The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
Structure-function analysis of the antioxidant properties of haptoglobin
Abstract
Haptoglobin serves as an antioxidant by virtue of its ability to prevent hemoglobin-driven oxidative tissue damage. It was recently demonstrated that an allelic polymorphism in the haptoglobin gene is predictive of the risk for numerous microvascular and macrovascular diabetic complications. Because these complications are attributed in large part to an increase in oxidative stress, a study was conducted to determine whether the different protein products of the 2 haptoglobin alleles differed in the antioxidant protection they provided. A statistically significant difference was found in the antioxidant capacity of purified haptoglobin protein produced from the 2 different alleles, consistent with the hypothesis that differences in genetically determined antioxidant status may explain differential susceptibility to diabetic vascular complications. These differences may be amplified in the vessel wall because of differences in the sieving capacity of the haptoglobin types. Therefore, an attempt was made to identify the minimal haptoglobin sequences necessary to inhibit oxidation by hemoglobin in vitro, and 2 independent haptoglobin peptides that function in this fashion as efficiently as native haptoglobin were identified. Identification of the biochemical basis for differences among haptoglobin types may lead to the rational development of new pharmacologic agents, such as the mini-haptoglobin described here, to avert the development of diabetic vascular complications.
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Citations
Cites
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Biological and clinical significance of haptoglobin polymorphism in humans
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Exchange of Heme among Hemoglobins and between Hemoglobin and Albumin
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Haptoglobin: The Evolutionary Product of Duplication, Unequal Crossing Over, and Point Mutation
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The antioxidant activity of haptoglobin towards haemoglobin-stimulated lipid peroxidation
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Cited by
Mechanisms of Cell Protection by Heme Oxygenase-1
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Philippidis, P., Mason, J. C., Evans, B. J., Nadra, I., Taylor, K. M., Haskard, D. O., & Landis, R. C. (2004) · Circulation Research · doi:10.1161/01.res.0000109414.78907.f9 · Cited by 476
Pulmonary Complications of Sickle Cell Disease
Gladwin, M. T., & Vichinsky, E. (2008) · New England Journal of Medicine · doi:10.1056/nejmra0804411 · Cited by 470
Rose, D. R., Yang, H., Serena, G., Sturgeon, C., Ma, B., Careaga, M., Hughes, H. K., Angkustsiri, K., Rose, M., Hertz-Picciotto, I., et al. (2018) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2018.03.025 · Cited by 227
Hemoglobin and Heme Scavenger Receptors
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Metadata
- Authors
- Melamed-Frank, M., Lache, O., Enav, B. I., Szafranek, T., Levy, N. S., Ricklis, R. M., & Levy, A. P.
- Venue
- Blood
- Publisher
- American Society of Hematology
- Published
- 2001-12-15
- Volume
- 98
- Issue
- 13
- Pages
- 3693-3698
- ISSN
- 0006-4971 (ISSN-L)
- 1528-0020
- OpenAlex
- W2119412894
- Cited by
- 339
- References
- 27
- FWCI
- 2.58
- Type
- journal article
- Language
- en
- Open access
- closed
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- Melamed-Frank, M., Lache, O., Enav, B. I., Szafranek, T., Levy, N. S., Ricklis, R. M., & Levy, A. P. (2001). Structure-function analysis of the antioxidant properties of haptoglobin. Blood. https://doi.org/10.1182/blood.v98.13.3693
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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