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This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Melamed-Frank, M. Articles by Levy, A. P. Search for Related Content PubMed PubMed Citation Articles by Melamed-Frank, M. Articles by Levy, A. P. Related Collections Hemostasis, Thrombosis, and Vascular Biology Red Cells Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 15 December 2001, Vol. 98, No. 13, pp. 3693-3698 HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY Structure-function analysis of the antioxidant properties of haptoglobin Meira Melamed-Frank, Orit Lache, Benjamin I. Enav, Tal Szafranek, Nina S. Levy, Rebecca M. Ricklis, and Andrew P. Levy From the Technion Faculty of Medicine, Technion-Israel Institute of Technology, Bat Galim, Israel. 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. © 2001 by The American Society of Hematology.   CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: F. M. Nakhoul, R. Miller-Lotan, H. Awad, R. Asleh, K. Jad, N. Nakhoul, R. Asaf, N. Abu-Saleh, and A. P. Levy Pharmacogenomic effect of vitamin E on kidney structure and function in transgenic mice with the haptoglobin 2-2 genotype and diabetes mellitus Am J Physiol Renal Physiol, April 1, 2009; 296(4): F830 - F838. [Abstract] [Full Text] [PDF] M. T. Gladwin and E. Vichinsky Pulmonary Complications of Sickle Cell Disease N. Engl. J. Med., November 20, 2008; 359(21): 2254 - 2265. [Full Text] [PDF] R. Asleh, S. Blum, S. Kalet-Litman, J. Alshiek, R. 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