메뉴 건너뛰기




Volumn 243, Issue 1-2, 1997, Pages 58-65

Characterizatlon of the correlation between ATP-dependent aminophospholipid translocation and Mg2+-ATPase activity in red blood cell membranes

Author keywords

Inhibition inhibitors; Mg2+ ATPase; P type ATPase; Phospholipid asymmetry; Pseudosubstrates

Indexed keywords

ADENOSINE TRIPHOSPHATASE (MAGNESIUM); ADENOSINE TRIPHOSPHATASE INHIBITOR; AMINOPHOSPHOLIPID; EOSIN; SURAMIN; ADENOSINE TRIPHOSPHATASE (CALCIUM MAGNESIUM); ADENOSINE TRIPHOSPHATE; MEMBRANE LIPID; PHOSPHATIDYLSERINE;

EID: 0030614439     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.58_1a.x     Document Type: Article
Times cited : (20)

References (49)
  • 1
    • 0016850035 scopus 로고
    • Rapid determination of inorganic phosphate in biological systems by a highly sensitive photometric method
    • Anner, B. & Moosmayer, M. (1975) Rapid determination of inorganic phosphate in biological systems by a highly sensitive photometric method, Anal. Biochem. 65, 305-309.
    • (1975) Anal. Biochem. , vol.65 , pp. 305-309
    • Anner, B.1    Moosmayer, M.2
  • 2
    • 0026760436 scopus 로고
    • The energy transduction mechanism is different among P-type ATPases
    • Asano, S., Kamiya, S. & Takeguchi, N. (1992) The energy transduction mechanism is different among P-type ATPases, J. Biol. Chem. 267, 6590-6595.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6590-6595
    • Asano, S.1    Kamiya, S.2    Takeguchi, N.3
  • 3
    • 0027973793 scopus 로고
    • Reconstitution of ATP-dependent aminophospholipid translocation in proteoliposomes
    • Auland, M. E., Roufogalis, B. D., Devaux, P. F. & Zachowski, A. (1994a) Reconstitution of ATP-dependent aminophospholipid translocation in proteoliposomes, Proc. Natl Acad. Sci. USA 91, 10938-10942.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 10938-10942
    • Auland, M.E.1    Roufogalis, B.D.2    Devaux, P.F.3    Zachowski, A.4
  • 6
    • 0027513151 scopus 로고
    • ATP-dependent aminophospholipid translocation in erythrocyte vesicles; stoichiometry of the transport
    • Beleznay, Zs., Zachowski, A., Devaux, P. F., Puente Navazo, M. & Ott, P. (1993a) ATP-dependent aminophospholipid translocation in erythrocyte vesicles; stoichiometry of the transport. Biochemistry 32, 3146-3152.
    • (1993) Biochemistry , vol.32 , pp. 3146-3152
    • Beleznay, Z.1    Zachowski, A.2    Devaux, P.F.3    Puente Navazo, M.4    Ott, P.5
  • 9
    • 0023620010 scopus 로고
    • Ion regulation of phosphatidylserine and phosphatidylethanolamine outside-inside translocation in human erythrocytes
    • Bitbol, M., Fellmann, P., Zachowski, A. & Devaux, P. F. (1987) Ion regulation of phosphatidylserine and phosphatidylethanolamine outside-inside translocation in human erythrocytes, Biochim. Biophys. Acta 904, 268-282.
    • (1987) Biochim. Biophys. Acta , vol.904 , pp. 268-282
    • Bitbol, M.1    Fellmann, P.2    Zachowski, A.3    Devaux, P.F.4
  • 10
    • 0025988322 scopus 로고
    • The insulin-like properties of vanadium: A curiosity or a perspective for the treatment of diabetes?
    • Brichard, S. M., Lederer, J. & Henquin, J. C. (1991) The insulin-like properties of vanadium: a curiosity or a perspective for the treatment of diabetes? Diabete & Metabolisme 17, 435-440.
    • (1991) Diabete & Metabolisme , vol.17 , pp. 435-440
    • Brichard, S.M.1    Lederer, J.2    Henquin, J.C.3
  • 12
    • 8044236523 scopus 로고
    • Alkalische Phosphatase
    • Richterich, R. & Colombo, J. P. eds S. Karger, Basel
    • Colombo, J. P. (1978) Alkalische Phosphatase, in Klinische Chemie, Theorie, Praxis, Interpretation (Richterich, R. & Colombo, J. P. eds) pp. 394-396, S. Karger, Basel.
