Aliphatic aldehydes promote myelin basic protein-induced fusion of phospholipid vesicles

Biochim Biophys Acta. 1985 Nov 7;820(2):319-23. doi: 10.1016/0005-2736(85)90127-0.

Abstract

Myelin basic protein induces slow and limited fusion of phospholipid vesicles composed of a mixture of phosphatidylcholine and phosphatidylethanolamine. Addition of palmitoyl aldehyde to these vesicles dramatically increases their ability to fuse in the presence of myelin basic protein. Compared to aliphatic aldehydes, fatty acids are much less potent promoters of myelin basic protein-induced membrane fusion. The ability of aliphatic aldehydes to promote myelin basic protein-induced membrane fusion may be of relevance to myelin structure and function and, particularly, to the pathology of demyelinating diseases such as multiple sclerosis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aldehydes*
  • Animals
  • Freeze Fracturing
  • Membrane Fusion*
  • Myelin Basic Protein*
  • Phosphatidylcholines
  • Phosphatidylethanolamines
  • Phospholipids*
  • Protein Processing, Post-Translational
  • Structure-Activity Relationship

Substances

  • Aldehydes
  • Myelin Basic Protein
  • Phosphatidylcholines
  • Phosphatidylethanolamines
  • Phospholipids