메뉴 건너뛰기




Volumn 347, Issue 5, 2005, Pages 1015-1023

Molecular crowding limits the role of fetal hemoglobin in therapy for sickle cell disease

Author keywords

HbF; HbS; Hydroxyurea; Polymerization kinetics

Indexed keywords

HEMOGLOBIN F; HEMOGLOBIN S; HYDROXYUREA; POLYMER;

EID: 15244361470     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.02.006     Document Type: Article
Times cited : (26)

References (32)
  • 1
    • 0344653612 scopus 로고    scopus 로고
    • Responses of E. coli to osmotic stress: Large changes in amounts of cytoplasmic solutes and water
    • M.T. Record Jr, E.S. Courtenay, D.S. Cayley, and H.J. Guttman Responses of E. coli to osmotic stress: large changes in amounts of cytoplasmic solutes and water Trends Biochem. Sci. 23 1998 143 148
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 143-148
    • Record Jr., M.T.1    Courtenay, E.S.2    Cayley, D.S.3    Guttman, H.J.4
  • 2
    • 0020184671 scopus 로고
    • How crowded is the cytoplasm?
    • A.B. Fulton How crowded is the cytoplasm? Cell 30 1982 345 347
    • (1982) Cell , vol.30 , pp. 345-347
    • Fulton, A.B.1
  • 3
    • 4544329005 scopus 로고    scopus 로고
    • Crowding and the polymerization of sickle hemoglobin
    • F.A. Ferrone, and M.A. Rotter Crowding and the polymerization of sickle hemoglobin J. Mol. Recogn. 17 2004 497 504
    • (2004) J. Mol. Recogn. , vol.17 , pp. 497-504
    • Ferrone, F.A.1    Rotter, M.A.2
  • 4
    • 0017256029 scopus 로고
    • Non-ideality and the thermodynamics of sickle-cell hemoglobin gelation
    • A.P. Minton Non-ideality and the thermodynamics of sickle-cell hemoglobin gelation J. Mol. Biol. 100 1977 519 542
    • (1977) J. Mol. Biol. , vol.100 , pp. 519-542
    • Minton, A.P.1
  • 5
    • 0017667829 scopus 로고
    • Thermodynamics of gelation of sickle cell deoxyhemoglobin
    • P.D. Ross, J. Hofrichter, and W.A. Eaton Thermodynamics of gelation of sickle cell deoxyhemoglobin J. Mol. Biol. 115 1977 111 134
    • (1977) J. Mol. Biol. , vol.115 , pp. 111-134
    • Ross, P.D.1    Hofrichter, J.2    Eaton, W.A.3
  • 6
    • 0025276708 scopus 로고
    • Sickle Cell hemoglobin polymerization
    • W.A. Eaton, and J. Hofrichter Sickle Cell hemoglobin polymerization Adv. Protein Chem. 40 1990 63 280
    • (1990) Adv. Protein Chem. , vol.40 , pp. 63-280
    • Eaton, W.A.1    Hofrichter, J.2
  • 7
    • 0021837479 scopus 로고
    • Kinetics of sickle hemoglobin polymerization II: A double nucleation mechanism
    • F.A. Ferrone, J. Hofrichter, and W.A. Eaton Kinetics of sickle hemoglobin polymerization II: a double nucleation mechanism J. Mol. Biol. 183 1985 611 631
    • (1985) J. Mol. Biol. , vol.183 , pp. 611-631
    • Ferrone, F.A.1    Hofrichter, J.2    Eaton, W.A.3
  • 8
    • 0036220417 scopus 로고    scopus 로고
    • Heterogeneous nucleation and crowding in sickle hemoglobin: An analytic approach
    • F.A. Ferrone, M. Ivanova, and R. Jasuja Heterogeneous nucleation and crowding in sickle hemoglobin: an analytic approach Biophys. J. 82 2002 399 406
    • (2002) Biophys. J. , vol.82 , pp. 399-406
    • Ferrone, F.A.1    Ivanova, M.2    Jasuja, R.3
  • 9
    • 0033560094 scopus 로고    scopus 로고
    • Induction of fetal hemoglobin in sickle cell disease
    • H.F. Bunn Induction of fetal hemoglobin in sickle cell disease Blood 93 1999 1787 1789
    • (1999) Blood , vol.93 , pp. 1787-1789
    • Bunn, H.F.1
  • 10
    • 0035094512 scopus 로고    scopus 로고
    • Pharmacologic induction of fetal hemoglobin: Raising the therapeutic bar in sickle cell disease
    • G.F. Atweh, and A.N. Schechter Pharmacologic induction of fetal hemoglobin: raising the therapeutic bar in sickle cell disease Curr. Opin. Hematol. 8 2001 123 130
    • (2001) Curr. Opin. Hematol. , vol.8 , pp. 123-130
    • Atweh, G.F.1    Schechter, A.N.2
  • 12
    • 0018199125 scopus 로고
    • Requirements for therapeutic inhibition of sickle haemoglobin gelation
    • H.R. Sunshine, J. Hofrichter, and W.A. Eaton Requirements for therapeutic inhibition of sickle haemoglobin gelation Nature 275 1978 238 240