    • (1978) Klinische Chemie, Theorie, Praxis, Interpretation , pp. 394-396
    • Colombo, J.P.1
  • 13
    • 0022371311 scopus 로고
    • Incorporation and translocation of aminophospolipids in human erythrocytes
    • Daleke, D. L. & Huestis, W. H. (1985) Incorporation and translocation of aminophospolipids in human erythrocytes, Biochemistry 24, 5406-5416.
    • (1985) Biochemistry , vol.24 , pp. 5406-5416
    • Daleke, D.L.1    Huestis, W.H.2
  • 14
    • 0027322674 scopus 로고
    • Inhibitory effect of modified batilomycins and concanamycins on P- and V-type adenosinetriphosphatases
    • Dröse, S., Bindseil, K. U., Bowman, E. J., Siebers, A., Zeeck, A. & Altendorf, K. (1993) Inhibitory effect of modified batilomycins and concanamycins on P- and V-type adenosinetriphosphatases, Biochemistry 32, 3902-3906.
    • (1993) Biochemistry , vol.32 , pp. 3902-3906
    • Dröse, S.1    Bindseil, K.U.2    Bowman, E.J.3    Siebers, A.4    Zeeck, A.5    Altendorf, K.6
  • 15
    • 0015847462 scopus 로고
    • Suramin: A potent ATPase inhibitor which acts on the inside surface of the sodium pump
    • Fortes, P. A. G., Ellory, J. C. & Lew, V. L. (1973) Suramin: a potent ATPase inhibitor which acts on the inside surface of the sodium pump, Biochim. Biophys. Acta 318, 262-272.
    • (1973) Biochim. Biophys. Acta , vol.318 , pp. 262-272
    • Fortes, P.A.G.1    Ellory, J.C.2    Lew, V.L.3
  • 16
    • 0027269893 scopus 로고
    • Inhibition of red blood cell calcium pump by cosin and other fluorescein analogues
    • Gatto, C. & Milanick, M. A. (1993) Inhibition of red blood cell calcium pump by cosin and other fluorescein analogues, Am. J. Physiol. 264, C1577-C1586.
    • (1993) Am. J. Physiol. , vol.264
    • Gatto, C.1    Milanick, M.A.2
  • 17
    • 0028898297 scopus 로고
    • Eosin, a potent inhibitor of the plasma membrane Ca pump, does not inhibit the cardiac Na-Ca exchanger
    • Gatto, C., Hale, C. C., Wanyan, X. & Milanick, M. A. (1995) Eosin, a potent inhibitor of the plasma membrane Ca pump, does not inhibit the cardiac Na-Ca exchanger, Biochemistry 34, 965-972.
    • (1995) Biochemistry , vol.34 , pp. 965-972
    • Gatto, C.1    Hale, C.C.2    Wanyan, X.3    Milanick, M.A.4
  • 18
    • 0025310050 scopus 로고
    • Is the glutathione S-conjugate carrier an mdr1 gene product?
    • Ishikawa, T. (1990) Is the glutathione S-conjugate carrier an mdr1 gene product? Trends Biochem. Sci. 15, 219-220.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 219-220
    • Ishikawa, T.1
  • 19
    • 0027190678 scopus 로고
    • Protein export function and in vitro ATPase activity are correlated in ABC-domain mutants of HlyB
    • Koronakis, V., Hughes, C. & Koronakis, E. (1993) Protein export function and in vitro ATPase activity are correlated in ABC-domain mutants of HlyB, Mol. Microbiol. 8, 1163-1175.
    • (1993) Mol. Microbiol. , vol.8 , pp. 1163-1175
    • Koronakis, V.1    Hughes, C.2    Koronakis, E.3
  • 20
    • 0016168782 scopus 로고
    • Suramin: A potent inhibitor of the calcium transport in sarcoplasmic reticulum
    • Layton, D. & Azzi, A. (1974) Suramin: a potent inhibitor of the calcium transport in sarcoplasmic reticulum, Biochem. Biophys. Res. Commun. 59, 322-325.
