Effect of bradykinin and PMA on the synthesis of proteoglycans during the cell cycle of endothelial cells in culture

Int Immunopharmacol. 2003 Mar;3(3):293-8. doi: 10.1016/S1567-5769(02)00262-X.

Abstract

Bradykinin (BK) and phorbol 12-myristate-13-acetate (PMA) were used in the present work to study the biosynthesis of proteoglycans (PG) during the cell cycle of endothelial cells. PMA, an activator of PKC, stimulated the synthesis of heparan sulfate proteoglycan (HSPG) secreted to the medium of endothelial cells mainly during the G(1) phase of the cell cycle [J. Cell. Biochem. 70 (1998) 563]. BK is a vasoactive peptide that increases calcium levels inside the cells indirectly stimulating PKC. Treatment of the endothelial cells with BK, as well as PMA, stimulated the synthesis of HSPG secreted to the medium and produced an antimitogenic effect on the cell cycle. These results led to the conclusion that PKC is directly involved in the synthesis of HSPG secreted to the medium. Also, comparing the effect showed by BK with PMA, one may suggest that different PKC isoforms are involved in these two processes and that their isoforms are mainly Ca(2+) dependent.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 1-Butanol / pharmacology
  • Animals
  • Bradykinin / pharmacology*
  • Cell Cycle / drug effects
  • Cell Cycle / physiology*
  • Cells, Cultured
  • Endothelium, Vascular / cytology
  • Endothelium, Vascular / drug effects
  • Endothelium, Vascular / metabolism*
  • Enzyme Inhibitors / pharmacology
  • Glycosaminoglycans / biosynthesis
  • Glycosaminoglycans / metabolism
  • Heparitin Sulfate / biosynthesis
  • Protein Kinase C / antagonists & inhibitors
  • Proteoglycans / biosynthesis*
  • Rabbits
  • Tetradecanoylphorbol Acetate / pharmacology*
  • Thymidine / metabolism

Substances

  • Enzyme Inhibitors
  • Glycosaminoglycans
  • Proteoglycans
  • 1-Butanol
  • Heparitin Sulfate
  • Protein Kinase C
  • Tetradecanoylphorbol Acetate
  • Bradykinin
  • Thymidine