Mechanism of action of didemnin B, a depsipeptide from the sea

Cancer Lett. 1984 Jul;23(3):279-88. doi: 10.1016/0304-3835(84)90095-8.

Abstract

With the brush border membrane vesicles prepared from the rat kidney cortex, didemnin B and its parent compound, didemnin A function neither as a K+-specific ionophore nor as an ionophore for Na+ ions while other depsipeptide antibiotics such as valinomycin and gramicidin promote transmembrane movement of K+ and Na+ ions, respectively. Didemnin B inhibits protein synthesis and DNA synthesis much more than RNA synthesis and is in general more potent than didemnin A. Time course studies reveal that the action of didemnin B is rapid and cannot be reversed after 2 h in contact with the cells. The inhibition of protein synthesis is almost superimposable to that of L1210 cells growth. DNA synthesis is also markedly inhibited. These results collectively suggest that didemnin B acts differently, at least in part, from other depsipeptide antibiotics and its biological effect is primarily mediated through its inhibition of protein synthesis and to a lesser extent its inhibition of DNA synthesis.

MeSH terms

  • Animals
  • Antibiotics, Antineoplastic*
  • Biological Transport, Active / drug effects
  • DNA, Neoplasm / biosynthesis
  • Depsipeptides*
  • In Vitro Techniques
  • Ionophores
  • Kidney Cortex / drug effects
  • Kidney Cortex / metabolism
  • Leukemia L1210 / drug therapy
  • Leukemia L1210 / metabolism
  • Male
  • Mice
  • Microvilli / drug effects
  • Microvilli / metabolism
  • Neoplasm Proteins / biosynthesis
  • Peptides, Cyclic / pharmacology
  • Potassium / metabolism
  • RNA, Neoplasm / biosynthesis
  • Rats
  • Sodium / metabolism

Substances

  • Antibiotics, Antineoplastic
  • DNA, Neoplasm
  • Depsipeptides
  • Ionophores
  • Neoplasm Proteins
  • Peptides, Cyclic
  • RNA, Neoplasm
  • didemnins
  • Sodium
  • Potassium