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Hormone-sensitive lipase

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Hormone-sensitive lipase

Lipase, hormone-sensitive
Identifiers
3.1.1.79
RNA expression pattern
Hormone-sensitive lipase (HSL) N-terminus
Identifiers
Symbol HSL_N
Pfam InterPro IPR010468

Hormone-sensitive lipase (

HSL is an intracellular neutral lipase that is capable of hydrolyzing a variety of esters.[3] The enzyme has a long and a short form. The long form is expressed in steroidogenic tissues such as testis, where it converts cholesteryl esters to free cholesterol for steroid hormone production. The short form is expressed in adipose tissue, among others, where it hydrolyzes stored triglycerides to free fatty acids.[4]

Nomenclature

During fasting-state the increased free fatty acid secretion by adipocyte cells was attributed to epinephrine hormone. Hence the name "hormone-sensitive lipase".[5] Other hormones like catecholamines, adrenocorticotropic hormone (ACTH), and glucagon can also stimulate such responses. Such enzymatic action plays a key role in providing major source of energy for most cells.

Function

The main function of hormone-sensitive lipase is to mobilize the stored fats.

HSL is activated when the body needs to mobilize energy stores, and so responds positively to catecholamines, ACTH. It is inhibited by insulin. Previously, glucagon was thought to activate HSL, however the removal of insulin's inhibitory effects ("cutting the brakes") is the source of activation. The lipolytic effect of glucagon in adipose tissue is minimal in humans.

Another important role is the release of cholesterol from cholesterol esters for use in the production of steroids.[8]

Activation

It may be activated by two mechanisms.[9]

  • In the first, phosphorylated perilipin A causes it to move to the surface of the lipid droplet, where it may begin hydrolyzing the lipid droplet.

References


Further reading

External links

  • Medical Subject Headings (MeSH)


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