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Volumn 201, Issue 8, 1998, Pages 1118-1127

Intracellular oxygen diffusion: The roles of myoglobin and lipid at cold body temperature

Author keywords

Cold temperature; Fish muscle; Lipid content; Mitochondria; Myoglobin; Oxygen diffusion

Indexed keywords


EID: 0031810172     PISSN: 00220949     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (71)

References (46)
  • 1
    • 0030873307 scopus 로고    scopus 로고
    • Myoglobin enhances cardiac performance in Antarctic icefish species that express the protein
    • ACIERNO, R., AGNISOLA, C., TOTA, B. AND SIDELL, B. D. (1997). Myoglobin enhances cardiac performance in Antarctic icefish species that express the protein. Am. J. Physiol. 273, R100-R106.
    • (1997) Am. J. Physiol. , vol.273
    • Acierno, R.1    Agnisola, C.2    Tota, B.3    Sidell, B.D.4
  • 2
    • 0014366858 scopus 로고
    • The solubilities of seven gases in olive oil with reference to theories of transport through the cell membrane
    • BATTINO, R., EVANS, F. D. AND DANFORTH, W. F. (1968). The solubilities of seven gases in olive oil with reference to theories of transport through the cell membrane. J. Am. Oil Chem. Soc. 45, 830-833.
    • (1968) J. Am. Oil Chem. Soc. , vol.45 , pp. 830-833
    • Battino, R.1    Evans, F.D.2    Danforth, W.F.3
  • 3
    • 0030819158 scopus 로고    scopus 로고
    • Kinetic characterization of myoglobins from vertebrates with vastly different body temperatures
    • CASHON, R. E., VAYDA, M. E. AND SIDELL, B. D. (1997). Kinetic characterization of myoglobins from vertebrates with vastly different body temperatures. Comp. Biochem. Physiol. 117B, 613-620.
    • (1997) Comp. Biochem. Physiol. , vol.117 B , pp. 613-620
    • Cashon, R.E.1    Vayda, M.E.2    Sidell, B.D.3
  • 4
    • 0029794340 scopus 로고    scopus 로고
    • High lipid content enhances the rate of oxygen diffusion through fish skeletal muscle
    • DESAULNIERS, N., MOERLAND, T. S. AND SIDELL, B. D. (1996). High lipid content enhances the rate of oxygen diffusion through fish skeletal muscle. Am. J. Physiol. 271, R42-R47.
    • (1996) Am. J. Physiol. , vol.271
    • Desaulniers, N.1    Moerland, T.S.2    Sidell, B.D.3
  • 5
    • 0028793905 scopus 로고
    • A theoretical analysis of intracellular oxygen diffusion
    • DUTTA, A. AND POPEL, A. S. (1995). A theoretical analysis of intracellular oxygen diffusion. J. theor. Biol. 176, 433-445.
    • (1995) J. Theor. Biol. , vol.176 , pp. 433-445
    • Dutta, A.1    Popel, A.S.2
  • 6
    • 0000079203 scopus 로고
    • Effects of acclimation temperature on routine metabolism, muscle mitochondrial volume density and capillary supply in the elver (Anguilla anguilla L.)
    • EGGINTON, S. AND JOHNSTON, I. A. (1984). Effects of acclimation temperature on routine metabolism, muscle mitochondrial volume density and capillary supply in the elver (Anguilla anguilla L.). J. therm. Biol. 9, 165-170.
    • (1984) J. Therm. Biol. , vol.9 , pp. 165-170
    • Egginton, S.1    Johnston, I.A.2
  • 7
    • 0024557971 scopus 로고
    • Thermal acclimation induces adaptive changes in subcellular structure of fish skeletal muscle
    • EGGINTON, S. AND SIDELL, B. D. (1989). Thermal acclimation induces adaptive changes in subcellular structure of fish skeletal muscle. Am. J. Physiol. 256, R1-R9.
