Hormone-Sensitive Lipase (HSL)

Hormone-sensitive lipase (HSL) is an intracellular neutral lipase that is capable of hydrolyzing triacylglycerols, diacylglycerols, monoacylglycerols, and cholesteryl esters, as well as other lipid and water-soluble substrates. HSL is highly expressed in adipose tissue and steroidogenic tissues, with lower amounts found in cardiac and skeletal muscle, macrophages, and pancreatic islets. HSL contains two main domains: the N-terminal domain and the C-terminal domain. The C-terminal portion forms an α/β hydrolase structure and contains the catalytic triad: Ser-423, Asp-703, and His-733. In normal physiology, HSL affects adipocyte lipolysis, steroidogenesis, spermatogenesis, and possibly insulin secretion and insulin action. Abnormal expression or genetic variations of HSL are associated with human disorders such as obesity, insulin resistance, type 2 diabetes, and hyperlipidemia^[1][2].

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