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Related Concept Videos

Hemoglobin01:24

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Hemoglobin is a globular protein made up of four subunits. Two of these subunits are alpha chains, and the other two are beta chains. Each subunit contains a molecule of heme, which has an iron atom and can bind to oxygen. When an oxygen molecule binds to one heme group, it changes the shape of hemoglobin, making it easier for the other heme groups to bind oxygen as well.
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Cardiac biomarkers are enzymes, proteins, and hormones released into the blood when cardiac cells are injured. They are powerful tools for triaging.
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Related Experiment Video

Updated: Oct 23, 2025

A Precision Medicine Tool for Measurement and Monitoring of Hemoglobin S in Sickle Cell Disease Patients Receiving Transfusion Therapy
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Haptoglobin as a Biomarker.

S N Naryzny1,2, O K Legina2

  • 1Institute of Biomedical Chemistry, ul. Pogodinskaya 10, 119121 Moscow, Russia.

Biochemistry (Moscow) Supplement. Series B, Biomedical Chemistry
|August 23, 2021
PubMed
Summary

Haptoglobin (Hp), a plasma glycoprotein, binds hemoglobin and protects tissues. Its diverse forms (proteoforms) and genetic variations show potential as biomarkers for diseases, including cancer.

Keywords:
biomarkerhaptoglobin

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Clinical Chemistry

Background:

  • Haptoglobin (Hp) is a plasma glycoprotein crucial for binding free hemoglobin (Hb), preventing oxidative damage, and exhibiting regulatory functions.
  • As an acute-phase protein, Hp levels fluctuate in disease, making its measurement a standard clinical practice.
  • Hp is synthesized in the liver and lungs and is investigated as a biomarker for various pathologies, including malignant neoplasms.

Purpose of the Study:

  • To review the structural and functional diversity of haptoglobin.
  • To explore the potential of haptoglobin as a biomarker for various pathologies.
  • To highlight the significance of haptoglobin's post-translational modifications, particularly glycosylation, in disease states.

Main Methods:

  • Literature review of studies on haptoglobin structure, function, genetics, and PTMs.
  • Analysis of research on haptoglobin's role in disease, especially cancer.
  • Examination of haptoglobin phenotypes and proteoforms.

Main Results:

  • Haptoglobin exhibits significant structural and functional diversity due to genetic polymorphism and post-translational modifications (PTMs), including glycosylation.
  • The human *Нр* gene's polymorphism leads to three major phenotypes (Hp 1-1, Hp 2-2, Hp 2-1), influencing individual disease predisposition.
  • Post-translational modifications, especially glycosylation of the β-chain, create multiple haptoglobin proteoforms with potentially distinct functions, relevant to pathological processes like cancer.

Conclusions:

  • Haptoglobin's structural and functional diversity, driven by genetic and post-translational variations, suggests its potential as a versatile biomarker.
  • Understanding haptoglobin proteoforms and their modifications is key to advancing diagnostics for diseases, including malignancies.
  • Further research into haptoglobin's diverse roles can unlock new therapeutic and diagnostic strategies.