5/1/23, 22:11 Haptoglobin - PubMed

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Review Antioxid Redox Signal. 2017 May 10;26(14):814-831. doi: 10.1089/ars.2016.6793.

Epub 2016 Nov 8.

Haptoglobin
Christian Brix Folsted Andersen  1 , Kristian Stødkilde  1 , Kirstine Lindhardt Sæderup  2 , Anne Kuhlee  3 , 
Stefan Raunser  3 , Jonas H Graversen  2 , Søren Kragh Moestrup  1   2   4

Affiliations
PMID: 27650279 DOI: 10.1089/ars.2016.6793

Abstract
Haptoglobin (Hp) is an abundant human plasma protein that tightly captures hemoglobin (Hb) during
hemolysis. The Hb-Hp complex formation reduces the oxidative properties of heme/Hb and promotes
recognition by the macrophage scavenger receptor CD163. This leads to Hb-Hp breakdown and heme
catabolism by heme oxygenase and biliverdin reductase. Gene duplications of a part of or the entire
Hp gene in the primate evolution have led to variant Hp gene products that collectively may be
designated "the haptoglobins (Hps)" as they all bind Hb. These variant products include the human-
specific multimeric Hp phenotypes in individuals, which are hetero- or homozygous for an Hp2 gene
allele. The Hp-related protein (Hpr) is another Hp duplication product in humans and other primates.
Alternative functions of the variant Hps are indicated by numerous reports on association between Hp
phenotypes and disease as well as the elucidation of a specific role of Hpr in the innate immune
defense. Recent Advances: Recent functional and structural information on Hp and receptor systems
for Hb removal now provides insight on how Hp carries out essential functions such as the Hb
detoxification/removal, and how Hpr, by acting as an Hp-lookalike, can sneak a lethal toxin into
trypanosome parasites that cause mammalian sleeping sickness. Critical Issues and Future Directions:
The new structural insight may facilitate ongoing attempts of developing Hp derivatives for
prevention of Hb toxicity in hemolytic diseases such as sickle cell disease and other
hemoglobinopathies. Furthermore, the new structural knowledge may help identifying yet unknown
functions based on other disease-relevant biological interactions involving Hps. Antioxid. Redox
Signal. 26, 814-831.

Keywords: blood; heme oxygenase; inflammation; metabolism; receptors.

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https://pubmed.ncbi.nlm.nih.gov/27650279/ 1/1