Chemical modulation of glycerolipid signaling and metabolic pathways.
Thirty years ago, glycerolipids captured the attention of biochemical researchers as novel cellular signaling entities. We now recognize that these biomolecules occupy signaling nodes critical to a number of physiological and pathological processes. Thus, glycerolipid-metabolizing enzymes present attractive targets for new therapies. A number of fields-ranging from neuroscience and cancer to diabetes and obesity-have elucidated the signaling properties of glycerolipids. The biochemical literature teems with newly emerging small molecule inhibitors capable of manipulating glycerolipid metabolism and signaling. This ever-expanding pool of chemical modulators appears daunting to those interested in exploiting glycerolipid-signaling pathways in their model system of choice. This review distills the current body of literature surrounding glycerolipid metabolism into a more approachable format, facilitating the application of small molecule inhibitors to novel systems. This article is part of a Special Issue entitled Tools to study lipid functions.
Department of Pharmacology, Vanderbilt University Medical Center, Nashville, TN 37232, USA.
Sarah A
SA
Scott
Department of Pharmacology, Vanderbilt University Medical Center, Nashville, TN 37232, USA; Vanderbilt Center for Neuroscience Drug Discovery, Vanderbilt University Medical Center, Nashville, TN 37232, USA.
Thomas P
TP
Mathews
Department of Pharmacology, Vanderbilt University Medical Center, Nashville, TN 37232, USA.
Pavlina T
PT
Ivanova
Department of Pharmacology, Vanderbilt University Medical Center, Nashville, TN 37232, USA; Vanderbilt Center for Neuroscience Drug Discovery, Vanderbilt University Medical Center, Nashville, TN 37232, USA; Department of Chemistry, Vanderbilt University, Nashville, TN 37235, USA; Vanderbilt Institute of Chemical Biology, Vanderbilt University, Nashville, TN 37235, USA.
Craig W
CW
Lindsley
Department of Pharmacology, Vanderbilt University Medical Center, Nashville, TN 37232, USA; Department of Biochemistry, Vanderbilt University Medical Center, Nashville, TN 37232, USA; Vanderbilt Institute of Chemical Biology, Vanderbilt University, Nashville, TN 37235, USA. Electronic address: alex.brown@vanderbilt.edu.
H Alex
HA
Brown
D000217:Acyltransferases / Q000378:metabolism; D005990:Glycerol / Q000737:chemistry; D008049:Lipase / Q000378:metabolism; D008055:Lipids / Q000737:chemistry / Q000502:physiology*; D010740:Phospholipases / Q000378:metabolism; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism; D010770:Phosphotransferases / Q000378:metabolism; D015398:Signal Transduction
D008055:Lipids; D000217:Acyltransferases; D010770:Phosphotransferases; D010740:Phospholipases; D008049:Lipase; D010744:Phosphoric Monoester Hydrolases; D005990:Glycerol
Autotaxin; Fatty acyltransferase; Glycerolipid; Inhibitor; Lipase; Lipid kinase; Lipin; Metabolism; Phospholipase