Amyloid beta peptides stimulate tissue-type plasminogen activator but not recombinant prourokinase

Thromb Res. 1997 Feb 1;85(3):217-24. doi: 10.1016/s0049-3848(97)00006-6.

Abstract

Tissue-type plasminogen activator (rt-PA) and prourokinase (rscu-PA) have been tested with respect to the influence of amyloid beta peptides on plasminogen activation which was monitored by cleavage of the chromogenic plasmin substrate S-2251. It was shown that rt-PA is stimulated by amyloid beta peptides at concentrations of 10 micrograms/ml in contrast to prourokinase, which does not alter its catalytic properties in presence of amyloid beta peptides. The stimulation of rt-PA can be inhibited by tranexamic acid indicating a molecular mode of stimulation similar to the fibrin mediated stimulation of rt-PA.

MeSH terms

  • Amyloid beta-Peptides / pharmacology*
  • Antifibrinolytic Agents / pharmacology
  • Chromogenic Compounds
  • Depression, Chemical
  • Humans
  • Hydrolysis
  • In Vitro Techniques
  • Recombinant Proteins / metabolism
  • Tissue Plasminogen Activator / metabolism*
  • Tranexamic Acid / pharmacology
  • Urokinase-Type Plasminogen Activator / metabolism*

Substances

  • Amyloid beta-Peptides
  • Antifibrinolytic Agents
  • Chromogenic Compounds
  • Recombinant Proteins
  • Tranexamic Acid
  • Tissue Plasminogen Activator
  • Urokinase-Type Plasminogen Activator