메뉴 건너뛰기




Volumn 253, Issue 3, 1998, Pages 627-636

Dicyclohexylcarbodiimide interaction with the voltage-dependent anion channel from sarcoplasmic reticulum

Author keywords

ATP transport; Dicyclohexylcarbodiimide; Sarcoplasmic reticulum; Single channel; Voltage dependent anion channel

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM MAGNESIUM); ADENOSINE TRIPHOSPHATE; ANION CHANNEL; DICYCLOHEXYLCARBODIIMIDE;

EID: 0032080218     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2530627.x     Document Type: Article
Times cited : (26)

References (40)
  • 1
    • 0021646029 scopus 로고
    • 2+ release from sarcoplasmic reticulum of skeletal muscle
    • 2+ release from sarcoplasmic reticulum of skeletal muscle, Physiol. Rev. 64, 1240-1319.
    • (1984) Physiol. Rev. , vol.64 , pp. 1240-1319
    • Martonosi, A.N.1
  • 2
    • 0025982123 scopus 로고
    • Excitation-contraction coupling and the mechanism of muscle contraction
    • Ehashi, S. (1991) Excitation-contraction coupling and the mechanism of muscle contraction, Annu. Rev. Physiol. 53, 1-16.
    • (1991) Annu. Rev. Physiol. , vol.53 , pp. 1-16
    • Ehashi, S.1
  • 4
    • 0027938197 scopus 로고
    • Immunolabelling of VDAC, the mitochondrial voltage-dependent anion channel, on sarcoplasmic reticulum from amphibian skeletal muscle
    • Lewis, T. M., Roberts, M. L. & Bretag, A. H. (1994) Immunolabelling of VDAC, the mitochondrial voltage-dependent anion channel, on sarcoplasmic reticulum from amphibian skeletal muscle, Neurosci. Lett. 181, 83-86.
    • (1994) Neurosci. Lett. , vol.181 , pp. 83-86
    • Lewis, T.M.1    Roberts, M.L.2    Bretag, A.H.3
  • 8
    • 0026730943 scopus 로고
    • The 'ins' and 'outs' of mitochondrial membrane channels
    • Mannella, C. A. (1992) The 'ins' and 'outs' of mitochondrial membrane channels, Trends Biol. Sci. 17, 315-320.
    • (1992) Trends Biol. Sci. , vol.17 , pp. 315-320
    • Mannella, C.A.1
  • 9
    • 0028341536 scopus 로고
    • Permeation of hydrophilic solutes through mitochondrial outer membranes: Review on mitochondrial porins
    • Benz, R. (1994) Permeation of hydrophilic solutes through mitochondrial outer membranes: review on mitochondrial porins, Biochim. Biophys. Acta 1197, 167-196.
    • (1994) Biochim. Biophys. Acta , vol.1197 , pp. 167-196
    • Benz, R.1
  • 10
    • 0029018094 scopus 로고
    • Further evidence for multitopological localization of mammalian porin (VDAC) in the plasmalemma forming part of a chloride channel complex affected in cystic fibrosis and encephalomyopathy
    • Reymann, S., Flörke, H., Heiden, M., Jakob, C., Stadtmuller, U., Stinacker, P., Lalk, V. E., Pardowitz, L. & Thinnes, F. P. (1995) Further evidence for multitopological localization of mammalian porin (VDAC) in the plasmalemma forming part of a chloride channel complex affected in cystic fibrosis and encephalomyopathy, Biochem. Mol. Med. 54, 75-87.
    • (1995) Biochem. Mol. Med. , vol.54 , pp. 75-87
    • Reymann, S.1    Flörke, H.2    Heiden, M.3    Jakob, C.4    Stadtmuller, U.5    Stinacker, P.6    Lalk, V.E.7    Pardowitz, L.8    Thinnes, F.P.9
  • 11
    • 0023392255 scopus 로고
    • Molecular genetics of the VDAC ion channel: Structure model and sequence analysis
    • Forte, M., Guy, H. R. & Manella, C. A. (1987) Molecular genetics of the VDAC ion channel: Structure model and sequence analysis, J. Bioenerg. Biomembr. 19, 341-351.
