The binding of plasminogen fragments to cultured human umbilical vein endothelial cells

Biochem Biophys Res Commun. 1992 Oct 30;188(2):703-11. doi: 10.1016/0006-291x(92)91113-5.

Abstract

Glu-plasminogen, kringle 1-5, kringle 1-3, and miniplasminogen exhibited strong binding to human umbilical vein endothelial cells (HUVEC). On the other hand, no significant binding was obtained with microplasminogen and kringle 4. Kringle 1-5 and miniplasminogen, which both contained kringle 5, specifically inhibited the binding of plasminogen to HUVEC while kringle 1-3 did not. The results implied plasminogen molecule contained at least two binding sites, with which it interacted HUVEC. The stronger binding site was located in kringle 5 and the weaker one was in kringle 1-3. Kringle 4 and the active site domain exhibited no significant binding to HUVEC. The interaction of plasminogen with HUVEC is mainly through binding site on kringle 5.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Cells, Cultured
  • Electrophoresis, Polyacrylamide Gel
  • Endothelium, Vascular / metabolism*
  • Humans
  • Iodine Radioisotopes
  • Kinetics
  • Molecular Weight
  • Peptide Fragments / isolation & purification
  • Peptide Fragments / metabolism*
  • Plasminogen / metabolism*
  • Protein Conformation
  • Umbilical Veins

Substances

  • Iodine Radioisotopes
  • Peptide Fragments
  • Plasminogen