The influence of PAMAM-OH dendrimers on the activity of human erythrocytes ATPases

Biochim Biophys Acta. 2011 Nov;1808(11):2714-23. doi: 10.1016/j.bbamem.2011.07.021. Epub 2011 Jul 23.

Abstract

Dendrimers are a relatively new and still not fully examined group of polybranched polymers. In this study polyamidoamine dendrimers with hydroxyl surface groups (PAMAM-OH) of third, fourth and fifth generation (G3, G4 and G5) were examined for their ability to influence the activity of human erythrocyte plasma membrane adenosinetriphosphatases (ATPases). Plasma membrane ATPases are a group of enzymes related, among others, to the maintenance of ionic balance inside the cell. An inhibition of their activity may result in a disturbance of cell functioning. Two of examined dendrimers (G4 and G5) were found to inhibit the activity of Na(+)/K(+) ATPase and Ca(2+) ATPase by 20-30%. The observed effect was diminished when higher concentrations of dendrimers were used. The experiment with the use of pyrene as fluorescent probe sensitive to the changes in microenvironment's polarity revealed that it was an effect of dendrimers' self-aggregation. Additional studies showed that PAMAM-OH dendrimers were able to decrease the fluidity of human erythrocytes plasma membrane. Obtained results suggest that change in plasma membrane fluidity was not caused by the dendrimer-lipid interaction, but dendrimer-protein interaction. Different pattern of influence of dendrimers on ATPases activity and erythrocyte membrane fluidity suggests that observed change in ATPases activity is not a result of dendrimer-lipid interaction, but may be related to direct interaction between dendrimers and ATPases.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / metabolism*
  • Calcium-Transporting ATPases / metabolism
  • Cell Membrane / drug effects
  • Cell Membrane / enzymology
  • Cells, Cultured
  • Dendrimers / chemistry
  • Dendrimers / pharmacology*
  • Enzyme Activation / drug effects
  • Erythrocytes / drug effects
  • Erythrocytes / enzymology*
  • Humans
  • Molecular Structure
  • Sodium-Potassium-Exchanging ATPase / metabolism

Substances

  • Dendrimers
  • PAMAM Starburst
  • Adenosine Triphosphatases
  • Calcium-Transporting ATPases
  • Sodium-Potassium-Exchanging ATPase