메뉴 건너뛰기




Volumn 1784, Issue 10, 2008, Pages 1454-1461

Polymeric nanoparticles for hemoglobin-based oxygen carriers

Author keywords

Bioerodible polymeric nanoparticle; Blood substitute; Hemoglobin based oxygen carrier

Indexed keywords

BLOOD SUBSTITUTE; COPOLYMER; HEMOGLOBIN BASED OXYGEN CARRIER; LIPOSOME; METHEMOGLOBIN; NANOPARTICLE; POLY(MALEIC ANHYDRIDE CO BUTYLVINYL ETHER); POLYMER; RECOMBINANT HEMOGLOBIN; UNCLASSIFIED DRUG;

EID: 52049092981     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.03.013     Document Type: Review
Times cited : (51)

References (111)
  • 2
    • 45849100301 scopus 로고    scopus 로고
    • Blood conservation - How practical?
    • Rao S.M. Blood conservation - How practical?. Indian J. Anaesth. 46 (2002) 168-174
    • (2002) Indian J. Anaesth. , vol.46 , pp. 168-174
    • Rao, S.M.1
  • 3
    • 34249995380 scopus 로고    scopus 로고
    • Alternatives to allogeneic blood transfusions
    • Pape A. Alternatives to allogeneic blood transfusions. Best Pract. Res. Clin. Anaesthesiol. 21 (2007) 221-239
    • (2007) Best Pract. Res. Clin. Anaesthesiol. , vol.21 , pp. 221-239
    • Pape, A.1
  • 5
    • 0033984989 scopus 로고    scopus 로고
    • Synthesis and physicochemical characterization of a series of hemoglobin-based oxygen carriers: objective comparison between cellular and acellular types
    • Sakai H., Yuasa M., Onuma H., Takeoka S., and Tsuchida E. Synthesis and physicochemical characterization of a series of hemoglobin-based oxygen carriers: objective comparison between cellular and acellular types. Bioconjug. Chem. 11 (2000) 56-64
    • (2000) Bioconjug. Chem. , vol.11 , pp. 56-64
    • Sakai, H.1    Yuasa, M.2    Onuma, H.3    Takeoka, S.4    Tsuchida, E.5
  • 6
    • 34248206717 scopus 로고    scopus 로고
    • Oxygen therapeutics pursuit of an alternative to the donor red blood cell
    • Ness P.M., and Cushing M.M. Oxygen therapeutics pursuit of an alternative to the donor red blood cell. Arch. Pathol. Lab. Med. 131 (2007) 734-741
    • (2007) Arch. Pathol. Lab. Med. , vol.131 , pp. 734-741
    • Ness, P.M.1    Cushing, M.M.2
  • 7
    • 3042637754 scopus 로고    scopus 로고
    • Large volume polymerized haemoglobin solution in a Jehovah's Witness following abruptio placenta
    • Cothren C.C., Moore E.E., Long J.S., Haenel J.B., Johnson J.L., and Ciesla D.J. Large volume polymerized haemoglobin solution in a Jehovah's Witness following abruptio placenta. Tranfus. Med. 14 (2004) 241-246
    • (2004) Tranfus. Med. , vol.14 , pp. 241-246
    • Cothren, C.C.1    Moore, E.E.2    Long, J.S.3    Haenel, J.B.4    Johnson, J.L.5    Ciesla, D.J.6
  • 8
    • 36148991843 scopus 로고    scopus 로고
    • Laboratory-Clinica Interface: oxygen carriers and cancer chemo- and radiotherapy sensitization: bench to bedside and back
    • Yu M., Dai M., Liu Q., and Xiu R. Laboratory-Clinica Interface: oxygen carriers and cancer chemo- and radiotherapy sensitization: bench to bedside and back. Cancer Treat. Rev. 33 (2007) 757-761
    • (2007) Cancer Treat. Rev. , vol.33 , pp. 757-761
    • Yu, M.1    Dai, M.2    Liu, Q.3    Xiu, R.4
  • 9
    • 1242353138 scopus 로고    scopus 로고
    • Oxygen therapeutics: can we tame hemoglobin?
