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Regulation of Fatty Acid Biosynthesis and Lipolysis

Lisa M. Salati

10.1002/cphy.cp070215

Source: Supplement 21: Handbook of Physiology, The Endocrine System, The Endocrine Pancreas and Regulation of Metabolism

Originally published: 2001

Published online: January 2011

Full Article on Wiley Online Library



Abstract

The sections in this article are:

1 Pathways of De Novo Fatty Acid Biosynthesis and Lipolysis
1.1 Regulation in the Pathways for Lipogenesis and Lipolysis
1.2 Cellular Sites of Lipogenesis and Lipolysis
1.3 Isolated Cell Models for the Study of Lipogenesis and Lipolysis
2 Establishing Insulin and Glucagon as Regulators of Lipogenesis and Lipolysis
3 Molecular Mechanisms Involved in the Regulation of Lipogenesis and Lipolysis
3.1 Criteria for Evaluating Putative Regulatory Mechanisms
3.2 Regulated Steps
4 Summary
Figure 1. Figure 1.

Schematic representation of the pathway involved in conversion of glucose to fatty acids. Key reactions of lipogenesis are identified by numbers: 1, glucose‐6‐phosphate dehydrogenase; 2, 6‐phosphogluconate dehydrogenase; 3, malic enzyme; 4, citrate‐transport protein; 5, ATP‐citrate lyase; 6, acetyl‐CoA carboxylase; 7, fatty acid synthase; 8, reactions of chain elongation; 9, stearoyl‐CoA desaturase; 10, acyltransferases.
Figure 2. Figure 2.

Schematic representation of lipolysis in adipose tissue. Phosphorylation of hormone‐sensitive lipase regulates the activity of the first reaction of lipolysis. The P symbolizes phosphate and indicates that this enzyme is active when phosphorylated.
Figure 3. Figure 3.

Model for roles of insulin and glucagon in the regulation of acetyl‐CoA carboxylase. Acetyl‐CoA carboxylase (ACC) is phosphorylated on the indicated serines and converted to a less active form by AMP‐activated protein kinase (AMPK). Residues Ser79 and Ser1200 are phosphorylated by AMPK, which is itself regulated by phosphorylation and dephosphorylation. The (+) and (−) symbols indicate an activating or inhibiting effect, respectively, by insulin or glucagon. Question marks indicate that the mode of action of insulin activation or glucagon inhibition of this step has not been demonstrated definitively.
Figure 4. Figure 4.

Model for regulation of hormone‐sensitive lipase by phosphorylation and dephosphorylation. Phosphorylation of hormone‐sensitive lipase by protein kinase A increases activity of the enzyme. In contrast, phosphorylation by AMP‐activated protein kinase does not change the kinetic properties of hormone‐sensitive lipase but does inhibit further phosphorylation and activation by protein kinase A.


Figure 1.

Schematic representation of the pathway involved in conversion of glucose to fatty acids. Key reactions of lipogenesis are identified by numbers: 1, glucose‐6‐phosphate dehydrogenase; 2, 6‐phosphogluconate dehydrogenase; 3, malic enzyme; 4, citrate‐transport protein; 5, ATP‐citrate lyase; 6, acetyl‐CoA carboxylase; 7, fatty acid synthase; 8, reactions of chain elongation; 9, stearoyl‐CoA desaturase; 10, acyltransferases.



Figure 2.

Schematic representation of lipolysis in adipose tissue. Phosphorylation of hormone‐sensitive lipase regulates the activity of the first reaction of lipolysis. The P symbolizes phosphate and indicates that this enzyme is active when phosphorylated.



Figure 3.

Model for roles of insulin and glucagon in the regulation of acetyl‐CoA carboxylase. Acetyl‐CoA carboxylase (ACC) is phosphorylated on the indicated serines and converted to a less active form by AMP‐activated protein kinase (AMPK). Residues Ser79 and Ser1200 are phosphorylated by AMPK, which is itself regulated by phosphorylation and dephosphorylation. The (+) and (−) symbols indicate an activating or inhibiting effect, respectively, by insulin or glucagon. Question marks indicate that the mode of action of insulin activation or glucagon inhibition of this step has not been demonstrated definitively.



Figure 4.

Model for regulation of hormone‐sensitive lipase by phosphorylation and dephosphorylation. Phosphorylation of hormone‐sensitive lipase by protein kinase A increases activity of the enzyme. In contrast, phosphorylation by AMP‐activated protein kinase does not change the kinetic properties of hormone‐sensitive lipase but does inhibit further phosphorylation and activation by protein kinase A.

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Article Title: Regulation of Fatty Acid Biosynthesis and Lipolysis
 

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Lisa M. Salati. Regulation of Fatty Acid Biosynthesis and Lipolysis. Compr Physiol 2011, Supplement 21: Handbook of Physiology, The Endocrine System, The Endocrine Pancreas and Regulation of Metabolism: 495-527. First published in print 2001. doi: 10.1002/cphy.cp070215