    • (1989) Am. J. Physiol. , vol.256
    • Egginton, S.1    Sidell, B.D.2
  • 8
    • 0021381912 scopus 로고
    • Heterogeneity of oxygen diffusion through hamster striated muscles
    • ELLSWORTH, M. AND PITTMAN, R. N. (1984). Heterogeneity of oxygen diffusion through hamster striated muscles. Am. J. Physiol. 246, H161-H167.
    • (1984) Am. J. Physiol. , vol.246
    • Ellsworth, M.1    Pittman, R.N.2
  • 9
    • 0021228406 scopus 로고
    • Skeletal muscle capillary supply in a fish that lacks respiratory pigments
    • FITCH, N. A., JOHNSTON, I. A. AND WOOD, R. E. (1984). Skeletal muscle capillary supply in a fish that lacks respiratory pigments. Respir. Physiol. 57, 201-211.
    • (1984) Respir. Physiol. , vol.57 , pp. 201-211
    • Fitch, N.A.1    Johnston, I.A.2    Wood, R.E.3
  • 10
    • 0000728710 scopus 로고
    • The cytoplasmic matrix: Its volume and surface area and the diffusion of molecules through it
    • GERSHON, N. D., PORTER, K. R. AND TRUS, B. L. (1985). The cytoplasmic matrix: Its volume and surface area and the diffusion of molecules through it. Proc. natn. Acad. Sci. U.S.A. 82, 5030-5034.
    • (1985) Proc. Natn. Acad. Sci. U.S.A. , vol.82 , pp. 5030-5034
    • Gershon, N.D.1    Porter, K.R.2    Trus, B.L.3
  • 11
    • 0028916402 scopus 로고
    • Thermal adaptation in biological membranes: Is homeoviscous adaptation the explanation?
    • HAZEL, J. R. (1995). Thermal adaptation in biological membranes: Is homeoviscous adaptation the explanation? A. Rev. Physiol. 57, 19-42.
    • (1995) A. Rev. Physiol. , vol.57 , pp. 19-42
    • Hazel, J.R.1
  • 12
    • 0016189989 scopus 로고
    • Molecular mechanisms of temperature compensation in poikilotherms
    • HAZEL, J. R. AND PROSSER, C. L. (1974). Molecular mechanisms of temperature compensation in poikilotherms. A. Rev. Physiol. 54, 620-677.
    • (1974) A. Rev. Physiol. , vol.54 , pp. 620-677
    • Hazel, J.R.1    Prosser, C.L.2
  • 13
    • 0002046798 scopus 로고
    • Respiratory and cardiovascular adaptations in hemoglobin-free fish: Resolved and unresolved problems
    • ed. G. di Prisco, B. Maresca and B. Tota, Berlin: Springer-Verlag
    • HEMMINGSEN, E. A. (1991). Respiratory and cardiovascular adaptations in hemoglobin-free fish: Resolved and unresolved problems. In Biology of Antarctic Fish (ed. G. di Prisco, B. Maresca and B. Tota), pp. 191-203. Berlin: Springer-Verlag.
    • (1991) Biology of Antarctic Fish , pp. 191-203
    • Hemmingsen, E.A.1
  • 14
    • 0002542607 scopus 로고
    • Osteology and relationships of the family Channichthyidae
    • IWAMI, T. (1985). Osteology and relationships of the family Channichthyidae. Mem. natn. Inst. polar Res. Tokyo Ser. E 36, 1-69.
    • (1985) Mem. Natn. Inst. Polar Res. Tokyo Ser. E , vol.36 , pp. 1-69
    • Iwami, T.1
  • 15
    • 0002682893 scopus 로고
    • Structure and function of fish muscles
    • JOHNSTON, I. A. (1981). Structure and function of fish muscles. Symp. Zool. Soc. Lond. 48, 71-13.
    • (1981) Symp. Zool. Soc. Lond. , vol.48 , pp. 71-113
    • Johnston, I.A.1
  • 16
    • 84985129992 scopus 로고
    • Temperature acclimation in crucian carp, Carassius carassius L., morphometric analyses of muscle fibre ultrastructure
    • JOHNSTON, I. A. AND MAITLAND, B. (1980). Temperature acclimation in crucian carp, Carassius carassius L., morphometric analyses of muscle fibre ultrastructure. J. Fish Biol. 17, 113-125.
