Stearoyl-CoA desaturase, a short-lived protein of endoplasmic reticulum with multiple control mechanisms
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 lipopro...
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Published in | Prostaglandins, leukotrienes and essential fatty acids Vol. 68; no. 2; pp. 123 - 133 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
Scotland
Elsevier Ltd
01.02.2003
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Subjects | |
Online Access | Get full text |
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Summary: | 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. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-3 content type line 23 ObjectType-Review-1 |
ISSN: | 0952-3278 1532-2823 |
DOI: | 10.1016/S0952-3278(02)00262-4 |