    • Alayash A.I. Oxygen therapeutics: can we tame hemoglobin?. Nature 3 (2004) 152-159
    • (2004) Nature , vol.3 , pp. 152-159
    • Alayash, A.I.1
  • 10
    • 0019459839 scopus 로고
    • Embryonic hemoglobins in man and other mammals
    • Fantoni A., Farace M.G., and Gambari R. Embryonic hemoglobins in man and other mammals. Blood 57 (1981) 623-633
    • (1981) Blood , vol.57 , pp. 623-633
    • Fantoni, A.1    Farace, M.G.2    Gambari, R.3
  • 11
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: a plausible model
    • Monod J., Wyman J., and Changeux J.P. On the nature of allosteric transitions: a plausible model. J. Mol. Biol. 12 (1965) 88-118
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 12
    • 1842483305 scopus 로고    scopus 로고
    • The structure-function relationship of hemoglobin in solution at atomic resolution
    • Lukin J.A., and Ho C. The structure-function relationship of hemoglobin in solution at atomic resolution. Chem. Rev. 104 (2004) 1219-1230
    • (2004) Chem. Rev. , vol.104 , pp. 1219-1230
    • Lukin, J.A.1    Ho, C.2
  • 13
    • 0003043542 scopus 로고
    • The possible effects of the aggregation of the molecules of haemoglobin on its oxygen dissociation curve
    • Hill A.V. The possible effects of the aggregation of the molecules of haemoglobin on its oxygen dissociation curve. J. Physiol. (Lond.) 40 (1910) IV-VII
    • (1910) J. Physiol. (Lond.) , vol.40
    • Hill, A.V.1
  • 14
    • 0142088892 scopus 로고    scopus 로고
    • Human haemoglobin. A new paradigm for oxygen binding involving two types of ab contacts
    • Shikama K., and Matsuoka A. Human haemoglobin. A new paradigm for oxygen binding involving two types of ab contacts. Eur. J. Biochem. 270 (2003) 4041-4051
    • (2003) Eur. J. Biochem. , vol.270 , pp. 4041-4051
    • Shikama, K.1    Matsuoka, A.2
  • 16
    • 0033054997 scopus 로고    scopus 로고
    • Red blood cell substitutes: fluorocarbon emulsions and hemoglobin solutions
    • Remy B., Deby-Dupont G., and Lamy M. Red blood cell substitutes: fluorocarbon emulsions and hemoglobin solutions. British Med. Bull. 55 (1999) 277-298
    • (1999) British Med. Bull. , vol.55 , pp. 277-298
    • Remy, B.1    Deby-Dupont, G.2    Lamy, M.3
  • 17
    • 0034529592 scopus 로고    scopus 로고
    • Blood substitutes: refocusing an elusive goal
    • Winslow R.M. Blood substitutes: refocusing an elusive goal. Br. J. Hematol. 111 (2000) 387-396
    • (2000) Br. J. Hematol. , vol.111 , pp. 387-396
    • Winslow, R.M.1
  • 18
    • 52049121344 scopus 로고    scopus 로고
    • R.M. Winslow, Methods and compositions for optimization of oxygen transport by cell-free systems. US Patent 6, 054,427: The Regents of the University of California, (2000).
    • R.M. Winslow, Methods and compositions for optimization of oxygen transport by cell-free systems. US Patent 6, 054,427: The Regents of the University of California, (2000).
  • 19
    • 14644410424 scopus 로고    scopus 로고
    • Targeted O2 delivery by low-p50 hemoglobin: a new basis for hemoglobin-based oxygen carriers
    • Winslow R.M. Targeted O2 delivery by low-p50 hemoglobin: a new basis for hemoglobin-based oxygen carriers. Artif. Cells Blood Substit. Immobil. Biotechnol. 33 (2005) 1-12
    • (2005) Artif. Cells Blood Substit. Immobil. Biotechnol. , vol.33 , pp. 1-12
    • Winslow, R.M.1
  • 20
    • 0036839090 scopus 로고    scopus 로고
    • Hemoglobin-based oxygen carriers
    • Stowell C.P. Hemoglobin-based oxygen carriers. Curr. Opin. Hematol. 9 (2002) 537-543
    • (2002) Curr. Opin. Hematol. , vol.9 , pp. 537-543
    • Stowell, C.P.1
  • 21
    • 4344592781 scopus 로고    scopus 로고
    • Hemoglobin-based red blood cell substitutes
    • Chang T.M.S. Hemoglobin-based red blood cell substitutes. Artif. Org. 28 (2004) 789-794
    • (2004) Artif. Org. , vol.28 , pp. 789-794
    • Chang, T.M.S.1
  • 22
    • 0014026391 scopus 로고
    • Survival of mammals breathing organic liquids equilibrated with oxygen at atmospheric pressure
    • Clark Jr. L.C., and Gollan F. Survival of mammals breathing organic liquids equilibrated with oxygen at atmospheric pressure. Science 152 (1966) 1755
    • (1966) Science , vol.152 , pp. 1755
    • Clark Jr., L.C.1    Gollan, F.2
  • 23
    • 0035465476 scopus 로고    scopus 로고
    • Oxygen carriers ('blood substitutes') Raion d'etre, chemistry, and some physiology
    • Riess J.G. Oxygen carriers ('blood substitutes') Raion d'etre, chemistry, and some physiology. Chem. Rev. 101 (2001) 2797-2894
    • (2001) Chem. Rev. , vol.101 , pp. 2797-2894
    • Riess, J.G.1
  • 24
    • 0023024415 scopus 로고
    • Isolation and characterization of a new hemoglobin derivative cross-linked between the alfa chains (lysine 99 alfa 1-lysine 99 alfa 2)
    • Chatterjee R., Welty E.V., Walder R.Y., Pruitt S.L., Rogers S.L., Arnone A., and Walder J.A. Isolation and characterization of a new hemoglobin derivative cross-linked between the alfa chains (lysine 99 alfa 1-lysine 99 alfa 2). J. Biol.Chem. 261 (1986) 9929-9937