    • (1980) J. Fish Biol. , vol.17 , pp. 113-125
    • Johnston, I.A.1    Maitland, B.2
  • 17
    • 0016840831 scopus 로고
    • Determination of diffusivity of oxygen and carbon dioxide in respiring tissue: Results in rat skeletal muscle
    • KAWASHIRO, T., NUSSE, W. AND SHEID, P. (1975). Determination of diffusivity of oxygen and carbon dioxide in respiring tissue: results in rat skeletal muscle. Pflügers Arch. 359, 231-239.
    • (1975) Pflügers Arch. , vol.359 , pp. 231-239
    • Kawashiro, T.1    Nusse, W.2    Sheid, P.3
  • 18
    • 84944482637 scopus 로고
    • The rate of diffusion of gases through animal tissues with some remarks about the coefficient of invasion
    • KROGH, A. (1919). The rate of diffusion of gases through animal tissues with some remarks about the coefficient of invasion. J. Physiol., Lond. 52, 391-122.
    • (1919) J. Physiol., Lond. , vol.52 , pp. 391-1122
    • Krogh, A.1
  • 19
    • 0028240683 scopus 로고
    • Anatomy and dynamics of a ligand-binding pathway in myoglobin: The roles of residues 45, 60, 64 and 68
    • LAMBRIGHT, D. G., BALASUBRAMANIAN, S., DECATUR, S. M. AND BOXER, S. G. (1994). Anatomy and dynamics of a ligand-binding pathway in myoglobin: The roles of residues 45, 60, 64 and 68. Biochemistry 33, 5518-5525.
    • (1994) Biochemistry , vol.33 , pp. 5518-5525
    • Lambright, D.G.1    Balasubramanian, S.2    Decatur, S.M.3    Boxer, S.G.4
  • 20
    • 0025279577 scopus 로고
    • Ultrastructure of aerobic muscle in Antarctic fishes may contribute to maintenance of diffusive fluxes
    • LONDRAVILLE, R. L. AND SIDELL, B. D. (1990a). Ultrastructure of aerobic muscle in Antarctic fishes may contribute to maintenance of diffusive fluxes. J. exp. Biol. 150, 205-220.
    • (1990) J. Exp. Biol. , vol.150 , pp. 205-220
    • Londraville, R.L.1    Sidell, B.D.2
  • 21
    • 0024988769 scopus 로고
    • Maximal diffusion-distance within skeletal muscle can be estimated from mitochondrial distributions
    • LONDRAVILLE, R. L. AND SIDELL, B. D. (1990b). Maximal diffusion-distance within skeletal muscle can be estimated from mitochondrial distributions. Respir. Physiol. 81, 291-302.
    • (1990) Respir. Physiol. , vol.81 , pp. 291-302
    • Londraville, R.L.1    Sidell, B.D.2
  • 22
    • 0002616311 scopus 로고
    • Channels of oxygen transport from blood to mitochondria
    • LONGMUIR, I. S. (1980). Channels of oxygen transport from blood to mitochondria. Adv. physiol. Sci. 25, 19-22.
    • (1980) Adv. Physiol. Sci. , vol.25 , pp. 19-22
    • Longmuir, I.S.1
  • 23
    • 0018191870 scopus 로고
    • Diffusion and consumption of oxygen in the resting frog sartorius muscle
    • MAHLER, M. (1978). Diffusion and consumption of oxygen in the resting frog sartorius muscle. J. gen. Physiol. 71, 533-557.
    • (1978) J. Gen. Physiol. , vol.71 , pp. 533-557
    • Mahler, M.1
  • 24
    • 0021802414 scopus 로고
    • Reappraisal of diffusion, solubility and consumption of oxygen in frog skeletal muscle, with applications to muscle energy balance
    • MAHLER, M., LOUY, C., HOMSHER, E. AND PESKOFF, A. (1985). Reappraisal of diffusion, solubility and consumption of oxygen in frog skeletal muscle, with applications to muscle energy balance. J. gen. Physiol. 86, 105-134.
