Roles and regulation of neutral sphingomyelinase-2 in cellular and pathological processes

Adv Biol Regul. 2015 Jan:57:24-41. doi: 10.1016/j.jbior.2014.10.002. Epub 2014 Oct 27.

Abstract

Our understanding of the functions of ceramide signaling has advanced tremendously over the past decade. In this review, we focus on the roles and regulation of neutral sphingomyelinase 2 (nSMase2), an enzyme that generates the bioactive lipid ceramide through the hydrolysis of the membrane lipid sphingomyelin. A large body of work has now implicated nSMase2 in a diverse set of cellular functions, physiological processes, and disease pathologies. We discuss different aspects of this enzyme's regulation from transcriptional, post-translational, and biochemical. Furthermore, we highlight nSMase2 involvement in cellular processes including inflammatory signaling, exosome generation, cell growth, and apoptosis, which in turn play important roles in pathologies such as cancer metastasis, Alzheimer's disease, and other organ systems disorders. Lastly, we examine avenues where targeted nSMase2-inhibition may be clinically beneficial in disease scenarios.

Keywords: Apoptosis; Ceramide; Exosomes; Inflammation; Sphingomyelinase.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Alzheimer Disease / genetics
  • Alzheimer Disease / metabolism*
  • Animals
  • Apoptosis*
  • Ceramides / genetics
  • Ceramides / metabolism
  • Exosomes / genetics
  • Exosomes / metabolism
  • Humans
  • Neoplasm Metastasis
  • Neoplasm Proteins / genetics
  • Neoplasm Proteins / metabolism*
  • Neoplasms / genetics
  • Neoplasms / metabolism*
  • Neoplasms / pathology
  • Protein Processing, Post-Translational / genetics
  • Signal Transduction*
  • Sphingomyelin Phosphodiesterase / genetics
  • Sphingomyelin Phosphodiesterase / metabolism*
  • Sphingomyelins / genetics
  • Sphingomyelins / metabolism
  • Transcription, Genetic / genetics

Substances

  • Ceramides
  • Neoplasm Proteins
  • Sphingomyelins
  • SMPD3 protein, human
  • Sphingomyelin Phosphodiesterase