    • (1986) J. Biol.Chem. , vol.261 , pp. 9929-9937
    • Chatterjee, R.1    Welty, E.V.2    Walder, R.Y.3    Pruitt, S.L.4    Rogers, S.L.5    Arnone, A.6    Walder, J.A.7
  • 26
    • 0029990895 scopus 로고    scopus 로고
    • Effect of a hemoglobin-based oxygen carrier (HBOC-201) on hemodynamics and oxygen transport in patients undergoing preoperative hemodilution for elective abdominal aortic surgery
    • Kasper S.M., Walter M., Grune F., Bischoff A., Erasmi H., and Buzello W. Effect of a hemoglobin-based oxygen carrier (HBOC-201) on hemodynamics and oxygen transport in patients undergoing preoperative hemodilution for elective abdominal aortic surgery. Cardiovasc. Anesth. 83 (1996) 921-927
    • (1996) Cardiovasc. Anesth. , vol.83 , pp. 921-927
    • Kasper, S.M.1    Walter, M.2    Grune, F.3    Bischoff, A.4    Erasmi, H.5    Buzello, W.6
  • 27
    • 0031858604 scopus 로고    scopus 로고
    • The first randomized trial of human polymerized hemoglobin as a blood substitute in acute trauma and emergency surgery
    • Gould S.A., Moore E.E., Hoyt D.B., Burch J.M., Haenel J.B., Garcia J., DeWoskin R., and Moss G.S. The first randomized trial of human polymerized hemoglobin as a blood substitute in acute trauma and emergency surgery. J. Am. Coll. Surg. 187 (1998) 113-122
    • (1998) J. Am. Coll. Surg. , vol.187 , pp. 113-122
    • Gould, S.A.1    Moore, E.E.2    Hoyt, D.B.3    Burch, J.M.4    Haenel, J.B.5    Garcia, J.6    DeWoskin, R.7    Moss, G.S.8
  • 31
    • 0019986743 scopus 로고
    • Micro-encapsulation IV: cross-linked hemoglobin microcapsules
    • Lévy M.C., Rambourg P., Lévy J., and Potron G. Micro-encapsulation IV: cross-linked hemoglobin microcapsules. J. Pharm. Sci. 71 (1982) 759-762
    • (1982) J. Pharm. Sci. , vol.71 , pp. 759-762
    • Lévy, M.C.1    Rambourg, P.2    Lévy, J.3    Potron, G.4
  • 32
    • 0026535070 scopus 로고
    • Protein solvation in allosteric regulation: a water effect
    • Colombo M.F., Rau D.C., and Parsegian A.A. Protein solvation in allosteric regulation: a water effect. Science 256 (1992) 655-659
    • (1992) Science , vol.256 , pp. 655-659
    • Colombo, M.F.1    Rau, D.C.2    Parsegian, A.A.3
  • 33
    • 0037062603 scopus 로고    scopus 로고
    • Site-specific crosslinking of human and bovine hemoglobins differentially alters oxygen binding and redox side reaction producing rhombic heme and heme degradation
    • Nagababu E., Somasundaran R., Rifkind J.M., Jia Y., and Alayash A.I. Site-specific crosslinking of human and bovine hemoglobins differentially alters oxygen binding and redox side reaction producing rhombic heme and heme degradation. Biochemistry 41 (2002) 7407-7415
    • (2002) Biochemistry , vol.41 , pp. 7407-7415
    • Nagababu, E.1    Somasundaran, R.2    Rifkind, J.M.3    Jia, Y.4    Alayash, A.I.5
  • 34
    • 0025883342 scopus 로고
    • Nitric oxide: physiology, pathophysiology, and pharmacology
    • Moncada S., Palmer R.M.J., and Higgs E.A. Nitric oxide: physiology, pathophysiology, and pharmacology. Pharmacol. Rev. 43 (1991) 109-131
    • (1991) Pharmacol. Rev. , vol.43 , pp. 109-131
    • Moncada, S.1    Palmer, R.M.J.2    Higgs, E.A.3
  • 38
    • 33846969212 scopus 로고    scopus 로고
    • Influence of intramolecular cross-links on the molecular, structural and functional properties of PEGylated haemoglobin
    • Hu T., Manjula B.N., Li D., Brenowitz M., and Acharya S.A. Influence of intramolecular cross-links on the molecular, structural and functional properties of PEGylated haemoglobin. Biochem. J. 402 (2007) 143-151
    • (2007) Biochem. J. , vol.402 , pp. 143-151
    • Hu, T.1    Manjula, B.N.2    Li, D.3    Brenowitz, M.4    Acharya, S.A.5
  • 41
    • 33750889018 scopus 로고    scopus 로고
    • Plasma viscosity regulates capillary perfusion during extreme hemodilution in hamster skinfold model
    • Tsai A.G., Friesenecker B., and McCarthy M. Plasma viscosity regulates capillary perfusion during extreme hemodilution in hamster skinfold model. Am. J. Physiol. 275 (1998) H2170-H2180
    • (1998) Am. J. Physiol. , vol.275
    • Tsai, A.G.1    Friesenecker, B.2    McCarthy, M.3
  • 42
    • 33749234394 scopus 로고    scopus 로고
    • Extension arm facilitated PEGylation of hemoglobin: correlation of the properties with the extent of PEGylation
    • Li D., Manjula B.N., and Acharya A.S. Extension arm facilitated PEGylation of hemoglobin: correlation of the properties with the extent of PEGylation. Protein J. 25 4 (2006)
    • (2006) Protein J. , vol.25 , Issue.4
    • Li, D.1    Manjula, B.N.2    Acharya, A.S.3
  • 44
    • 0035975686 scopus 로고    scopus 로고
    • The role of facilitated diffusion in oxygen transport by cell-free hemoglobins: implications for the design of hemoglobin-based oxygen carrier
