Protein synthesis of eucaryotic cells could be decreased by antisense-DNA of the multi KH domain protein vigilin

Int J Mol Med. 2003 Jul;12(1):35-43.

Abstract

Vigilin, a member of the KH protein family, is exceptional among these proteins as it contains 14 KH domains in consecutive order. Vigilin is present in the nucleus and the cytoplasm of all eucaryotic cells studied so far and has apparently high affinity to tRNA and mRNA. There is circumstantial evidence that vigilin expression parallels high translational activity as demonstrated for pancreatic cells in vitro and in vivo as well as for carcinoma cell lines. On a molecular level we have recently demonstrated that vigilin promotes in vitro the export of tRNA from the nucleus to the translational machinery in the cytoplasm and may hence function as an intercompartimental conveyor. In the present study we show that exposure to a vigilin antisense oligo DNA (VAOD) expectedly resulted in a decrease of vigilin-expression, and was concomitant to lower amylase- and trypsin synthesis in freshly isolated pancreatic cells. In addition, carcinoma cells reacted with an increased mortality under exposure to VAOD giving further support for the notion that vigilin participates in cellular life-sustaining processes such as protein translation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Carcinoma / drug therapy*
  • Carrier Proteins*
  • DNA, Antisense / pharmacology*
  • Humans
  • Immunoblotting
  • Male
  • Pancreas / drug effects*
  • Protein Structure, Tertiary
  • Protein Synthesis Inhibitors / pharmacology*
  • RNA-Binding Proteins / genetics*
  • Rats
  • Rats, Sprague-Dawley

Substances

  • Carrier Proteins
  • DNA, Antisense
  • Protein Synthesis Inhibitors
  • RNA-Binding Proteins
  • high density lipoprotein binding protein