Erythrocyte membrane reacylation in juvenile neuronal ceroid-lipofuscinosis: measurement of membrane-bound carnitine palmitoyl transferase, acyl-CoA synthetase, and lysophospholipid: acyl-CoA acyltransferase activities

Am J Med Genet. 1995 Jun 5;57(2):304-6. doi: 10.1002/ajmg.1320570239.

Abstract

In order to study the biochemical mechanisms responsible for the membrane fatty acid deficiency in juvenile neuronal ceroid-lipofuscinosis, we have analyzed the reacylation pathway in isolated erythrocyte membranes in 5 patients. We studied membrane carnitine palmitoyl transferase, and developed a combined assay to study acyl-CoA synthetase and lysophospholipid acyl-CoA acyltransferase activities. There were no significant differences between control and patient membranes, suggesting that abnormalities in these 3 putative candidate enzymes are not responsible for the disease.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • 1-Acylglycerophosphocholine O-Acyltransferase / blood*
  • Carnitine O-Palmitoyltransferase / blood*
  • Child
  • Coenzyme A Ligases / blood*
  • Erythrocyte Membrane / enzymology*
  • Humans
  • Neuronal Ceroid-Lipofuscinoses / blood*
  • Neuronal Ceroid-Lipofuscinoses / enzymology
  • Reference Values
  • Repressor Proteins*
  • Saccharomyces cerevisiae Proteins*

Substances

  • Repressor Proteins
  • Saccharomyces cerevisiae Proteins
  • Carnitine O-Palmitoyltransferase
  • 1-Acylglycerophosphocholine O-Acyltransferase
  • Coenzyme A Ligases
  • FAA2 protein, S cerevisiae
  • long-chain-fatty-acid-CoA ligase