    • McCarthy M.R., Vandegriff K.D., and Winslow R.M. The role of facilitated diffusion in oxygen transport by cell-free hemoglobins: implications for the design of hemoglobin-based oxygen carrier. Biophys. Chem. 92 (2001) 103-117
    • (2001) Biophys. Chem. , vol.92 , pp. 103-117
    • McCarthy, M.R.1    Vandegriff, K.D.2    Winslow, R.M.3
  • 46
    • 0035284411 scopus 로고    scopus 로고
    • Peptide and protein pegylation: a review of problems and solution
    • Veronese F.M. Peptide and protein pegylation: a review of problems and solution. Biomaterials 22 (2001) 405-417
    • (2001) Biomaterials , vol.22 , pp. 405-417
    • Veronese, F.M.1
  • 48
    • 29644434820 scopus 로고    scopus 로고
    • Influence of conjugation of poly(ethylene glycol) to Hb on the oxygen-binding and solution properties of the peg-hb conjugate
    • Hu T., Prabhakaran M., Acharya S.A., and Manjula B.N. Influence of conjugation of poly(ethylene glycol) to Hb on the oxygen-binding and solution properties of the peg-hb conjugate. Biochem. J. 392 (2005) 555-564
    • (2005) Biochem. J. , vol.392 , pp. 555-564
    • Hu, T.1    Prabhakaran, M.2    Acharya, S.A.3    Manjula, B.N.4
  • 50
    • 0037343959 scopus 로고    scopus 로고
    • Site-specific PEGylation of hemoglobin at Cys-93(β): correlation between the colligative properties of the PEGylated protein and the length of the conjugated PEG chain
    • Manjula B.N., Tsai A., Upadhya R., Perumalsamy K., Smith P.K., Malavallil A., Vandergriff K., and Winslow R.M. Site-specific PEGylation of hemoglobin at Cys-93(β): correlation between the colligative properties of the PEGylated protein and the length of the conjugated PEG chain. Bioconjug. Chem. 14 (2003) 464-472
    • (2003) Bioconjug. Chem. , vol.14 , pp. 464-472
    • Manjula, B.N.1    Tsai, A.2    Upadhya, R.3    Perumalsamy, K.4    Smith, P.K.5    Malavallil, A.6    Vandergriff, K.7    Winslow, R.M.8
  • 54
    • 0033036813 scopus 로고    scopus 로고
    • Polyethylene glyco-modified liposome-encapsulated hemoglobin: a long circulating red cell substitute
    • Philips W.T., Klpper R.W., and Awasthi V.D. Polyethylene glyco-modified liposome-encapsulated hemoglobin: a long circulating red cell substitute. J. Pharm. Exp. Therapeutics 288 (1999) 665-670
    • (1999) J. Pharm. Exp. Therapeutics , vol.288 , pp. 665-670
    • Philips, W.T.1    Klpper, R.W.2    Awasthi, V.D.3
  • 56
    • 0347413685 scopus 로고    scopus 로고
    • Determination of size distribution and encapsulation efficiency of liposome-encapsulated hemoglobin blood substitutes using asymmetric flow field-flow fractionation coupled with multi-angle static light scattering
    • Arifin D.R., and Palmer A.F. Determination of size distribution and encapsulation efficiency of liposome-encapsulated hemoglobin blood substitutes using asymmetric flow field-flow fractionation coupled with multi-angle static light scattering. Biotechnol. Prog. 19 (2003) 1798-1811
    • (2003) Biotechnol. Prog. , vol.19 , pp. 1798-1811
    • Arifin, D.R.1    Palmer, A.F.2
  • 57
    • 0842289676 scopus 로고    scopus 로고
    • Microencapsulation of bovine hemoglobin with high bio-activity and high entrapment efficiency using a W/O/W double emulsion technique
    • Meng F.T., Ma G.H., Liu Y.D., Qiu W., and Su Z.G. Microencapsulation of bovine hemoglobin with high bio-activity and high entrapment efficiency using a W/O/W double emulsion technique. Colloids surf., B Biointerfaces 33 (2004) 177-183
    • (2004) Colloids surf., B Biointerfaces , vol.33 , pp. 177-183
    • Meng, F.T.1    Ma, G.H.2    Liu, Y.D.3    Qiu, W.4    Su, Z.G.5
  • 58
    • 22944465780 scopus 로고    scopus 로고
    • Polymersome encapsulated hemoglobin: a novel type of oxygen carrier
    • Arifin D.R., and Palmer A.F. Polymersome encapsulated hemoglobin: a novel type of oxygen carrier. Biomacromolecules 6 (2005) 2172-2181
    • (2005) Biomacromolecules , vol.6 , pp. 2172-2181
    • Arifin, D.R.1    Palmer, A.F.2
  • 59
    • 0033079841 scopus 로고    scopus 로고
    • Future prospects for artificial blood
    • Chang T.M.S. Future prospects for artificial blood. Trends Biotechnol. 17 (1999) 61-67
    • (1999) Trends Biotechnol. , vol.17 , pp. 61-67
    • Chang, T.M.S.1
  • 61
    • 0034205025 scopus 로고    scopus 로고
    • Evaluation of human hemoglobin vesicle as an oxygen carrier: recovery from hemorrhagic shock in rabbits
    • Ogata Y. Evaluation of human hemoglobin vesicle as an oxygen carrier: recovery from hemorrhagic shock in rabbits. Polym. Adv. Technol. 11 (2000) 301-306
    • (2000) Polym. Adv. Technol. , vol.11 , pp. 301-306
    • Ogata, Y.1
  • 62
    • 4544360318 scopus 로고    scopus 로고
    • Hemorrhagic shock resuscitation with an artificial oxygen carrier, hemoglobin vesicle, maintains intestinal perfusion and suppresses the increase in plasma tumor necrosis factor-α