    • (1978) Nature , vol.275 , pp. 238-240
    • Sunshine, H.R.1    Hofrichter, J.2    Eaton, W.A.3
  • 14
    • 0037414164 scopus 로고    scopus 로고
    • Effect of hydroxyurea on mortality and morbidity in adult sickle cell anemia: Risks and benefits up to 9 years of treatment
    • M.H. Steinberg, F. Barton, O. Castro, C.H. Pegelow, S.K. Ballas, and A. Kutlar Effect of hydroxyurea on mortality and morbidity in adult sickle cell anemia: risks and benefits up to 9 years of treatment JAMA 289 2003 1645 1651
    • (2003) JAMA , vol.289 , pp. 1645-1651
    • Steinberg, M.H.1    Barton, F.2    Castro, O.3    Pegelow, C.H.4    Ballas, S.K.5    Kutlar, A.6
  • 15
    • 10544232620 scopus 로고    scopus 로고
    • A multiparameter analysis of sickle erythrocytes in patients undergoing hydroxyurea therapy
    • K.R. Bridges, G.D. Barabino, C. Brugnara, M.R. Cho, G.W. Christoph, and G. Dover A multiparameter analysis of sickle erythrocytes in patients undergoing hydroxyurea therapy Blood 88 1996 4701 4710
    • (1996) Blood , vol.88 , pp. 4701-4710
    • Bridges, K.R.1    Barabino, G.D.2    Brugnara, C.3    Cho, M.R.4    Christoph, G.W.5    Dover, G.6
  • 16
    • 0021527508 scopus 로고
    • Kinetics of nucleation controlled polymerization: A perturbation treatment for use with a secondary pathway
    • M.F. Bishop, and F.A. Ferrone Kinetics of nucleation controlled polymerization: a perturbation treatment for use with a secondary pathway Biophys. J. 46 1984 631 644
    • (1984) Biophys. J. , vol.46 , pp. 631-644
    • Bishop, M.F.1    Ferrone, F.A.2
  • 17
    • 0016369152 scopus 로고
    • Kinetics and mechanism of deoxyhemoglobin S gelation: A new approach to understanding sickle cell disease
    • J. Hofrichter, P.D. Ross, and W.A. Eaton Kinetics and mechanism of deoxyhemoglobin S gelation: a new approach to understanding sickle cell disease Proc. Natl Acad. Sci. USA 71 1974 4864 4868
    • (1974) Proc. Natl Acad. Sci. USA , vol.71 , pp. 4864-4868
    • Hofrichter, J.1    Ross, P.D.2    Eaton, W.A.3
  • 18
    • 0023195612 scopus 로고
    • Delay time of hemoglobin S polymeriztion prevents most cells from sickling
    • A. Mozzarelli, J. Hofrichter, and W.A. Eaton Delay time of hemoglobin S polymeriztion prevents most cells from sickling Science 237 1987 500 506
    • (1987) Science , vol.237 , pp. 500-506
    • Mozzarelli, A.1    Hofrichter, J.2    Eaton, W.A.3
  • 19
    • 0019987431 scopus 로고
    • Kinetics of sickle haemoglobin polymerization in single red cells
    • M. Coletta, J. Hofrichter, F.A. Ferrone, and W.A. Eaton Kinetics of sickle haemoglobin polymerization in single red cells Nature 300 1982 194 197
    • (1982) Nature , vol.300 , pp. 194-197
    • Coletta, M.1    Hofrichter, J.2    Ferrone, F.A.3    Eaton, W.A.4
  • 20
    • 0030893396 scopus 로고    scopus 로고
    • Fetal hemoglobin in sickle cell anemia: Determinants of response to hydroxyurea. Multicenter study of hydroxyurea
    • M.H. Steinberg, Z.H. Lu, F.B. Barton, M.L. Terrin, S. Charache, and G.J. Dover Fetal hemoglobin in sickle cell anemia: determinants of response to hydroxyurea. Multicenter study of hydroxyurea Blood 89 1997 1078 1088
    • (1997) Blood , vol.89 , pp. 1078-1088
    • Steinberg, M.H.1    Lu, Z.H.2    Barton, F.B.3    Terrin, M.L.4    Charache, S.5    Dover, G.J.6
  • 21
    • 0023275919 scopus 로고
    • Fetal hemoglobin-containing cells have the same mean corpuscular hemoglobin as cells without fetal hemoglobin: A reciprocal relationship between gamma- and beta-globin gene expression in normal subjects and in those with high fetal hemoglobin production
    • G.J. Dover, and S.H. Boyer Fetal hemoglobin-containing cells have the same mean corpuscular hemoglobin as cells without fetal hemoglobin: a reciprocal relationship between gamma- and beta-globin gene expression in normal subjects and in those with high fetal hemoglobin production Blood 69 1987 1109 1113
    • (1987) Blood , vol.69 , pp. 1109-1113
