ArticleNitric oxide : biology and chemistry2012
Enhanced nitrite reductase activity associated with the haptoglobin complexed hemoglobin dimer: functional and antioxidative implications.
Article in Nitric oxide : biology and chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 19 citations in OpenAlex.
- How Nitric Oxide Hindered the Search for Hemoglobin-Based Oxygen Carriers as Human Blood Substitutes.International journal of molecular sciences · 2023Review
- Interaction between a haptoglobin genetic variant and coronary artery disease (CAD) risk factors on CAD severity in Singaporean Chinese population.Molecular genetics & genomic medicine · 2020Article
- PPAR-Behavioural neurology · 2018Article
- HbE/β-Thalassemia and Oxidative Stress: The Key to Pathophysiological Mechanisms and Novel Therapeutics.Antioxidants & redox signaling · 2017Review
- Evaluating the capacity to generate and preserve nitric oxide bioactivity in highly purified earthworm erythrocruorin: a giant polymeric hemoglobin with potential blood substitute properties.The Journal of biological chemistry · 2015Article
- Redox properties of human hemoglobin in complex with fractionated dimeric and polymeric human haptoglobin.Free radical biology & medicine · 2014Article
- Generating S-nitrosothiols from hemoglobin: mechanisms, conformational dependence, and physiological relevance.The Journal of biological chemistry · 2013Article
- HBOC vasoactivity: interplay between nitric oxide scavenging and capacity to generate bioactive nitric oxide species.Antioxidants & redox signaling · 2013Review
- Cell-free hemoglobin and its scavenger proteins: new disease models leading the way to targeted therapies.Cold Spring Harbor perspectives in medicine · 2013Review
- Haptoglobin genotype and risk markers of cardiovascular disease in patients with chronic kidney disease.International journal of nephrology · 2013Article
- Article
- Blood substitutes: evolution from noncarrying to oxygen- and gas-carrying fluids.ASAIO journal (American Society for Artificial Internal Organs : 1992)Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The presence of acellular hemoglobin (Hb) within the circulation is generally viewed as a pathological state that can result in toxic consequences. Haptoglobin (Hp), a globular protein found in the plasma, binds with high avidity the αβ dimers derived from the dissociation of Hb tetramer and thus helps clear free Hb. More recently there have been compelling indications that the redox properties of the Hp bound dimer (Hb-Hp) may play a more active role in controlling toxicity by limiting the potential tissue damage caused by propagation of the free-radicals generated within the heme containing globin chains. The present study further examines the potential protective effect of Hp through its impact on the production of nitric oxide (NO) from nitrite through nitrite reductase activity of the Hp bound αβ Hb dimer. The presented results show that the Hb dimer in the Hb-Hp complex has oxygen binding, CO recombination and spectroscopic properties consistent with an Hb species having properties similar to but not exactly the same as the R quaternary state of the Hb tetramer. Consistent with these observations is the finding that the initial nitrite reductase rate for Hb-Hp is approximately ten times that of HbA under the same conditions. These results in conjunction with the earlier redox properties of the Hb-Hp are discussed in terms of limiting the pathophysiological consequences of acellular Hb in the circulation.
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Registered trials
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