    • Yoshizu A., Izumi Y., Park S., Sakai H., Takeoka S., Horinouchi H., Ikeda E., Tsuchida E., and Kobayashi K. Hemorrhagic shock resuscitation with an artificial oxygen carrier, hemoglobin vesicle, maintains intestinal perfusion and suppresses the increase in plasma tumor necrosis factor-α. ASAIO J. 50 (2004) 458-463
    • (2004) ASAIO J. , vol.50 , pp. 458-463
    • Yoshizu, A.1    Izumi, Y.2    Park, S.3    Sakai, H.4    Takeoka, S.5    Horinouchi, H.6    Ikeda, E.7    Tsuchida, E.8    Kobayashi, K.9
  • 63
    • 17044387058 scopus 로고    scopus 로고
    • New generation of hemoglobin-based oxygen carriers evaluated for oxygenation of critically ischemic hamster flap tissue
    • Contaldo C., Plock J., Sakai H., Takeoka S., Tsuchida E., Leunig M., Banic A., and Erni D. New generation of hemoglobin-based oxygen carriers evaluated for oxygenation of critically ischemic hamster flap tissue. Crit. Care Med. 33 (2005) 806-812
    • (2005) Crit. Care Med. , vol.33 , pp. 806-812
    • Contaldo, C.1    Plock, J.2    Sakai, H.3    Takeoka, S.4    Tsuchida, E.5    Leunig, M.6    Banic, A.7    Erni, D.8
  • 64
    • 1642346631 scopus 로고    scopus 로고
    • Neutral and anionic liposome-encapsulated hemoglobin: effect of postinserted poly(ethylene glycol)-distearoylphosphatidylethanolamine on distribution and circulation kinetics
    • Awasthi V.D., Garcia D., Klipper R., Goins B.A., and Phillips W.T. Neutral and anionic liposome-encapsulated hemoglobin: effect of postinserted poly(ethylene glycol)-distearoylphosphatidylethanolamine on distribution and circulation kinetics. J. Pharmacol. Exp. Ther. 309 (2004) 241-248
    • (2004) J. Pharmacol. Exp. Ther. , vol.309 , pp. 241-248
    • Awasthi, V.D.1    Garcia, D.2    Klipper, R.3    Goins, B.A.4    Phillips, W.T.5
  • 65
    • 4444315484 scopus 로고    scopus 로고
    • Kinetics of liposome-encapsulated hemoglobin after 25% hypovolemic exchange transfusion
    • Awasthi V.D., Garcia D., Klipper R., Phillips W.T., and Goins B.A. Kinetics of liposome-encapsulated hemoglobin after 25% hypovolemic exchange transfusion. Int. J. Pharmaceutics 283 (2004) 53-62
    • (2004) Int. J. Pharmaceutics , vol.283 , pp. 53-62
    • Awasthi, V.D.1    Garcia, D.2    Klipper, R.3    Phillips, W.T.4    Goins, B.A.5
  • 66
    • 1642408475 scopus 로고    scopus 로고
    • Metabolism of hemoglobin-vesicles (artificial oxygen carriers) and their influence on organ functions in a rat model
    • Sakai H., Horinouchi H., Masada Y., Takeoka S., Ikeda E., Takaori M., Kobayashi K., and Tsuchida E. Metabolism of hemoglobin-vesicles (artificial oxygen carriers) and their influence on organ functions in a rat model. Biomaterials 25 (2004) 4317-4325
    • (2004) Biomaterials , vol.25 , pp. 4317-4325
    • Sakai, H.1    Horinouchi, H.2    Masada, Y.3    Takeoka, S.4    Ikeda, E.5    Takaori, M.6    Kobayashi, K.7    Tsuchida, E.8
  • 68
    • 0021259483 scopus 로고
    • Oxidative interaction between haemoglobin and membrane lipid. A liposome Model
    • Szebeni J., Winterbourn C.C., and Carrell R.W. Oxidative interaction between haemoglobin and membrane lipid. A liposome Model. Biochem. J. 220 (1984) 685-692
    • (1984) Biochem. J. , vol.220 , pp. 685-692
    • Szebeni, J.1    Winterbourn, C.C.2    Carrell, R.W.3
  • 69
    • 0021873081 scopus 로고
    • Encapsulation of hemoglobin in phospholipid liposomes: characterization and stability
    • Szebeni J., Di Iorio E.E., Hauser H., and Winterhalter K.H. Encapsulation of hemoglobin in phospholipid liposomes: characterization and stability. Biochemistry 24 (1985) 2827-2832
    • (1985) Biochemistry , vol.24 , pp. 2827-2832
    • Szebeni, J.1    Di Iorio, E.E.2    Hauser, H.3    Winterhalter, K.H.4
  • 70
    • 0034090354 scopus 로고    scopus 로고
    • Poly(ethylene glycol)-conjugation and deoxygenation enable long-term preservation of hemoglobin-vesicles as oxygen carriers in a liquid state
    • Sakai H., Tomiyama K., Sou K., Takeoka S., and Tsuchida E. Poly(ethylene glycol)-conjugation and deoxygenation enable long-term preservation of hemoglobin-vesicles as oxygen carriers in a liquid state. Bioconjug. Chem. 11 (2000) 425-432
    • (2000) Bioconjug. Chem. , vol.11 , pp. 425-432
    • Sakai, H.1    Tomiyama, K.2    Sou, K.3    Takeoka, S.4    Tsuchida, E.5
  • 71
    • 4844221727 scopus 로고    scopus 로고
    • Toxicities of hemoglobin solutions: in search of in vitro and in-vivo model systems
    • Buehler P.W., and Alayash A.I. Toxicities of hemoglobin solutions: in search of in vitro and in-vivo model systems. Transfusion 44 (2004) 1516-1530
    • (2004) Transfusion , vol.44 , pp. 1516-1530
    • Buehler, P.W.1    Alayash, A.I.2
  • 72
    • 0042281579 scopus 로고    scopus 로고
    • Vesicles and liposomes: a self-assembly principle beyond lipids
    • Antonietti M., and Förster S. Vesicles and liposomes: a self-assembly principle beyond lipids. Adv. Mater. 15 (2003) 1323-1333
    • (2003) Adv. Mater. , vol.15 , pp. 1323-1333
    • Antonietti, M.1    Förster, S.2
  • 73
    • 0141927263 scopus 로고    scopus 로고