    • (1987) J. Bioenerg. Biomembr. , vol.19 , pp. 341-351
    • Forte, M.1    Guy, H.R.2    Manella, C.A.3
  • 12
    • 0025055329 scopus 로고
    • The cationically selective state of the mitochondrial outer membrane pore: A study with intact mitochondrial porin
    • Benz, R., Kottke, M. & Brdiczka, D. (1990) The cationically selective state of the mitochondrial outer membrane pore: a study with intact 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
  • 13
    • 79959414421 scopus 로고
    • Anion channels in the mitochondrial outer membrane
    • Colombini, M. (1994) Anion channels in the mitochondrial outer membrane. Curr. Topics Memb. Trans. 42, 73-101.
    • (1994) Curr. Topics Memb. Trans. , vol.42 , pp. 73-101
    • Colombini, M.1
  • 14
    • 0024458675 scopus 로고
    • Voltage gating in the mitochondrial channel, VDAC
    • Colombini, M. (1989) Voltage gating in the mitochondrial channel, VDAC, J. Memb. Bimb. 111, 103-111.
    • (1989) J. Memb. Bimb. , vol.111 , pp. 103-111
    • Colombini, M.1
  • 15
    • 0026598425 scopus 로고
    • Determination of the number of polypeptide subunits in a functional VDAC channel from Saccharomyces cerevisiae
    • Penng, S., Blachly-Dyson, E., Colombini, M. & Forte, M. (1992) Determination of the number of polypeptide subunits in a functional VDAC channel from Saccharomyces cerevisiae, J. Bioenerg. Biomembr. 24, 27-32.
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 27-32
    • Penng, S.1    Blachly-Dyson, E.2    Colombini, M.3    Forte, M.4
  • 16
    • 0028348792 scopus 로고
    • Characterization and partial purification of the VDAC channel modulating protein from calf liver mitochondria
    • Liu, M. Y. & Colombini, M. (1994) Characterization and partial purification of the VDAC channel modulating protein from calf liver mitochondria, Biochim. Biophys. Acta 1185, 203-212.
    • (1994) Biochim. Biophys. Acta , vol.1185 , pp. 203-212
    • Liu, M.Y.1    Colombini, M.2
  • 17
    • 0000249418 scopus 로고
    • Dicyclohexylcarbodiimide as a probe for proton translocating enzymes
    • Solioz, M. (1984) Dicyclohexylcarbodiimide as a probe for proton translocating enzymes. Trends Biochem. Sci. 7, 309-314.
    • (1984) Trends Biochem. Sci. , vol.7 , pp. 309-314
    • Solioz, M.1
  • 18
    • 0027242022 scopus 로고
    • Location of the dicyclohexylcarbodiimide-reactive glutamate residue in the bovine heart mitochondrial porin
    • De Pinto, V. Aljamal, J. A. & Palmier, F. (1993) Location of the dicyclohexylcarbodiimide-reactive glutamate residue in the bovine heart mitochondrial porin, J. Biol. Chem. 268, 12 977-12 982.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12977-12982
    • De Pinto, V.1    Aljamal, J.A.2    Palmier, F.3
  • 19
    • 0021950768 scopus 로고
    • The 35 kDa DCCD-binding protein from pig heart mitochondria is the mitochondrial porin
    • De Pinto, V., Tommasino, M., Benz, R. & Palmieri, F. (1985) The 35 kDa DCCD-binding protein from pig heart mitochondria is the mitochondrial porin, Biochim. Biophys. Acta 813, 230-242.
    • (1985) Biochim. Biophys. Acta , vol.813 , pp. 230-242
    • De Pinto, V.1    Tommasino, M.2    Benz, R.3    Palmieri, F.4
  • 20
    • 0024463946 scopus 로고
    • Hexokinase-binding properties of the mitochondrial VDAC protein: Inhibition by DCCD and location of putative DCCD-binding sites
