Inhibition of the translocation of cytidylyltransferase can be a delayed mechanism to control phosphatidylcholine biosynthesis "in vivo"

Life Sci. 1990;47(14):1181-6. doi: 10.1016/0024-3205(90)90209-a.

Abstract

To determine whether CTP: Phosphocholine cytidylyltransferase is responsible for the previously observed decrease in phosphatidylcholine biosynthesis during thioacetamide treatment, rats were injected daily i.p. with either this agent (50 mg/kg/day) or diluent for 3 and 60 days. Microsomal and cytosolic enzymatic activities were estimated. Results demonstrated that cytosolic enzyme activity appears significantly decreased; however microsomal enzyme only appears significantly decreased after 60 days of treatment. At this time period microsomal percentage of enzyme activity is also significantly decreased. From these results it can be deduced that inhibition of enzyme translocation can be a delayed adaptative response "in vivo".

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Biological Transport
  • Choline-Phosphate Cytidylyltransferase
  • Liver / drug effects
  • Liver / enzymology*
  • Male
  • Microsomes, Liver / drug effects
  • Microsomes, Liver / enzymology
  • Nucleotidyltransferases / metabolism*
  • Phosphatidylcholines / biosynthesis*
  • Rats
  • Rats, Inbred Strains
  • Thioacetamide / pharmacology

Substances

  • Phosphatidylcholines
  • Thioacetamide
  • Nucleotidyltransferases
  • Choline-Phosphate Cytidylyltransferase