    • (1974) Biochem. Biophys. Res. Commun. , vol.59 , pp. 322-325
    • Layton, D.1    Azzi, A.2
  • 21
    • 85093986891 scopus 로고
    • Dynamics of the holes in human erythrocyte membrane ghosts
    • Lieber, M. R. & Steck, T. L. (1982) Dynamics of the holes in human erythrocyte membrane ghosts, J. Biol. Chem. 257, 11 660-11 666.
    • (1982) J. Biol. Chem. , vol.257 , pp. 11660-11666
    • Lieber, M.R.1    Steck, T.L.2
  • 22
    • 0018953667 scopus 로고
    • Glutathione reduces cytoplasmic vanadate, mechanism and physiological implications
    • Macara, I. G., Kustin, K. & Cantley, L. C. Jr (1980) Glutathione reduces cytoplasmic vanadate, mechanism and physiological implications, Biochim. Biophys. Acta 629, 95-106.
    • (1980) Biochim. Biophys. Acta , vol.629 , pp. 95-106
    • Macara, I.G.1    Kustin, K.2    Cantley Jr., L.C.3
  • 23
    • 0014690701 scopus 로고
    • + and adenosine triphosphate
    • + and adenosine triphosphate, J. Biol. Chem. 244, 3733-3739.
    • (1969) J. Biol. Chem. , vol.244 , pp. 3733-3739
    • De Meis, L.1
  • 24
    • 0025780777 scopus 로고
    • Vanadate-sensitive ATPase from chromaffine granule membranes formed a phosphoenzyme intermediate and was activated by phosphatidylserine
    • Moriyama, Y., Nelson, N., Maeda, M. & Futai, M. (1991) Vanadate-sensitive ATPase from chromaffine granule membranes formed a phosphoenzyme intermediate and was activated by phosphatidylserine, Arch. Biochem. Biophys. 286, 252-256.
    • (1991) Arch. Biochem. Biophys. , vol.286 , pp. 252-256
    • Moriyama, Y.1    Nelson, N.2    Maeda, M.3    Futai, M.4
  • 26
    • 0024566916 scopus 로고
    • Aminophospholipid translocase of human erythrocytes: Phospholipid substrate specificity and effect of cholesterol
    • Morrot, G., Hervé, P., Zachowski, A., Fellmann, P. & Devaux, P. F. (1989) Aminophospholipid translocase of human erythrocytes: Phospholipid substrate specificity and effect of cholesterol. Biochemistry 28, 3456-3462.
    • (1989) Biochemistry , vol.28 , pp. 3456-3462
    • Morrot, G.1    Hervé, P.2    Zachowski, A.3    Fellmann, P.4    Devaux, P.F.5
  • 27
    • 0028915482 scopus 로고
    • Mechanism of the change in shape of human erythrocytes induced by lidocaine
    • Nishiguchi, E., Ozono, S., Takakuwa, Y. & Hamasaki, N. (1995) Mechanism of the change in shape of human erythrocytes induced by lidocaine, Cell. Struct. Func. 20, 71-79.
    • (1995) Cell. Struct. Func. , vol.20 , pp. 71-79
    • Nishiguchi, E.1    Ozono, S.2    Takakuwa, Y.3    Hamasaki, N.4
  • 28
    • 0014802297 scopus 로고
    • Metabolism of external adenine nucleotides by human red blood cells
    • Parker, J. C. (1970) Metabolism of external adenine nucleotides by human red blood cells, Am. J. Physiol. 218, 1568-1574.
    • (1970) Am. J. Physiol. , vol.218 , pp. 1568-1574
    • Parker, J.C.1
  • 29
    • 33646830005 scopus 로고
    • Ion motive ATPases. I. Ubiquity, properties, and significance to cell function
    • Pederson, P. L. & Carafoli, E. (1987) Ion motive ATPases. I. Ubiquity, properties, and significance to cell function, Trends Biochem. Sci. 12, 146-150.
    • (1987) Trends Biochem. Sci. , vol.12 , pp. 146-150
    • Pederson, P.L.1    Carafoli, E.2
  • 30
    • 0017613512 scopus 로고
    • A simplification of the protein assay method of Lowry et al. which is more generally applicable
    • Peterson, G. L. (1977) A simplification of the protein assay method of Lowry et al. which is more generally applicable, Anal. Biochem. 83, 346-356.