    • Nakashima, R. A. (1989) Hexokinase-binding properties of the mitochondrial VDAC protein: inhibition by DCCD and location of putative DCCD-binding sites, J. Bioenerg. Biomembr. 21, 461-469.
    • (1989) J. Bioenerg. Biomembr. , vol.21 , pp. 461-469
    • Nakashima, R.A.1
  • 21
    • 0022595453 scopus 로고
    • Hexokinase receptor complex in hepatoma mitochondria: Evidence from N,N′-dicyclohexylcarbodiimide-labeling studies for the involvement of the pore-forming protein VDAC
    • Nakashima, R. A., Mangan, P. S., Colombini, M. & Pedersen, P. L. (1986) Hexokinase receptor complex in hepatoma mitochondria: evidence from N,N′-dicyclohexylcarbodiimide-labeling studies for the involvement of the pore-forming protein VDAC, Biochemistry 25, 1015-1021.
    • (1986) Biochemistry , vol.25 , pp. 1015-1021
    • Nakashima, R.A.1    Mangan, P.S.2    Colombini, M.3    Pedersen, P.L.4
  • 22
    • 0014940130 scopus 로고
    • Purification and properties of an adenosine trisphosphate from sarcoplasmic reticulum
    • MacLennan, D. H. (1970) Purification and properties of an adenosine trisphosphate from sarcoplasmic reticulum, J. Biol. Chem. 247, 4508-4518.
    • (1970) J. Biol. Chem. , vol.247 , pp. 4508-4518
    • MacLennan, D.H.1
  • 25
    • 2442738537 scopus 로고
    • Determination of microgram quantities
    • Kaplan, R. S. & Pedersen, F. L. (1985) Determination of microgram quantities. Anal. Biochem. 150, 95-104.
    • (1985) Anal. Biochem. , vol.150 , pp. 95-104
    • Kaplan, R.S.1    Pedersen, F.L.2
  • 26
    • 0028958295 scopus 로고
    • Immunoelectron microscopic study of the distribution of porin of outer membranes of rat heart mitochondria
    • Konstantinova, S. A., Manella, V. P., Skulachev, V. P. & Zorov, D. B. (1995) Immunoelectron microscopic study of the distribution of porin of outer membranes of rat heart mitochondria, J. Bioenerg. Biomembr. 27, 93-99.
    • (1995) J. Bioenerg. Biomembr. , vol.27 , pp. 93-99
    • Konstantinova, S.A.1    Manella, V.P.2    Skulachev, V.P.3    Zorov, D.B.4
  • 28
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T. & Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc. Natl Acad. Sci. USA 76, 4350-4354.
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 29
    • 0028170670 scopus 로고
    • 2+ release channel of sarcoplasmic reticulum: Low affinity binding site as probed by Terbium fluorescence
    • 2+ release channel of sarcoplasmic reticulum: low affinity binding site as probed by Terbium fluorescence, J. Biol. Chem. 269, 24 864-24 869.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24864-24869
    • Hadad, N.1    Abramson, J.J.2    Zahle, T.3    Shoshan-Barmatz, V.4
  • 31
    • 0026297727 scopus 로고
    • Studies on human porin. VI. Production and characterization of eight monoclonal mouse antibodies against the human VDAC 'porin 31 HL' and their application for histotopological studies in human skeletal muscle
    • Babel, D., Walter, G., Gotz, H., Thinnes, F. P., Jurgens, L., Konig, U. & Hilschmann, N. (1991) Studies on human porin. VI. Production and characterization of eight monoclonal mouse antibodies against the human VDAC 'porin 31 HL' and their application for histotopological studies in human skeletal muscle. Biol. Chem. Hoppe-Seyler 372, 1027-1034.
    • (1991) Biol. Chem. Hoppe-Seyler , vol.372 , pp. 1027-1034
    • Babel, D.1    Walter, G.2    Gotz, H.3    Thinnes, F.P.4    Jurgens, L.5    Konig, U.6    Hilschmann, N.7
  • 32
