Sutton, H.C.3
  • 40
    • 0014670957 scopus 로고
    • The location of different synthetic systems for fatty acids in inner and outer mitochondrial membranes from rabbit heart
    • Whereat AF, Orishino MW, Nelson J. 1969. The location of different synthetic systems for fatty acids in inner and outer mitochondrial membranes from rabbit heart. J Biol Chem. 244:6498-6506.
    • (1969) J Biol Chem , vol.244 , pp. 6498-6506
    • Whereat, A.F.1    Orishino, M.W.2    Nelson, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.