    • (1985) J. Gen. Physiol. , vol.86 , pp. 105-134
    • Mahler, M.1    Louy, C.2    Homsher, E.3    Peskoff, A.4
  • 25
    • 77049129026 scopus 로고
    • Passage of molecules through capillary walls
    • PAPPENHEIMER, J. R. (1953). Passage of molecules through capillary walls. Physiol. Rev. 33, 383-423.
    • (1953) Physiol. Rev. , vol.33 , pp. 383-423
    • Pappenheimer, J.R.1
  • 26
    • 0019209443 scopus 로고
    • Structure and refinement of oxymyoglobin at 1.6 Å resolution
    • PHILLIPS, S. E. V. (1980). Structure and refinement of oxymyoglobin at 1.6 Å resolution. J. molec. Biol. 142, 531-554.
    • (1980) J. Molec. Biol. , vol.142 , pp. 531-554
    • Phillips, S.E.V.1
  • 28
    • 0025000048 scopus 로고
    • Thermodynamic study of protein dynamic structure in the oxygen binding reaction of myoglobin
    • SATO, F., SHIRO, Y., SKAGUCHI, Y., IIZUKA, T. AND HAYASHI, H. (1990). Thermodynamic study of protein dynamic structure in the oxygen binding reaction of myoglobin. J. biol. Chem. 265, 18823-18828.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18823-18828
    • Sato, F.1    Shiro, Y.2    Skaguchi, Y.3    Iizuka, T.4    Hayashi, H.5
  • 29
    • 0023159910 scopus 로고
    • Temperature affects the diffusion of small molecules through cytosol of fish muscle
    • SIDELL, B. D. AND HAZEL, J. R. (1987). Temperature affects the diffusion of small molecules through cytosol of fish muscle. J. exp. Biol. 129, 191-203.
    • (1987) J. Exp. Biol. , vol.129 , pp. 191-203
    • Sidell, B.D.1    Hazel, J.R.2
  • 30
    • 0343839939 scopus 로고    scopus 로고
    • Physiological and evolutionary aspects of myoglobin expression in the hemoglobinless antarctic icefishes
    • ed. H. O. Pörtner and R. Playle. London: Cambridge University Press (in press)
    • SIDELL, B. D. AND VAYDA, M. E. (1997). Physiological and evolutionary aspects of myoglobin expression in the hemoglobinless antarctic icefishes. In Cold Ocean Physiology (ed. H. O. Pörtner and R. Playle). London: Cambridge University Press (in press).
    • (1997) Cold Ocean Physiology
    • Sidell, B.D.1    Vayda, M.E.2
  • 32
    • 2642697417 scopus 로고    scopus 로고
    • The myoglobin gene of Antarctic teleosts contains three A+T-rich introns
    • in press
    • SMALL, D. J., VAYDA, M. E. AND SIDELL, B. D. (1998). The myoglobin gene of Antarctic teleosts contains three A+T-rich introns. J. molec. Evol. (in press).
    • (1998) J. Molec. Evol.
    • Small, D.J.1    Vayda, M.E.2    Sidell, B.D.3
  • 33
    • 0025958683 scopus 로고
    • Dioxygen solubility in aqueous phosphatidylcholine dispersions
    • SMOTKIN, E. S., MOY, T. AND PLACHY, W. (1991). Dioxygen solubility in aqueous phosphatidylcholine dispersions. Biochim. biophys. Acta 1061, 33-38.
    • (1991) Biochim. Biophys. Acta , vol.1061 , pp. 33-38
    • Smotkin, E.S.1    Moy, T.2    Plachy, W.3
  • 34
    • 0028949615 scopus 로고
    • Proteins and temperature
    • SOMERO, G. N. (1995). Proteins and temperature. A. Rev. Physiol. 57, 43-68.