    • Stealth liposomes and long circulating nanoparticles: critical issues in pharmacokinetics, opsonization and protein-binding properties
    • Moghimi S.M., and Szebeni J. Stealth liposomes and long circulating nanoparticles: critical issues in pharmacokinetics, opsonization and protein-binding properties. Prog. Lipid Res. 42 (2003) 463-478
    • (2003) Prog. Lipid Res. , vol.42 , pp. 463-478
    • Moghimi, S.M.1    Szebeni, J.2
  • 75
    • 36949017465 scopus 로고    scopus 로고
    • Haemoglobin-vesicles as artificial oxygen carriers: present situation and future visions
    • Sakai H., Sou K., Horinouchi H., Kobayashi K., and Tsuchida E. Haemoglobin-vesicles as artificial oxygen carriers: present situation and future visions. J. Intern. Med. 263 (2008) 4-15
    • (2008) J. Intern. Med. , vol.263 , pp. 4-15
    • Sakai, H.1    Sou, K.2    Horinouchi, H.3    Kobayashi, K.4    Tsuchida, E.5
  • 76
    • 1142297583 scopus 로고    scopus 로고
    • Heparin coated poly(alkylcyanoacrylate) nanoparticles coupled to hemoglobin: a new oxygen carrier
    • Chauvierre C., Marden M.C., Vauthier C., Labarre D., Couvreur P., and Leclerc L. Heparin coated poly(alkylcyanoacrylate) nanoparticles coupled to hemoglobin: a new oxygen carrier. Biomaterials 25 (2004) 3081-3086
    • (2004) Biomaterials , vol.25 , pp. 3081-3086
    • Chauvierre, C.1    Marden, M.C.2    Vauthier, C.3    Labarre, D.4    Couvreur, P.5    Leclerc, L.6
  • 77
    • 33845616309 scopus 로고    scopus 로고
    • Preparation of hemoglobin-loaded nano-sized particles with porous structure as oxygen carriers
    • Zhao J., Liua C., Yuan Y., Tao X., Shan X., Sheng Y., and Wu F. Preparation of hemoglobin-loaded nano-sized particles with porous structure as oxygen carriers. Biomaterials 28 (2007) 1414-1422
    • (2007) Biomaterials , vol.28 , pp. 1414-1422
    • Zhao, J.1    Liua, C.2    Yuan, Y.3    Tao, X.4    Shan, X.5    Sheng, Y.6    Wu, F.7
  • 78
    • 0029991651 scopus 로고    scopus 로고
    • Submicron polymer membrane hemoglobin nanocapsules as potential blood substitutes: preparation and characterization
    • Yu W.P., and Chang T.M. Submicron polymer membrane hemoglobin nanocapsules as potential blood substitutes: preparation and characterization. Artif. Cells Blood Substit. Immobil. Biotechnol. 24 (1996) 169-183
    • (1996) Artif. Cells Blood Substit. Immobil. Biotechnol. , vol.24 , pp. 169-183
    • Yu, W.P.1    Chang, T.M.2
  • 79
    • 1242319583 scopus 로고    scopus 로고
    • A new red blood cell substitute
    • Chang T.M.S. A new red blood cell substitute. Crit. Care Med. 32 (2004) 612-613
    • (2004) Crit. Care Med. , vol.32 , pp. 612-613
    • Chang, T.M.S.1
  • 80
    • 22944461112 scopus 로고    scopus 로고
    • Engineering temperature-sensitive hydrogel nanoparticles entrapping hemoglobin as a novel type of oxygen carrier
    • Patton J.N., and Palmer A.F. Engineering temperature-sensitive hydrogel nanoparticles entrapping hemoglobin as a novel type of oxygen carrier. Biomacromolecules 6 (2005) 2204-2212
    • (2005) Biomacromolecules , vol.6 , pp. 2204-2212
    • Patton, J.N.1    Palmer, A.F.2
  • 81
    • 2442667452 scopus 로고    scopus 로고
    • Hemolysate-filled polyethyleneimine and polyurea microcapsules as potential red blood cell substitutes: effect of aqueous monomer type on properties of the prepared microcapsules
    • El-Gibaly I., and Anwar M. Hemolysate-filled polyethyleneimine and polyurea microcapsules as potential red blood cell substitutes: effect of aqueous monomer type on properties of the prepared microcapsules. Int. J. Pharm. 27 (2004) 25-40
    • (2004) Int. J. Pharm. , vol.27 , pp. 25-40
    • El-Gibaly, I.1    Anwar, M.2
  • 82
    • 33644899373 scopus 로고    scopus 로고
    • Physical properties of hemoglobin-poly(acrylamide) hydrogel-based oxygen carriers: effect of reaction pH
    • Patton J.N., and Palmer A.F. Physical properties of hemoglobin-poly(acrylamide) hydrogel-based oxygen carriers: effect of reaction pH. Langmuir 22 (2006) 2212-2221
    • (2006) Langmuir , vol.22 , pp. 2212-2221
    • Patton, J.N.1    Palmer, A.F.2
  • 85
    • 0022504872 scopus 로고
    • Lipid-peroxidation in hemoglobin-containing liposomes - effects of membrane phospholipid-composition and cholesterol content
    • Szebeni J., and Toth K. Lipid-peroxidation in hemoglobin-containing liposomes - effects of membrane phospholipid-composition and cholesterol content. Biochim. Biophys. Acta 857 (1986) 139-145
    • (1986) Biochim. Biophys. Acta , vol.857 , pp. 139-145
    • Szebeni, J.1    Toth, K.2
  • 86
    • 0018651542 scopus 로고
    • Properties of cytochrome b5 and methemoglobin reduction in human erythrocytes
    • Abe K., and Sugita Y. Properties of cytochrome b5 and methemoglobin reduction in human erythrocytes. Eur. J. Biochem. 101 (1979) 423-428
    • (1979) Eur. J. Biochem. , vol.101 , pp. 423-428
    • Abe, K.1    Sugita, Y.2
  • 87
    • 0027762222 scopus 로고
