The multi-functional role of sphingosylphosphorylcholine

Graeme F. Nixon* (Corresponding Author), Fiona A. Mathieson, Irene Hunter

*Corresponding author for this work

Research output: Contribution to journalLiterature review

77 Citations (Scopus)
7 Downloads (Pure)


The sphingomyelin metabolite, sphingosylphosphorylcholinc (SPC) has been the subject of much recent interest and controversy. Studies have indicated that SPC naturally occurs in plasma and a constituent of lipoproteins. Synthesis is also increased in some pathological conditions. Research has demonstrated that SPC is a potentially important lipid mediator of cell type specific functions in major tissues, such as heart, blood vessels, skin, brain and immune system. These effects are regulated via a number of different intracellular signalling cascades, also dependent upon cell type. Initial reports identifying high affinity SPC receptors at first appeared to reinforce the physiological relevance of this sphingolipid. However, these studies have now been retracted. Some SPC effects have been shown be occur via plasma membrane receptors for the related sphingolipid, sphingosine I-phosphate (SIP). Despite a lack of well-defined receptor signal transduction mechanisms and sparse pharmacological data, several key characteristics of SPC are now emerging. SPC can act as a mitogen in several different cell types and in certain circumstances, may also be a pro-inflammatory mediator. In this review, these actions of SPC are discussed with a view to understanding the potential physiological relevance of this sphingolipid. (c) 2007 Elsevier Ltd. All rights reserved.

Original languageEnglish
Pages (from-to)62-75
Number of pages14
JournalProgress in Lipid Research
Publication statusPublished - 2008


  • sphingosylphosphorylcholine
  • sphingosine 1-phosphate
  • cardiovascular
  • inflammation
  • epidermis
  • calcium
  • protein-coupled receptor
  • vascular smooth-muscle
  • sphingosine 1-phosphate receptor
  • mesenchymal stem-cells
  • niemann-pick-disease
  • lipoprotein-associated lysosphingolipids
  • intercellular-adhesion molecule-1
  • phospholipase-c activation
  • human dermal fibroblasts
  • human endothelial-cells


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