Complementation in Zellweger syndrome: biochemical analysis of newly generated peroxisomes

Hum Hered. 1992;42(3):172-8. doi: 10.1159/000154062.

Abstract

The Zellweger syndrome is characterized by a defect which results in the abnormal biogenesis of peroxisomes. As a consequence, metabolic activities associated with peroxisomes such as the oxidation of very long chain fatty acids, the synthesis of plasmalogens, and the catabolism of phytanic and pipecolic acids are impaired. Since this disorder is genetically heterogeneous and several complementation groups are known, we were able to study the normalization of peroxisomal activity during the process of complementation. The restoration of catalase and dihydroxyacetone phosphate acyltransferase activities peaked within 3-4 days postfusion while the oxidation of lignoceric acid was much delayed (7-8 days). Electron microscopy indicated that by 6 days following hybridization, peroxisome structure and density in heterokaryons was comparable to normal control cells. The heterogenous biochemical response during peroxisome normalization could be due to several factors including a possible requirement for restoration of peroxisomal structural integrity for maximum activation of certain metabolic pathways.

Publication types

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

MeSH terms

  • Acyltransferases / metabolism
  • Cell Line
  • Fatty Acids / metabolism
  • Genetic Complementation Test
  • Humans
  • Microbodies / metabolism*
  • Microbodies / ultrastructure
  • Oxidation-Reduction
  • Zellweger Syndrome / genetics*
  • Zellweger Syndrome / metabolism
  • Zellweger Syndrome / pathology

Substances

  • Fatty Acids
  • Acyltransferases
  • glycerone-phosphate O-acyltransferase
  • lignoceric acid