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Topography of ether phospholipid biosynthesis.

D Hardeman1, H van den Bosch

  • 1Centre for Biomembranes and Lipid Enzymology, University of Utrecht, The Netherlands.

Biochimica Et Biophysica Acta
|November 6, 1989
PubMed
Summary

Dihydroxyacetone-phosphate acyltransferase (DHAP-AT) activity was studied in peroxisomes. Acyl-DHAP, a lipid intermediate, rapidly moves across the peroxisomal membrane, facilitating ether lipid biosynthesis.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Lipid Metabolism

Background:

  • Ether lipid biosynthesis initiates with dihydroxyacetone-phosphate acyltransferase (DHAP-AT) on the peroxisomal membrane.
  • The product, acyl-DHAP, is converted to alkyl-DHAP by alkyl-DHAP synthase, with further steps occurring in peroxisomes and the endoplasmic reticulum.

Purpose of the Study:

  • To investigate the localization and transbilayer movement of acyl-DHAP within the peroxisomal membrane.
  • To understand the interaction between DHAP-AT and alkyl-DHAP synthase in ether lipid biosynthesis.

Main Methods:

  • Modified assay conditions for DHAP-AT (omission of BSA, lower temperature and palmitoyl-CoA concentration).
  • Labeling peroxisomes with endogenously generated acyl-DHAP.
  • Extraction of acyl-DHAP with BSA and assessment of its extractability.
  • Trypsin treatment of peroxisomes.
  • Assays using large unilamellar vesicles (LUVs) composed of peroxisomal phospholipids.
  • Enzyme kinetic studies comparing endogenous and exogenous acyl-DHAP.

Main Results:

  • Endogenously generated acyl-DHAP was rapidly extractable from the outer peroxisomal surface, indicating fast transbilayer movement.
  • Trypsin treatment did not alter acyl-DHAP extractability.
  • A small proportion of non-extractable acyl-DHAP accumulated upon short incubation.
  • No transmembrane movement of acyl-DHAP was observed in peroxisomal phospholipid LUVs.
  • Acyl-DHAP served as a substrate for alkyl-DHAP synthase.
  • Endogenously generated acyl-DHAP was utilized more efficiently than exogenously added substrate.

Conclusions:

  • Acyl-DHAP exhibits rapid transbilayer movement across the peroxisomal membrane, despite its localization at the inner surface.
  • The efficient utilization of endogenously generated acyl-DHAP suggests a functional complex between DHAP-AT and alkyl-DHAP synthase within the peroxisomal membrane.

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