Haptoglobin and CD163: captor and receptor gating hemoglobin to macrophage lysosomes

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

The plasma protein haptoglobin and the endocytic hemoglobin receptor HbSR/CD163 are key molecules in the process of removing hemoglobin released from ruptured erythrocytes. Hemoglobin in plasma is instantly bound with high affinity to haptoglobin--an interaction leading to the recognition of the complex by HbSR/CD163 and endocytosis in macrophages. The haptoglobin-dependent HbSR/CD163 scavenging system for hemoglobin clearance prevents toxic effects of hemoglobin in plasma and kidney and explains the decrease in the haptoglobin plasma concentration in patients with accelerated hemolysis. The HbSR/CD163 activity may be of quantitative importance for iron uptake in macrophages in general and for some iron-associated pathological processes, e.g. the atherogenesis-promoting oxidation of LDL leading to foam cell formation and apoptosis in the vessel wall.

Original languageEnglish
JournalRedox Report (Online)
Volume6
Issue number6
Pages (from-to)386-388
ISSN1351-0002
DOIs
Publication statusPublished - 2001
Externally publishedYes

Keywords

  • Animals
  • Antigens, CD
  • Antigens, Differentiation, Myelomonocytic
  • Apoptosis
  • CHO Cells
  • Cell Membrane
  • Cricetinae
  • Haptoglobins
  • Humans
  • Lipid Peroxides
  • Lysosomes
  • Macrophages
  • Oxygen
  • Protein Structure, Tertiary
  • Receptors, Cell Surface
  • Transfection

Fingerprint

Dive into the research topics of 'Haptoglobin and CD163: captor and receptor gating hemoglobin to macrophage lysosomes'. Together they form a unique fingerprint.

Cite this