S-adenosyl-L-methionine synthetase and phospholipid methyltransferase are inhibited in human cirrhosis

Hepatology. 1988 Jan-Feb;8(1):65-8. doi: 10.1002/hep.1840080113.

Abstract

We have measured the activity S-adenosyl-L-methionine synthetase in liver biopsies from a group of controls (n = 17) and in 26 cirrhotics (12 alcoholic and 14 posthepatic). The activity of this enzyme was markedly reduced in the group of cirrhotics (285 +/- 32 pmoles per min per mg protein) when compared with that observed in controls (505 +/- 37 pmoles per min per mg protein). No differences in S-adenosyl-L-methionine synthetase was observed between both groups of cirrhotics. Similarly, a marked reduction in the activity phospholipid methyltransferase was also observed in liver biopsies from the same group of cirrhotics (105 +/- 12 pmoles per min per mg protein) when compared with the control subjects (241 +/- 13 pmoles per min per mg protein). Again, no difference in the activity of this enzyme was observed between both groups of cirrhotics. These results indicated a marked deficiency in the metabolism of S-adenosyl-L-methionine in cirrhosis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Female
  • Humans
  • Liver / enzymology
  • Liver Cirrhosis / enzymology*
  • Liver Cirrhosis, Alcoholic / enzymology*
  • Male
  • Methionine Adenosyltransferase / metabolism*
  • Methyltransferases / metabolism*
  • Middle Aged
  • Phosphatidyl-N-Methylethanolamine N-Methyltransferase
  • Phosphatidylethanolamine N-Methyltransferase
  • S-Adenosylmethionine / metabolism
  • Transferases / metabolism*

Substances

  • S-Adenosylmethionine
  • Transferases
  • Methyltransferases
  • Phosphatidylethanolamine N-Methyltransferase
  • Phosphatidyl-N-Methylethanolamine N-Methyltransferase
  • Methionine Adenosyltransferase