    • Dover, G.J.1    Boyer, S.H.2
  • 22
    • 0018565753 scopus 로고
    • Gelation of sickle cell hemoglobin in mixtures with normal adult and fetal hemoglobins
    • H.R. Sunshine, J. Hofrichter, and W.A. Eaton Gelation of sickle cell hemoglobin in mixtures with normal adult and fetal hemoglobins J. Mol. Biol. 133 1979 435 467
    • (1979) J. Mol. Biol. , vol.133 , pp. 435-467
    • Sunshine, H.R.1    Hofrichter, J.2    Eaton, W.A.3
  • 23
    • 0029008481 scopus 로고
    • The biophysics of sickle cell hydroxyurea therapy
    • W.A. Eaton, and J. Hofrichter The biophysics of sickle cell hydroxyurea therapy Science 268 1995 1142 1143
    • (1995) Science , vol.268 , pp. 1142-1143
    • Eaton, W.A.1    Hofrichter, J.2
  • 24
    • 0030464953 scopus 로고    scopus 로고
    • Hydroxyurea and sickle cell anemia. Clinical utility of a myelosuppressive "switching" agent. The multicenter study of hydroxyurea in sickle cell anemia
    • S. Charache, F.B. Barton, R.D. Moore, M.L. Terrin, M.H. Steinberg, and G.J. Dover Hydroxyurea and sickle cell anemia. Clinical utility of a myelosuppressive "switching" agent. The multicenter study of hydroxyurea in sickle cell anemia Medicine (Baltimore) 75 1996 300 326
    • (1996) Medicine (Baltimore) , vol.75 , pp. 300-326
    • Charache, S.1    Barton, F.B.2    Moore, R.D.3    Terrin, M.L.4    Steinberg, M.H.5    Dover, G.J.6
  • 26
    • 0031809842 scopus 로고    scopus 로고
    • Fetal hemoglobin and F-cell responses to long-term hydroxyurea treatment in young sickle cell patients. The French study group on sickle cell disease
    • M. Maier-Redelsperger, M. de Montalembert, A. Flahault, M.G. Neonato, R. Ducrocq, and M.P. Masson Fetal hemoglobin and F-cell responses to long-term hydroxyurea treatment in young sickle cell patients. The French study group on sickle cell disease Blood 91 1998 4472 4479
    • (1998) Blood , vol.91 , pp. 4472-4479
    • Maier-Redelsperger, M.1    De Montalembert, M.2    Flahault, A.3    Neonato, M.G.4    Ducrocq, R.5    Masson, M.P.6
  • 27
    • 0033559320 scopus 로고    scopus 로고
    • Sustained induction of fetal hemoglobin by pulse butyrate therapy in sickle cell disease
    • G.F. Atweh, M. Sutton, I. Nassif, V. Boosalis, G.J. Dover, and S. Wallenstein Sustained induction of fetal hemoglobin by pulse butyrate therapy in sickle cell disease Blood 93 1999 1790 1797
    • (1999) Blood , vol.93 , pp. 1790-1797
    • Atweh, G.F.1    Sutton, M.2    Nassif, I.3    Boosalis, V.4    Dover, G.J.5    Wallenstein, S.6
  • 28
    • 0021815445 scopus 로고
    • Kinetics of sickle hemoglobin polymerization I: Studies using temperature-jump and laser photolysis techniques
    • F.A. Ferrone, J. Hofrichter, and W.A. Eaton Kinetics of sickle hemoglobin polymerization I: studies using temperature-jump and laser photolysis techniques J. Mol. Biol. 183 1985 591 610
    • (1985) J. Mol. Biol. , vol.183 , pp. 591-610
    • Ferrone, F.A.1    Hofrichter, J.2    Eaton, W.A.3
  • 29
    • 0031026601 scopus 로고    scopus 로고
    • Homogeneous nucleation in sickle hemoglobin. Stochastic measurements with a parallel method
    • Z. Cao, and F.A. Ferrone Homogeneous nucleation in sickle hemoglobin. Stochastic measurements with a parallel method Biophys. J. 72 1997 343 372
    • (1997) Biophys. J. , vol.72 , pp. 343-372
    • Cao, Z.1    Ferrone, F.A.2
  • 30
    • 0025284406 scopus 로고
    • Nucleation and growth of fibres and gel formation in sickle cell haemoglobin
    • R.E. Samuel, E.D. Salmon, and R.W. Briehl Nucleation and growth of fibres and gel formation in sickle cell haemoglobin Nature 345 1990 833 835
    • (1990) Nature , vol.345 , pp. 833-835
    • Samuel, R.E.1    Salmon, E.D.2    Briehl, R.W.3
  • 32
    • 0010588495 scopus 로고
    • Hemoglobin and myoglobin ligand kinetics
    • L.J. Parkhurst Hemoglobin and myoglobin ligand kinetics Ann. Rev. Phys. Chem. 30 1979 503 546
    • (1979) Ann. Rev. Phys. Chem. , vol.30 , pp. 503-546
    • Parkhurst, L.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.