Glycophorins

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Glycophorins are integral membrane proteins in the cell membrane of erythrocytes . Glycophorins are the most common transmembrane proteins found in human erythrocytes. They are heavily glycolized and contribute (along with other glycoproteins and glycolipids ) to the negative charges on the surface of the erythrocyte membrane. By rejecting other negatively charged molecules, this charge prevents interactions with other blood components and endothelial cells . Glycophorins are on the adapter proteins ankyrin , band-4.1 protein , and actin with Spektrinfilamenten linked.

Glycophorins are used by the malaria pathogen Plasmodium falciparum to get into the erythrocytes.

Four glycophorins are known in humans:

  • Glycophorin A
  • Glycophorin B
  • Glycophorin C
  • Glycophorin E.

literature

  • Löffler / Petridas: Biochemistry and Pathobiochemistry . 9th edition. Springer-Verlag, Berlin 2014, ISBN 978-3-642-17972-3 , pp. 516 .

Further literature

  • C. Bauer, W. Wuillemin. Blood, Plasma Proteins, Coagulation, Fibrinolysis, Comprehensive Human Physiology and Thrombocyte Function. Comprehensive Human Physiology. 1996. pp 1651-1677

Individual evidence

  1. ↑ p55 p55 Protein Is a Member of PSD Scaffold Proteins in the Rat Brain and Interacts With Various PSD Proteins doi : 10.1016 / j.molbrainres.2004.12.023
  2. ↑ a b Löffler / Petridas: Biochemistry and Pathobiochemistry . 9th edition. Springer-Verlag, Berlin 2014, ISBN 978-3-642-17972-3 , pp. 516 .