Inhibition of myocardial lipase by palmityl CoA

McDonough, Kathleen H.; Neely, James R.

doi:10.1016/0022-2828(88)90330-6

Cited by 16 publications

(3 citation statements)

References 29 publications

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“…Furthermore, the stimulatory effect in islets is not via HSL; whereas the inhibitory effect in adipocytes occurs at least partly via inhibition of HSL. This latter finding is consistent with previous reports, which indicate that LC-CoA inhibits partially purified adipocyte HSL activity (18,27,39).…”

Section: Resultssupporting

confidence: 83%

“…Of relevance to lipolysis, previous studies document that 25 mol/l palmitoylCoA (Pal-CoA) and 40 mol/l oleoyl-CoA inactivate lipase activity half-maximally in pigeon adipose tissue, whereas 100 mol/l Pal-CoA reduces lipase activity by 90% (39). Perfusion of rat hearts with 100 and 200 mol/l Pal-CoA reduces lipase activity by 17 and 67%, respectively (27). HSL from bovine perirenal adipose tissue is inhibited 50% by 0.1 mol/l oleoylCoA (18).…”

mentioning

confidence: 99%

“…Insulin inhibits HSL through phosphodiesterase-3-dependent cAMP degradation (16,20). It has also been proposed that long-chain acyl-CoA esters (LC-CoA) may have a role in regulating lipases (18,27,39) and, in particular, adipocyte HSL activity (18,39).…”

mentioning

confidence: 99%

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Regulation of lipolytic activity by long-chain acyl-coenzyme A in islets and adipocytes

Hu¹,

Deeney²,

Nolan³

et al. 2005

American Journal of Physiology-Endocrinology and Metabolism

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Intracellular lipolysis is a major pathway of lipid metabolism that has roles, not only in the provision of free fatty acids as energy substrate, but also in intracellular signal transduction. The latter is likely to be particularly important in the regulation of insulin secretion from islet β-cells. The mechanisms by which lipolysis is regulated in different tissues is, therefore, of considerable interest. Here, the effects of long-chain acyl-CoA esters (LC-CoA) on lipase activity in islets and adipocytes were compared. Palmitoyl-CoA (Pal-CoA, 1–10 μM) stimulated lipase activity in islets from both normal and hormone-sensitive lipase (HSL)-null mice and in phosphatase-treated islets, indicating that the stimulatory effect was neither on HSL nor phosphorylation dependent. In contrast, we reproduced the previously published observations showing inhibition of HSL activity by LC-CoA in adipocytes. The inhibitory effect of LC-CoA on adipocyte HSL was dependent on phosphorylation and enhanced by acyl-CoA-binding protein (ACBP). In contrast, the stimulatory effect on islet lipase activity was blocked by ACBP, presumably due to binding and sequestration of LC-CoA. These data suggest the following intertissue relationship between islets and adipocytes with respect to fatty acid metabolism, LC-CoA signaling, and lipolysis. Elevated LC-CoA in islets stimulates lipolysis to generate a signal to increase insulin secretion, whereas elevated LC-CoA in adipocytes inhibits lipolysis. Together, these opposite actions of LC-CoA lower circulating fat by inhibiting its release from adipocytes and promoting fat storage via insulin action.

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Section: Resultssupporting

confidence: 83%

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confidence: 99%