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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/31292
Title: Trapping of human hemoglobin by haptoglobin: Molecular mechanisms and clinical applications
Authors: Khuanpiroon Ratanasopa
Sandeep Chakane
Muhammad Ilyas
Chanin Nantasenamat
Leif Bulow
Lunds Universitet
Mahidol University
Keywords: Biochemistry, Genetics and Molecular Biology
Issue Date: 10-Jun-2013
Citation: Antioxidants and Redox Signaling. Vol.18, No.17 (2013), 2364-2374
Abstract: Significance: Haptoglobin (Hp) is an abundant plasma protein controlling the fate of hemoglobin (Hb) released from red blood cells after intravascular hemolysis. The complex formed between Hp and Hb is extraordinary strong, and once formed, this protein-protein association can be considered irreversible. Recent Advances: A model of the Hp-Hb complex has been generated and the first steps toward understanding the mechanism behind the shielding effects of Hp have been taken. The clinical potential of the complex for modulating inflammatory reactions and for functioning as an Hb-based oxygen carrier have been described. Critical Issues: The three-dimensional structure of the Hp-Hb complex is unknown. Moreover, Hp is not a homogeneous protein. There are two common alleles at the Hp genetic locus denoted Hp1 and Hp2, which when analyzed on the protein levels result in differences between their physiological behavior, particularly in their shielding against Hb-driven oxidative stress. Additional cysteine residues on the α-subunit allow Hp2 to form a variety of native multimers, which influence the biophysical and biological properties of Hp. The multimeric conformations, in turn, also modulate the glycosylation patterns of Hp by steric hindrance. Future Directions: A detailed analysis of the influence of Hp glycosylation will be instrumental to generate a deeper understanding of its biological function. Several pathological conditions also modify the glycan compositions allowing Hp to be potentially used as a marker protein for these disorders. Antioxid. Redox Signal. 18, 2364-2374. © 2013, Mary Ann Liebert, Inc.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84876908109&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/31292
ISSN: 15577716
15230864
Appears in Collections:Scopus 2011-2015

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