Recent Progress in the Development of Recombinant Human Hemoglobin (rHb1.1) as an Oxygen Therapeutic

Freytag, J W; Caspari, R.F.; Gorczynski, Richard J.

doi:10.1016/b978-044420524-7/50006-0

Cited by 2 publications

(13 citation statements)

References 18 publications

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“…Furthermore, Marquardt and colleagues prepared di-Hb in which two rHb1.1 units are covalently cross-linked by gene fusion using a peptide linker and they also prepared tetra-Hb that is chemically cross-linked with bismaleimidohexane between a cysteine residue into di-Hb [14]. A pharmacokinetic study in rats demonstrated that the half-life of di-Hb and tetra-Hb are approximately 1.4 and 1.6 times longer than that of rHb1.1 [14,15]. …”

Section: Recombinant Hb (Rhb11 Optro®)mentioning

confidence: 99%

Comparison of the Pharmacokinetic Properties of Hemoglobin-Based Oxygen Carriers

Taguchi

Yamasaki

Maruyama

et al. 2017

JFB

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Hemoglobin (Hb) is an ideal material for use in the development of an oxygen carrier in view of its innate biological properties. However, the vascular retention of free Hb is too short to permit a full therapeutic effect because Hb is rapidly cleared from the kidney via glomerular filtration or from the liver via the haptogloblin-CD 163 pathway when free Hb is administered in the blood circulation. Attempts have been made to develop alternate acellular and cellular types of Hb based oxygen carriers (HBOCs), in which Hb is processed via various routes in order to regulate its pharmacokinetic properties. These HBOCs have been demonstrated to have superior pharmacokinetic properties including a longer half-life than the Hb molecule in preclinical and clinical trials. The present review summarizes and compares the pharmacokinetic properties of acellular and cellular type HBOCs that have been developed through different approaches, such as polymerization, PEGylation, cross-linking, and encapsulation.

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Section: Recombinant Hb (Rhb11 Optro®)mentioning

confidence: 99%

Comparison of the Pharmacokinetic Properties of Hemoglobin-Based Oxygen Carriers

Taguchi

Yamasaki

Maruyama

et al. 2017

JFB

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“…c. Genetically Engineered Hemoglobin. Production of recombinant modified human Hb (rHb, section IV.E) is attractive and has resulted in superb scientific achievements. ,− Manufacture of rHb requires expression of α and β globins, the presence or addition of sufficient heme and its incorporation into the protein, proper folding, separation of the resulting Hb from other bacterial proteins, lipids, nucleic acids, and endotoxins, and thorough purification. Because of the large dose of protein that needs to be administered in order to provide clinical efficacy, the acceptable level of endotoxins and other contamination must be extremely low.…”

Section: Raw Materials Procurementmentioning

confidence: 99%

“…Normal and modified human Hb genes were expressed in bacteria ( E. coli ), ,,,,− ,,− yeast ( Saccharomyces cerevisiae ), ,− mice, − pigs, ,, and plants, in particular tobacco, allowing the production of a large variety of normal and mutant rHbs. The availability of a precise three-dimensional structure of Hb 226 was instrumental for the design of these proteins.…”

Section: E Genetic Engineering Of Hemoglobinmentioning

confidence: 99%

“…Genetic engineering opens fascinating perspectives in terms of manipulation of the properties of Hb. It might ideally provide Hb mutants with (simultaneously) increased molecular stability, reduced O 2 affinity, reduced autoxidation rate, reduced rate of reaction with NO, and increased circulation half-life. ,,,,, …”

Section: E Genetic Engineering Of Hemoglobinmentioning

confidence: 99%

“…The circulation half-life of Hb products is generally described by a single number, although most products consist of an array of species with different pharmacokinetics and, possibly, different mechanisms contributing to clearance at different time points. Clearance from circulation is strongly species and dose-dependent. ,,,,1071a,− It did not always fit an exponential decay model and was sometimes clearly biphasic. ,,,1071a Many Hb products were found to diffuse out of the vasculature into the interstitial spaces, serous cavities, and gastrointestinal and respiratory tracts, which can translate into significant changes in intravascular volume. Initial rapid loss from circulation was seen with stroma-free Hb, polymerized pyridoxalated Hb, ATP-modified Hb, α,α-DBBF-cross-linked Hb, , pseudo-cross-linked Hb, NFPLP-cross-linked Hb, α,α-DBBF cross-linked Hb distributed rapidly in the skin, muscle, and skeleton .…”

Section: Protein Modification Has An Impact On Oxygen Deliverymentioning

confidence: 99%

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Oxygen Carriers (“Blood Substitutes”)Raison d'Etre, Chemistry, and Some PhysiologyBlut ist ein ganz besondrer Saft

2001

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Pharmaceutical Corporation in San Diego; however, the opinion expressed here are solely his and not necessarily those of the Corporation. Jean G. Riess received his chemical engineer and doctorat-e `s-sciences degrees (the latter with Professor Guy Ourisson in 1963) from the University of Strasbourg. He then spent two years with John Van Wazer at Monsanto in Saint-Louis, MO, learning some phosphorus and transitionmetal chemistry. In 1968 he became Professor at the University of Nice, France, where he founded, directed, and eventually became honorary director of the Unite ´de Chimie Mole ´culaire (associated with the Centre National de la Recherche Scientifique). His research successively involved phosphorus chemistry, transition-metal chemistry, organometallics, and eventually perfluorochemicals. His present interests are in fluorocarbons, fluorinated amphiphiles, and their colloid chemistry, including fluorocarbon emulsions for in vivo O 2 delivery, fluorinated self-assemblies, and drug delivery systems. Professor Riess has published about 360 papers and holds ca. 25 patents. He has served on numerous councils and committees and has chaired or co-chaired international conferences on phosphorus chemistry and blood substitutes. He has won awards from the French Academy of Sciences, French Chemical Society, Alexander von Humboldt Stifftung, City of Nice and Controlled Release Society, as well as Alliance's first Distinguished Contribution Award. He holds an honorary Research Associate position at the University of California at San Diego and sits on the Board of Directors of Alliance Pharmaceutical Corp.

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Recent Progress in the Development of Recombinant Human Hemoglobin (rHb1.1) as an Oxygen Therapeutic

Cited by 2 publications

References 18 publications

Comparison of the Pharmacokinetic Properties of Hemoglobin-Based Oxygen Carriers

Comparison of the Pharmacokinetic Properties of Hemoglobin-Based Oxygen Carriers

Oxygen Carriers (“Blood Substitutes”)Raison d'Etre, Chemistry, and Some PhysiologyBlut ist ein ganz besondrer Saft

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