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Volumn 33, Issue 9, 2001, Pages 844-864

Macromolecular crowding and its role as intracellular signalling of cell volume regulation

Author keywords

Cell volume; Macromolecular crowding; Shrinkage dependent phosphorylation.; Swelling dependent dephosphorylation

Indexed keywords

CELL PROTEIN; ENZYME; ION;

EID: 0034927970     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1357-2725(01)00058-9     Document Type: Review
Times cited : (49)

References (191)
  • 1
    • 0025018285 scopus 로고
    • Holobiochemistry: The effect of local environment upon the equilibria and rates of biochemical reactions
    • (1990) Int. J. Biochem. , vol.22 , pp. 1063-1067
    • Minton, A.P.1
  • 4
    • 0020184671 scopus 로고
    • How crowded is the cytoplasm?
    • (1982) Cell , vol.30 , pp. 345-347
    • Fulton, A.B.1
  • 6
    • 0026730739 scopus 로고
    • Confinement as a determinant of macromolecular structure and reactivity
    • (1992) Biophys. J. , vol.63 , pp. 1090-1100
    • Minton, A.P.1
  • 8
    • 84985735713 scopus 로고
    • Excluded volume as a determinant of macromolecular structure and reactivity
    • (1981) Biopolymers , vol.20 , pp. 2093
    • Minton, A.P.1
  • 9
    • 0020668187 scopus 로고
    • The effect of volume occupancy upon the thermodynamic activity of proteins: Some biochemical consequences
    • (1983) Mol. Cell. Biochem. , vol.55 , pp. 119-140
    • Minton, A.P.1
  • 11
    • 84985721961 scopus 로고
    • Light scattering of bovine serum albumin solutions: Extension of the hard particle model to allow for electrostatic repulsion
    • (1982) Biopolymers , vol.21 , pp. 451-458
    • Minton, A.P.1    Edelhoch, H.2
  • 14
    • 0000314004 scopus 로고
    • A theory of partial osmotic pressures and membrane equilibria with special reference to the application of Dalton's law to haemoglobin solutions in the presence of salts
    • (1928) Proc. Roy. Soc. London Sct. A. , vol.120 , pp. 573-603
    • Adaire, G.S.1
  • 21
    • 0032311227 scopus 로고    scopus 로고
    • Molecular crowding: Analysis of effects of high concentrations of inert co-solutes on biochemical equilibria and rates in terms of volume exclusion
    • (1998) Methods Enzymol. , vol.295 , pp. 127-149
    • Minton, A.P.1
  • 24
    • 0028839750 scopus 로고
    • Condensation and cohesion of lambda DNA in cell extracts and other media: Implication for the structure and function of DNA in prokaryotes
    • (1995) Biophys. Chem. , vol.57 , pp. 71-92
    • Murphy, L.D.1    Zimmerman, S.B.2
  • 26
    • 0027496418 scopus 로고
    • Macromolecular crowding effects on macromolecular interactions: Some implications for genome structure and function
    • (1993) Biochim. Biophys. Acta. , vol.1216 , pp. 175-185
    • Zimmerman, S.B.1
  • 29
    • 0027235856 scopus 로고
    • Crowding-induced organisation of cytoskeletal elements: 1. Spontaneous demixing of cytosolic proteins and model filaments to form filament bundles
    • (1993) Biophys. J. , vol.65 , pp. 1147-1154
    • Madden, T.L.1    Herzfeld, J.2
  • 35
    • 0029887968 scopus 로고    scopus 로고
    • Substrate modulation of aldolase B binding in hepatocytes
    • (1996) Biochem. J. , vol.315 , pp. 651-658
    • Agius, L.1
  • 38
    • 0033587619 scopus 로고    scopus 로고
    • Direct observation of the self-association of dilute proteins in the presence of inert macromolecules at high concentration via tracer sedimentation equilibrium: Theory, experiment, and biological significance
    • (1999) Biochemistry , vol.38 , pp. 9379-9388
    • Rivas, G.1    Fernandez, J.A.2    Minton, A.P.3
  • 41
    • 0024316210 scopus 로고
    • Osmoelastic coupling in biological structures: Formation of parallel bundles of actin filaments in a crystalline-like structure caused by osmotic stress
    • (1989) Biochemistry , vol.28 , pp. 6513-6518
    • Suzuki, A.1    Yamazaki, M.2    Ito, T.3
  • 43
    • 0028787059 scopus 로고
    • Crowding-induced organization of cytoskeletal elements. III: Spontaneous bundling and sorting of self-assembled filaments with different flexibilities
    • (1995) Biophys. Chem. , vol.57 , pp. 93-102
    • Kulp, D.T.1    Herzfeld, J.2
  • 47
    • 0033039815 scopus 로고    scopus 로고
    • Folding and unfolding of a giant duplex-DNA in a mixed solution with polycations, polyanions and crowding neutral polymers