    • 0018785338 scopus 로고
    • 2+ binding site in a Hydrophobic region
    • 2+ binding site in a Hydrophobic region, Biochemistry 18, 108-113.
    • (1979) Biochemistry , vol.18 , pp. 108-113
    • Pick, U.1    Racker, E.2
  • 33
    • 0024347661 scopus 로고
    • Interaction of non-classical detergents with the mitochondrial porin: A new purification procedure and characterization of the pore-forming unit
    • De Pinto, V., Benz, R. & Palmieri, F. (1989) Interaction of non-classical detergents with the mitochondrial porin: a new purification procedure and characterization of the pore-forming unit. Eur. J. Biochem. 183, 179-187.
    • (1989) Eur. J. Biochem. , vol.183 , pp. 179-187
    • De Pinto, V.1    Benz, R.2    Palmieri, F.3
  • 34
    • 0028938271 scopus 로고
    • Trace amounts of Triton X-100 modify the inhibitor sensitivity of the mitochondrial porin
    • Bathori, G., Fonyo, A. & Ligeti, H. (1995) Trace amounts of Triton X-100 modify the inhibitor sensitivity of the mitochondrial porin, Biochim. Biophys. Acta 1234, 249-254.
    • (1995) Biochim. Biophys. Acta , vol.1234 , pp. 249-254
    • Bathori, G.1    Fonyo, A.2    Ligeti, H.3
  • 36
    • 0027517017 scopus 로고
    • Effect of the local anesthetics on single channel behavior of skeletal muscle calcium channel
    • Xu, L., Jones, R. & Meissner, G. (1993)Effect of the local anesthetics on single channel behavior of skeletal muscle calcium channel, J. Gen. Physiol. 101, 207-233.
    • (1993) J. Gen. Physiol. , vol.101 , pp. 207-233
    • Xu, L.1    Jones, R.2    Meissner, G.3
  • 37
    • 0017726385 scopus 로고
    • Time- and voltage-dependent interaction of arrythmic drugs with cardiac sodium channel
    • Hondenghem, L. & Katzung, B. (1977) Time- and voltage-dependent interaction of arrythmic drugs with cardiac sodium channel, Biochim. Biophys. Acta 472, 373-398.
    • (1977) Biochim. Biophys. Acta , vol.472 , pp. 373-398
    • Hondenghem, L.1    Katzung, B.2
  • 38
    • 0017144669 scopus 로고
    • Voltage-dependent action of TTX in mammalian cardiac muscle
    • Baer, M., Best, M. & Reuter, H. (1476) Voltage-dependent action of TTX in mammalian cardiac muscle, Nature 263, 344-345.
    • (1476) Nature , vol.263 , pp. 344-345
    • Baer, M.1    Best, M.2    Reuter, H.3
  • 39
    • 0026517122 scopus 로고
    • Calcium channel characteristics conferred on the sodium channel by single mutations
    • Heinemann, S. H., Terlau, H., Stuhmer, W., Imoto, K. & Numa, S. (1992) Calcium channel characteristics conferred on the sodium channel by single mutations. Nature 356, 441-443.
    • (1992) Nature , vol.356 , pp. 441-443
    • Heinemann, S.H.1    Terlau, H.2    Stuhmer, W.3    Imoto, K.4    Numa, S.5
  • 40
    • 0030583220 scopus 로고    scopus 로고
    • The identification of the phosphorylated 150/160-kDa proteins of sarcoplasmic reticulum, their kinuse and their association with the ryanodine receptor
    • Shoshan-Barmatz, V., Orr, I., Weil, S., Meyer, H., Varsanyi, M. & Heilmeyer, L. M. G. (1996) The identification of the phosphorylated 150/160-kDa proteins of sarcoplasmic reticulum, their kinuse and their association with the ryanodine receptor, Biochim. Biophys. Acta. 1283, 89-100.
    • (1996) Biochim. Biophys. Acta , vol.1283 , pp. 89-100
    • Shoshan-Barmatz, V.1    Orr, I.2    Weil, S.3    Meyer, H.4    Varsanyi, M.5    Heilmeyer, L.M.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.