hormone-sensitive lipase

Only the initial enzyme is affected by hormones, hence its hormone-sensitive lipase name.

Ketosis is absent because the presence of some insulin inhibits hormone-sensitive lipase (lipolysis).

Hence the name "hormone-sensitive lipase".

ASP is also known for its augmentation of glucose transport and inhibiting action on hormone-sensitive lipase.

Hormone-sensitive lipase, a protein found in the cytosol of adipocytes important in the hydrolysis of triacylglycerols.

When blood sugar is low, decreasing insulin levels signal the adipocytes to activate hormone-sensitive lipase, and to convert triglycerides into free fatty acids.

Lower levels of cAMP decrease the activity of protein kinase A to phosphorylate, thereby activating, hormone-sensitive lipase.

As a consequence, cAMP activates protein kinase A, which phosphorylates (and activates) hormone-sensitive lipase.

Upon release of insulin from the pancreas, white adipose cells' insulin receptors cause a dephosphorylation cascade that lead to the inactivation of hormone-sensitive lipase.

When the body requires fatty acids as an energy source, the hormone glucagon signals the breakdown of the triglycerides by hormone-sensitive lipase to release free fatty acids.

It has long been held that hormone-sensitive lipase (HSL) is the enzyme that hydrolyses triacylglycerides to free fatty acids from fats (lipolysis).

Although PKA also phosphorylates hormone-sensitive lipase, which can increase its activity, the more than 50-fold increase in fat mobilization (triggered by epinephrine) is primarily due to perilipin phosphorylation.

Monoacylglycerol lipase functions together with hormone-sensitive lipase (LIPE) to hydrolyze intracellular triglyceride stores in adipocytes and other cells to fatty acids and glycerol.

Perilipin acts as a protective coating from the body's natural lipases, such as hormone-sensitive lipase, which break triglycerides into glycerol and free fatty acids for use in metabolism, a process called lipolysis.

Increases intracellular cGMP levels that induce the phosphorylation of a hormone-sensitive lipase and perilipin A via the activation of a cGMP-dependent protein kinase-I (cGK-I)

Xanthines such as caffeine, theobromine, and thyroid hormone are phosphodiesterase inhibitors (enhance lipolysis as inhibition of phosphodiesterase enzyme, thereby preserving cAMP, also activating kinase enzyme, which phosphorylates hormone-sensitive lipase and activates lipolysis).

Induction of the ß-oxidation pathway with a concomitant decrease in FA synthesis by fibrates results in a lower availability of FAs for triglyceride synthesis, a process that is amplified by the inhibition of hormone-sensitive lipase in adipose tissue by fibrates.

However, when hormones such as epinepherine are secreted, or when insulin levels drop in response to low blood glucose levels, this triggers an intracellular secondary messenger cascade that phosphorylates hormone-sensitive lipase to break triglycerides into glycerol and free fatty acids for use in metabolism, a process called lipolysis.

MiR-143 has also been experimentally shown to regulate genes that are crucial for adipocyte differentiation, (including GLUT4, Hormone-sensitive lipase, the fatty acid-binding protein, aP2 and PPAR-γ2), demonstrating that miRNAs are also involved in fat metabolism and endocrine function in humans.