    • (1977) Anal. Biochem. , vol.83 , pp. 346-356
    • Peterson, G.L.1
  • 31
    • 0027988235 scopus 로고
    • Organic anion-transporting ATPase of rat liver
    • Pikula S., Hayden, J. B., Awasthi, S. & Zimniak, P. (1994) Organic anion-transporting ATPase of rat liver, J. Biol. Chem. 269, 27566-27573.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27566-27573
    • Pikula, S.1    Hayden, J.B.2    Awasthi, S.3    Zimniak, P.4
  • 32
    • 0027158879 scopus 로고
    • The MgIA component of the binding protein-dependent galactose transport system of Salmonella typhimurium is a galactose-slimulated ATPase
    • Richarme, G., el Yaagoubi, A. & Kohiyama, M. (1993) The MgIA component of the binding protein-dependent galactose transport system of Salmonella typhimurium is a galactose-slimulated ATPase, J. Biol. Chem. 268, 9473-9477.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9473-9477
    • Richarme, G.1    El Yaagoubi, A.2    Kohiyama, M.3
  • 33
    • 0344683171 scopus 로고
    • Improved procedure for the extraction of lipids from human erythrocytes
    • Rose, H. G. & Oklander, M. (1965) Improved procedure for the extraction of lipids from human erythrocytes, J. Lipid Res. 6, 428-431.
    • (1965) J. Lipid Res. , vol.6 , pp. 428-431
    • Rose, H.G.1    Oklander, M.2
  • 35
    • 0014779155 scopus 로고
    • Two-dimensional thin layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots
    • Rouser, G., Fleischer, S. & Yamamoto, A. (1970) Two-dimensional thin layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots, Lipids 5, 494-496.
    • (1970) Lipids , vol.5 , pp. 494-496
    • Rouser, G.1    Fleischer, S.2    Yamamoto, A.3
  • 36
    • 0028307550 scopus 로고
    • Phosphatidylcholine translocase: A physiological role for the mrd2 gene
    • Ruetz, S. & Gros, P. (1994) Phosphatidylcholine translocase: A physiological role for the mrd2 gene, Cell 77, 1071-1081.
    • (1994) Cell , vol.77 , pp. 1071-1081
    • Ruetz, S.1    Gros, P.2
  • 37
    • 0022782816 scopus 로고
    • Characterization of human erythrocyte cytoskeletal ATPase
    • Sato, S., Jinbu, Y. & Nakao, M. (1986) Characterization of human erythrocyte cytoskeletal ATPase, J. Biochem. 100, 643-649.
    • (1986) J. Biochem. , vol.100 , pp. 643-649
    • Sato, S.1    Jinbu, Y.2    Nakao, M.3
  • 38
    • 0001505065 scopus 로고
    • ATP dependent asymmetric distribution of spin labeled phospholipids in the erythrocyte membrane relation to shape
    • Seigneuret, M. & Devaux, P. F. (1984) ATP dependent asymmetric distribution of spin labeled phospholipids in the erythrocyte membrane relation to shape, Proc. Natl Acad. Sci. USA 81, 3751-3755.
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 3751-3755
    • Seigneuret, M.1    Devaux, P.F.2
  • 39
    • 0027937143 scopus 로고
    • Reconstitution of drug transport by purified P-glycoprotein
    • Shapiro, A. B. & Ling, V. (1994) Reconstitution of drug transport by purified P-glycoprotein, J. Biol. Chem. 269, 3745-3754.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3745-3754
    • Shapiro, A.B.1    Ling, V.2
  • 41
    • 0029437151 scopus 로고
    • Inhibition of phosphate-metabolizing enzymes by oxovanadium(V) complexes
    • Stankiewicz, P. J., Tracey, A. S. & Crans, D. C. (1995) Inhibition of phosphate-metabolizing enzymes by oxovanadium(V) complexes, Met. Ions Biol. Syst. 31, 287-324.
    • (1995) Met. Ions Biol. Syst. , vol.31 , pp. 287-324
    • Stankiewicz, P.J.1    Tracey, A.S.2    Crans, D.C.3
  • 42
    • 77957008400 scopus 로고
    • Preparation and assay of acetyl phosphate
    • Stadtman, E. R. (1957) Preparation and assay of acetyl phosphate, Methods Enzymol. 3, 228-230.
