Stearoyl-CoA desaturase, a short-lived protein of endoplasmic reticulum with multiple control mechanisms

Prostaglandins Leukot Essent Fatty Acids. 2003 Feb;68(2):123-33. doi: 10.1016/s0952-3278(02)00262-4.


Stearoyl-CoA desaturase (SCD) is a short-lived, polytopic membrane-bound non-heme iron enzyme localized primarily in the endoplasmic reticulum. SCD is required for the biosynthesis of monounsaturated fatty acids, and plays a key role in hepatic synthesis of triglycerides and very-low-density lipoproteins. The intracellular concentration of SCD fluctuates in a wide range in response to complex and often competing hormonal and dietary factors. A combination of transcriptional regulation and rapid protein degradation produces transient elevations of SCD enzyme activity in response to physiologic demands. Dysregulation of SCD has been implicated in non-alcoholic fatty liver disease, hyperlipidemia, and obesity.

Publication types

  • Review

MeSH terms

  • Animals
  • CCAAT-Enhancer-Binding Proteins / metabolism
  • DNA, Complementary / metabolism
  • DNA-Binding Proteins / metabolism
  • Endoplasmic Reticulum / metabolism*
  • Fatty Acids, Unsaturated / metabolism
  • Humans
  • Liver / metabolism
  • Mice
  • Microsomes, Liver / metabolism
  • Models, Biological
  • Protein Isoforms
  • Saccharomyces cerevisiae / metabolism
  • Stearoyl-CoA Desaturase / isolation & purification
  • Stearoyl-CoA Desaturase / metabolism*
  • Stearoyl-CoA Desaturase / physiology*
  • Sterol Regulatory Element Binding Protein 1
  • Tissue Distribution
  • Transcription Factors*
  • Triglycerides / metabolism


  • CCAAT-Enhancer-Binding Proteins
  • DNA, Complementary
  • DNA-Binding Proteins
  • Fatty Acids, Unsaturated
  • Protein Isoforms
  • SREBF1 protein, human
  • Srebf1 protein, mouse
  • Sterol Regulatory Element Binding Protein 1
  • Transcription Factors
  • Triglycerides
  • Stearoyl-CoA Desaturase