    • (1999) Biophys. Chem. , vol.76 , pp. 133-143
    • Kidoaki, S.1    Yoshikawa, K.2
  • 49
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • (1996) Nature , vol.38 , pp. 571-580
    • Hartl, F.U.1
  • 58
    • 0028321726 scopus 로고
    • Protein disulfide isomerase exhibits chaperone and anti-chaperone activity in the oxidative folding of lysozyme
    • (1994) J. Biol. Chem. , vol.269 , pp. 7764-7771
    • Puig, A.1    Gilbert, H.F.2
  • 64
    • 0034039755 scopus 로고    scopus 로고
    • Effect of a concentrated "inert" macromolecular co-solutes on the stability of a globular protein with respect to denaturation by heat and by chaotropes: A statistical-thermodynamic model
    • (2000) Biophys J. , vol.78 , pp. 101-109
    • Minton, A.P.1
  • 76
    • 0027175290 scopus 로고
    • Effect of sodium and betaine in cultured media on development and relative rates of protein synthesis in preimplantation mouse embryos in vitro
    • (1993) Mol. Reprod. Dev. , vol.35 , pp. 24-28
    • Anbari, K.1    Schultz, R.M.2
  • 91
    • 0026594194 scopus 로고
    • Regulation of glycogen synthesis and glycolysis by insulin, pH and cell volume. Interaction between swelling and alkalinization in mediating the effects of insulin
    • (1992) Biochem. J. , vol.282 , pp. 797-805
    • Peak, M.1    Al-Habori, M.2    Agius, L.3
  • 110
    • 0030048284 scopus 로고    scopus 로고
    • The role of cellular hydration in the regulation of cell function
    • (1996) Biochem. J. , vol.313 , pp. 697-710
    • Haussinger, D.1
  • 112
    • 0029938846 scopus 로고    scopus 로고
    • Protein kinase-signalling pathway triggered by cell swelling and involved in the activation of glycogen synthase and acetyl CoA carboxylase in isolated rat hepatocytes
    • (1996) J. Biol. Chem. , vol.271 , pp. 16668-16673
    • Krause, U.1    Rider, M.H.2    Hue, L.3
  • 113
    • 0025819501 scopus 로고
    • Function follows form: Generation of intracellular signals by cell deformation
    • (1991) FASEB J. , vol.5 , pp. 2013-2019
    • Watson, P.A.1
  • 115
    • 0031850240 scopus 로고    scopus 로고
    • The cytoskeleton and cell signalling: Component localization and mechanical coupling
    • (1998) Physiol. Rev. , vol.78 , pp. 763-781
    • Janmey, P.A.1
  • 118
    • 0026080491 scopus 로고
    • Okadaic acid inhibition of KCl cotransport. Evidence that protein dephosphorylation is necessary for activation of transport by either cell swelling or N-ethylmaleimide
    • (1991) J. Gen. Physiol. , vol.97 , pp. 799-817
    • Jennings, M.L.1    Schulz, R.K.2
  • 124
  • 132
    • 0027304320 scopus 로고
    • Urea alters set point volume for K-Cl cotransport, Na-H exchange, and Ca-Na exchange in dog red blood cells
    • (1993) Am. J. Physiol. , vol.256
    • Parker, J.C.1
  • 134
    • 0028964141 scopus 로고
    • Effects of urea on K-Cl co-transport in sheep red blood cells: Evidence for two signals of swelling
    • (1995) Am. J. Physiol. , vol.268
    • Dunham, P.B.1
  • 142
  • 143
    • 0025369920 scopus 로고
    • Kinetics of activation and inactivation of swelling-stimulated K/Cl transport. The volume-sensitive parameter is the rate constant for inactivation
    • (1990) J. Gen. Physiol. , vol.95 , pp. 1021-1040
    • Jennings, M.L.1    Al-Rohil, N.2
  • 157
    • 0027500729 scopus 로고
    • The role of ATP in swelling-stimulated K-Cl cotransport in human red cell ghosts. Phosphorylation-dephosphorylation events are not in the signal transduction pathway
    • (1993) J. Gen. Physiol. , vol.102 , pp. 551-573
    • Sachs, J.R.1    Martin, D.W.2
  • 166
    • 0026794359 scopus 로고
    • Activation of the Na-K-2Cl co-transporter in rat parotid acinar cells by aluminium fluoride and phosphatase inhibitors
    • (1992) J. Biol. Chem. , vol.267 , pp. 21558-21563
    • Paulais, M.1    Turner, R.J.2
  • 170
    • 0027688928 scopus 로고
    • The ATP and Mg dependence of Na-K-2Cl co-transport reflects a requirement for protein phosphorylation: Studies using calyculin A
    • (1993) Pfluegers Arch. , vol.425 , pp. 321-328
    • Palfrey, H.C.1    Pewitt, E.B.2
  • 172
    • 4243654223 scopus 로고
    • Myosin light chain phosphorylation in endothelial cells is regulated by cell volume and correlates with volume-regulatory Na-K-2Cl co-transport
    • (1992) J. Gen. Physiol. , vol.102
    • Klein, J.D.1    O'Neill, W.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.