    • (1995) A. Rev. Physiol. , vol.57 , pp. 43-68
    • Somero, G.N.1
  • 35
    • 2642693282 scopus 로고
    • The effect of temperature on facilitated oxygen diffusion and its relation to warm tuna muscle
    • STEVENS, E. D. (1982). The effect of temperature on facilitated oxygen diffusion and its relation to warm tuna muscle. Can. J. Zool. 60, 1148-1152.
    • (1982) Can. J. Zool. , vol.60 , pp. 1148-1152
    • Stevens, E.D.1
  • 36
    • 0019546624 scopus 로고
    • One why of the warmth of warm-bodied fish
    • STEVENS, E. D. AND CAREY, F. G. (1981). One why of the warmth of warm-bodied fish. Am. J. Physiol. 240, R151-R155.
    • (1981) Am. J. Physiol. , vol.240
    • Stevens, E.D.1    Carey, F.G.2
  • 37
    • 0025945387 scopus 로고
    • Effect of alkyl chain unsaturation and cholesterol intercalation on oxygen transport in membranes: A pulse-ESR spin labeling study
    • SUBCZYNSKI, W. I., HYDE, J. S. AND KUSUMI, A. (1991). Effect of alkyl chain unsaturation and cholesterol intercalation on oxygen transport in membranes: a pulse-ESR spin labeling study. Biochemistry 30, 8578-8590.
    • (1991) Biochemistry , vol.30 , pp. 8578-8590
    • Subczynski, W.I.1    Hyde, J.S.2    Kusumi, A.3
  • 38
    • 0001253053 scopus 로고
    • Oxygen permeability of phosphatidylcholine-cholesterol membranes
    • SUBCZYNSKI, W. K., HYDE, J. S. AND KUSUMI, A. (1989). Oxygen permeability of phosphatidylcholine-cholesterol membranes. Proc. natn. Acad. Sci. U.S.A. 86, 4474-4478.
    • (1989) Proc. Natn. Acad. Sci. U.S.A. , vol.86 , pp. 4474-4478
    • Subczynski, W.K.1    Hyde, J.S.2    Kusumi, A.3
  • 39
    • 0017364269 scopus 로고
    • Structure of myoglobin refined at 2.0 Å resolution. I. Crystallographic refinement of metmyoglobin from sperm whale
    • TAKANO, T. (1977). Structure of myoglobin refined at 2.0 Å resolution. I. Crystallographic refinement of metmyoglobin from sperm whale. J. molec. Biol. 110, 537-568.
    • (1977) J. Molec. Biol. , vol.110 , pp. 537-568
    • Takano, T.1
  • 40
    • 0002728509 scopus 로고
    • Changes in mitochondrial distribution and diffusion distances in muscle of goldfish upon acclimation to warm and cold temperatures
    • TYLER, S. AND SIDELL, B. D. (1984). Changes in mitochondrial distribution and diffusion distances in muscle of goldfish upon acclimation to warm and cold temperatures. J. Exp. Zool. 232, 1-9.
    • (1984) J. Exp. Zool. , vol.232 , pp. 1-9
    • Tyler, S.1    Sidell, B.D.2
  • 43
    • 0019324356 scopus 로고
    • The diffusion-solubility of oxygen in lipid bilayers
    • WINDREM, D. A. AND PLACHY, W. Z. (1980). The diffusion-solubility of oxygen in lipid bilayers. Biochim. Biophys. Acta 600, 655-665.
    • (1980) Biochim. Biophys. Acta , vol.600 , pp. 655-665
    • Windrem, D.A.1    Plachy, W.Z.2
  • 45
    • 0014858661 scopus 로고
    • Myoglobin facilitated oxygen diffusion: Role of myoglobin in oxygen entry into muscle
    • WITTENBERG, J. B. (1970). Myoglobin facilitated oxygen diffusion: Role of myoglobin in oxygen entry into muscle. Physiol. Rev. 50, 559-636.
    • (1970) Physiol. Rev. , vol.50 , pp. 559-636
    • Wittenberg, J.B.1


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