    • Purification of concentrated hemoglobin using organic solvent and heat treatment protein
    • Sakai H., Takeoka S., Seino Y., Nishide H., and Tuschida E. Purification of concentrated hemoglobin using organic solvent and heat treatment protein. Expr. Purif. 4 (1993) 563-569
    • (1993) Expr. Purif. , vol.4 , pp. 563-569
    • Sakai, H.1    Takeoka, S.2    Seino, Y.3    Nishide, H.4    Tuschida, E.5
  • 88
    • 0023775078 scopus 로고
    • Hemoglobin Corpuscles. Report of a research project for Honours Physiology, Medical Library, McGill University, 1957. Also reprinted as part of "30th anniversary in Artificial Red Blood Cells Research"
    • Chang T.M.S. Hemoglobin Corpuscles. Report of a research project for Honours Physiology, Medical Library, McGill University, 1957. Also reprinted as part of "30th anniversary in Artificial Red Blood Cells Research". Biomater. Artif. Cells 16 (1988) 1-9
    • (1988) Biomater. Artif. Cells , vol.16 , pp. 1-9
    • Chang, T.M.S.1
  • 89
    • 0342980853 scopus 로고    scopus 로고
    • Two future generations of blood substitutes based on polyhemoglobin-SOD-catalase and nanoencapsulation
    • Chang T.M.S., D'Agnillo F., Yu W.P., and Razack S. Two future generations of blood substitutes based on polyhemoglobin-SOD-catalase and nanoencapsulation. Adv. drug deliv. rev. 40 (2000) 213-218
    • (2000) Adv. drug deliv. rev. , vol.40 , pp. 213-218
    • Chang, T.M.S.1    D'Agnillo, F.2    Yu, W.P.3    Razack, S.4
  • 90
    • 52049087658 scopus 로고    scopus 로고
    • T.M.S. Chang, D. Powanda, W.P. Yu, Biodegradable polymeric nanocapsules and uses thereof (2002) PCT/CA2002/001331-WO/2003/017987 (2003).
    • T.M.S. Chang, D. Powanda, W.P. Yu, Biodegradable polymeric nanocapsules and uses thereof (2002) PCT/CA2002/001331-WO/2003/017987 (2003).
  • 91
    • 0344494642 scopus 로고    scopus 로고
    • Prolonged oxygen-carrying ability of hemoglobin vesicles by coencapsulation of catalane in vivo
    • Teramura Y., Kanazawa H., Sakai H., Takeoka S., and Tsuchida E. Prolonged oxygen-carrying ability of hemoglobin vesicles by coencapsulation of catalane in vivo. Bioconjug. Chem. 14 (2003) 1171-1176
    • (2003) Bioconjug. Chem. , vol.14 , pp. 1171-1176
    • Teramura, Y.1    Kanazawa, H.2    Sakai, H.3    Takeoka, S.4    Tsuchida, E.5
  • 92
    • 0028303693 scopus 로고
    • Suppression of methemoglobin formation by glutathione in a concetrated hemoglobin solution and in a hemoglobin-vesicle
    • Sakai H., Takeoka S., Seino Y., and Tsuchida E. Suppression of methemoglobin formation by glutathione in a concetrated hemoglobin solution and in a hemoglobin-vesicle. Bull. Chem. Soc. Jpn. 67 (1994) 1120-1125
    • (1994) Bull. Chem. Soc. Jpn. , vol.67 , pp. 1120-1125
    • Sakai, H.1    Takeoka, S.2    Seino, Y.3    Tsuchida, E.4
  • 94
    • 14044255326 scopus 로고    scopus 로고
    • Photopolymerization of bovine hemoglobin entrapped nanoscale hydrogel particles within liposomal reactors for use as an artificial blood substitute
    • Patton J.N., and F Palmer A. Photopolymerization of bovine hemoglobin entrapped nanoscale hydrogel particles within liposomal reactors for use as an artificial blood substitute. Biomacromolecules 6 (2005) 414-424
    • (2005) Biomacromolecules , vol.6 , pp. 414-424
    • Patton, J.N.1    F Palmer, A.2
  • 95
    • 33749021377 scopus 로고    scopus 로고
    • Hemoglobin vesicles containing methemoglobin and l-tyrosine to suppress methemoglobin formation in vitro and in vivo
    • Atoji T., Aihara M., Sakai H., Tsuchida E., and Takeoka S. Hemoglobin vesicles containing methemoglobin and l-tyrosine to suppress methemoglobin formation in vitro and in vivo. Bioconjug. Chem. 17 (2006) 1241-1245
    • (2006) Bioconjug. Chem. , vol.17 , pp. 1241-1245
    • Atoji, T.1    Aihara, M.2    Sakai, H.3    Tsuchida, E.4    Takeoka, S.5
  • 99
    • 33750065411 scopus 로고    scopus 로고
    • Bioerodible polymeric nanoparticles for targeted delivery of proteic drugs
    • Chiellini E.E., Chiellini F., and Solaro R. Bioerodible polymeric nanoparticles for targeted delivery of proteic drugs. J. Nanosci. Nanotechnol. 6 (2006) 3040-3047
    • (2006) J. Nanosci. Nanotechnol. , vol.6 , pp. 3040-3047
    • Chiellini, E.E.1    Chiellini, F.2    Solaro, R.3
  • 100
    • 84986637916 scopus 로고
    • Dissolution of alkyl vinyl ether-maleic anhydride copolymers and ester derivatives
    • Woodruff C.W., Peck G.E., and Banker G.S. Dissolution of alkyl vinyl ether-maleic anhydride copolymers and ester derivatives. J. Pharm. Sci. 61 (1972) 1912-1916
    • (1972) J. Pharm. Sci. , vol.61 , pp. 1912-1916
    • Woodruff, C.W.1    Peck, G.E.2    Banker, G.S.3
  • 103
    • 43049175550 scopus 로고    scopus 로고
    • F. Chiellini, A.M. Piras, M. Gazzarri, C. Bartoli, M. Ferri, L. Paolini. Bioactive polymeric materials for targeted administration of active agents - synthesis and evaluation. Macromol. Biosci. (in press), doi:10.1002/mabi.200700228.