    • (1957) Methods Enzymol. , vol.3 , pp. 228-230
    • Stadtman, E.R.1
  • 43
    • 0016360444 scopus 로고
    • Preparation of impermeable ghosts and inside-out vesicles from human erythrocyte membranes
    • Steck, T. L. & Kant, J. A. (1974) Preparation of impermeable ghosts and inside-out vesicles from human erythrocyte membranes, Methods Enzymol. 31, 172-180.
    • (1974) Methods Enzymol. , vol.31 , pp. 172-180
    • Steck, T.L.1    Kant, J.A.2
  • 44
    • 0018242065 scopus 로고
    • Molecular mechanism of active calcium transport by sarcoplasmic reticulum
    • Tada, M., Yamamoto, T. & Tonomura, Y. (1978) Molecular mechanism of active calcium transport by sarcoplasmic reticulum, Physiol. Rev. 58, 1-79.
    • (1978) Physiol. Rev. , vol.58 , pp. 1-79
    • Tada, M.1    Yamamoto, T.2    Tonomura, Y.3
  • 45
    • 0022635635 scopus 로고
    • ATP-dependent translocation of aminophospholipids across the human erythrocyte membrane
    • Tilley, L., Cribier, S., Roelofsen, B., Op den Kamp, J. A. F. & van Deenen, L. L. M. (1986) ATP-dependent translocation of aminophospholipids across the human erythrocyte membrane, FEBS Lett. 194, 21-27.
    • (1986) FEBS Lett. , vol.194 , pp. 21-27
    • Tilley, L.1    Cribier, S.2    Roelofsen, B.3    Op Den Kamp, J.A.F.4    Van Deenen, L.L.M.5
  • 46
    • 0024506317 scopus 로고
    • Identification of a kinesin-like microtubule-based motor protein in Dictyostelium discoideum
    • Wagner, M. C., Pfister, K. K., Bloom, G. S. & Brady, S. T. (1989) Identification of a kinesin-like microtubule-based motor protein in Dictyostelium discoideum, Cell. Motil. Cytoskel., 12, 195-215.
    • (1989) Cell. Motil. Cytoskel. , vol.12 , pp. 195-215
    • Wagner, M.C.1    Pfister, K.K.2    Bloom, G.S.3    Brady, S.T.4
  • 47
    • 0028172257 scopus 로고
    • 2,4-Dinitrophenol and carbonylcyanide p-trifluoromethoxyphenylhydrazone activate the glutathione S-conjugate transport ATPase of human erythrocyte membranes
    • Winter, C. G., DeLuca, D. C. & Szumilo, H. (1994) 2,4-Dinitrophenol and carbonylcyanide p-trifluoromethoxyphenylhydrazone activate the glutathione S-conjugate transport ATPase of human erythrocyte membranes, Arch. Biochem. Biophys. 314, 17-22.
    • (1994) Arch. Biochem. Biophys. , vol.314 , pp. 17-22
    • Winter, C.G.1    DeLuca, D.C.2    Szumilo, H.3
  • 48
    • 0022545254 scopus 로고
    • Outside-inside translocation of aminophospholipids in the human erythrocyte membrane is mediated by a specific enzyme
    • Zachowski, A., Favre, E., Cribier, S., Hervé, P. & Devaux, P. F. (1986) Outside-inside translocation of aminophospholipids in the human erythrocyte membrane is mediated by a specific enzyme, Biochemistry 25, 2585-2590.
    • (1986) Biochemistry , vol.25 , pp. 2585-2590
    • Zachowski, A.1    Favre, E.2    Cribier, S.3    Hervé, P.4    Devaux, P.F.5
  • 49
    • 0025976707 scopus 로고
    • Pre-steady-state and steady-state kinetic analysis of the low molecular mass phosphotyrosyl protein phosphatase from bovine heart
    • Zhang, Z.-Y. & Van Etten, R. L. (1991) Pre-steady-state and steady-state kinetic analysis of the low molecular mass phosphotyrosyl protein phosphatase from bovine heart, J. Biol. Chem. 266, 1516-1525.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1516-1525
    • Zhang, Z.-Y.1    Van Etten, R.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.