Polynitroxyl hemoglobin: a pharmacokinetic study of covalently bound nitroxides to hemoglobin platforms

Buehler, Paul W.; Haney, Chad R.; Gulati, Anil; Ma, Li; Hsia, Carleton J. C.

doi:10.1016/j.freeradbiomed.2004.04.008

Cited by 30 publications

(18 citation statements)

References 36 publications

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“…Although albumin, aa cross-linked Hb, and polynitroxylated aa cross-linked Hb did improve these parameters, only the HBOCs improved survival time with the polynitroxylated HBOC, proving to be less hypertensive than other HBOCs as measured by increases in both cardiac output and systemic vascular resistance (41). Similar results have been noted with the polynitroxyation of other HBOCs (40). Therefore, this approach to add antioxidant activity directly onto HBOCs, may improve the efficacious of HBOCs as resuscitative fluids.…”

Section: A the Rational Design Of Hemoglobin-based Oxygen Carriersmentioning

confidence: 55%

The Redox Activity of Hemoglobins: From Physiologic Functions to Pathologic Mechanisms

Reeder

2010

Antioxidants & Redox Signaling

165

188

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Pentacoordinate respiratory hemoproteins such as hemoglobin and myoglobin have evolved to supply cells with oxygen. However, these respiratory heme proteins are also known to function as redox enzymes, reacting with compounds such as nitric oxide and peroxides. The recent discoveries of hexacoordinate hemoglobins in vertebrates and nonsymbiotic plants suggest that the redox activity of globins is inherent to the molecule. The uncontrolled formation of radical species resulting from such redox chemistry on respiratory hemoproteins can lead to oxidative damage and cellular toxicity. In this review, we examine the functions of various globins and the mechanisms by which these globins act as redox enzymes under physiologic conditions. Evidence that redox reactions also occur under disease conditions, leading to pathologic complications, also is examined, focusing on recent discoveries showing that the ferryl oxidation state of these hemoproteins is present in these disease states in vivo. In addition, we review the latest advances in the understanding of globin redox mechanisms and how they might affect cellular signaling pathways and how they might be controlled therapeutically or, in the case of hemoglobin-based blood substitutes, through rational design.

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Section: A the Rational Design Of Hemoglobin-based Oxygen Carriersmentioning

confidence: 55%

The Redox Activity of Hemoglobins: From Physiologic Functions to Pathologic Mechanisms

Reeder

2010

Antioxidants & Redox Signaling

165

188

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“…On the other hand, it would be a folly not to use a more complex substitute if indicated. We also need to intensify research on the many important ongoing developments around the world (Bian et al 2011, Buehler et al 2004,Gould et al 1995, Hoffman et al 1990, Natanson et al 2008, Seetharama et al 2013, Sims et al 2001, Tam et al 1976, Wei et al 2013, Yabuki et al 1990, Yu et al 2010, Zhu et al 2007, Zhou et,al. 2013, Lui and Kluger 2010, Wong and Chang 2007, Bucci 2011, Chang 1957, Greenburg 2013, Sakai 2013, Wong 1988.…”

mentioning

confidence: 99%

Red blood cell replacement, or nanobiotherapeutics with enhanced red blood cell functions?

Chang

2015

Artificial Cells, Nanomedicine, and Biotechnology

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“…Ischemia-reperfusion injury has been noted to occur after cardiopulmonary bypass in children undergoing surgery for congenital heart disease (Shum-Tim). An extension of our PolyHb-SOD-CAT approach is the development of synthetic mimics of SOD for complexing with modifi ed hemoglobin in the form of polynitroxyl hemoglobin with covalently bound nitroxides (Buehler et al 2004). …”

Section: Discussionmentioning

confidence: 99%

Nanobiotechnology-based Blood Substitutes and the Cardiovascular Systems in Transfusion Medicine

Hunter¹,

Preedy²

2011

Nanomedicine and the Cardiovascular System

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Red blood cell membrane contains blood group antigens, and typing and matching are needed before donor blood can be transfused into patients. This results in delays in emergency situations. Donor blood requires storage at 4ºC using standard methods and is good for less than 42 d. Red blood cells cannot be sterilized to remove hepatitis viruses, HIV and other potential emerging infective agents. There is also a shortage of donor blood especially in emergencies, war or disasters. Nanobiotechnology has allowed the development of different types of red blood cell substitutes. The fi rst-generation type is a simple modifi ed hemoglobin oxygen carrier that has immediate potential for clinical uses. In particular, such substitutes do not have blood group antigens and can be

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Polynitroxyl hemoglobin: a pharmacokinetic study of covalently bound nitroxides to hemoglobin platforms

Cited by 30 publications

References 36 publications

The Redox Activity of Hemoglobins: From Physiologic Functions to Pathologic Mechanisms

The Redox Activity of Hemoglobins: From Physiologic Functions to Pathologic Mechanisms

Red blood cell replacement, or nanobiotherapeutics with enhanced red blood cell functions?

Nanobiotechnology-based Blood Substitutes and the Cardiovascular Systems in Transfusion Medicine

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