    • F. Chiellini, A.M. Piras, M. Gazzarri, C. Bartoli, M. Ferri, L. Paolini. Bioactive polymeric materials for targeted administration of active agents - synthesis and evaluation. Macromol. Biosci. (in press), doi:10.1002/mabi.200700228.
  • 104
    • 52049121690 scopus 로고    scopus 로고
    • J. Cowdall, J. Davies, M. Roberts, A Carlsson, R. Solaro, G. Mazzanti, E.E. Chiellini, E. Söderlind, Microparticles based on hybrid polymeric materials for controlled release of biologically active molecules, a process for preparing the same and their uses for in vivo and in vitro therapy, prophylaxis and diagnostics (1998) PCT/1998/000191 - EP 1 001 744 B1 (2005).
    • J. Cowdall, J. Davies, M. Roberts, A Carlsson, R. Solaro, G. Mazzanti, E.E. Chiellini, E. Söderlind, Microparticles based on hybrid polymeric materials for controlled release of biologically active molecules, a process for preparing the same and their uses for in vivo and in vitro therapy, prophylaxis and diagnostics (1998) PCT/1998/000191 - EP 1 001 744 B1 (2005).
  • 105
    • 52049125797 scopus 로고    scopus 로고
    • J. Cowdall, J. Davies, M. Roberts, A Carlsson, R. Solaro, G. Mazzanti, E.E. Chiellini, F. Chiellini, E. Söderlind, Microparticles for controlled delivery of biologically active molecules (1998) PCT/IT1998/000192 - EP 1 003 482 B1 (2005).
    • J. Cowdall, J. Davies, M. Roberts, A Carlsson, R. Solaro, G. Mazzanti, E.E. Chiellini, F. Chiellini, E. Söderlind, Microparticles for controlled delivery of biologically active molecules (1998) PCT/IT1998/000192 - EP 1 003 482 B1 (2005).
  • 106
    • 0035730395 scopus 로고    scopus 로고
    • Targeted administration of proteic drugs. I. Preparation of polymeric nanoparticles
    • Chiellini E., Chiellini E.E., Chiellini F., and Solaro R. Targeted administration of proteic drugs. I. Preparation of polymeric nanoparticles. J. Bioact. Compat. Polym. 16 (2001) 441-465
    • (2001) J. Bioact. Compat. Polym. , vol.16 , pp. 441-465
    • Chiellini, E.1    Chiellini, E.E.2    Chiellini, F.3    Solaro, R.4
  • 108
    • 43049161349 scopus 로고    scopus 로고
    • A new biocompatible nanoparticle delivery system for the release of fibrinolytic drugs
    • Piras A.M., Chiellini F., Fiumi C., Bartoli C., and Chiellini E. A new biocompatible nanoparticle delivery system for the release of fibrinolytic drugs. Int. J. Pharm. 357 (2008) 260-271
    • (2008) Int. J. Pharm. , vol.357 , pp. 260-271
    • Piras, A.M.1    Chiellini, F.2    Fiumi, C.3    Bartoli, C.4    Chiellini, E.5
  • 110
    • 0002238956 scopus 로고
    • Cyclodextrins in pharmaceuticals
    • Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Szejtli J. Cyclodextrins in pharmaceuticals. Cyclodextrin Technology (1988), Kluwer Academic Publishers, Dordrecht, The Netherlands 186-306
    • (1988) Cyclodextrin Technology , pp. 186-306
    • Szejtli, J.1
  • 111
    • 15944398355 scopus 로고    scopus 로고
    • The clinical sequelae of intravascular hemolysis and extracellular plasma hemoglobin. A novel mechanism of human disease
    • Rother R.P., Bell L., Hillmen P., and Gladwin M.T. The clinical sequelae of intravascular hemolysis and extracellular plasma hemoglobin. A novel mechanism of human disease. JAMA 293 (2005) 1653-1662
    • (2005) JAMA , vol.293 , pp. 1653-1662
    • Rother, R.P.1    Bell, L.2    Hillmen, P.3    Gladwin, M.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.