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Activities of adipose triglyceride lipase (ATGL (show PNPLA2 Proteins)), hormone sensitive lipolitic enzyme (HSL) and monoacylglycerol lipase (MGL (show MGLL Proteins)) were significantly higher (51 %, 38 %, 49 %) in the DE group than the HF group (p < 0.05). MGL (show CLEC10A Proteins), there were no differences between the CO group, HF group, and DC group, with the DE group (70 %) being significantly higher (p < 0.05).
Results clearly indicate that SF-1 (show SF1 Proteins) is involved in the regulation of LIPE expression after activation of protein kinase A in adrenocortical cells.
A role for HSL in kidney lipolysis:fasting up-regulates HSL levels and phosphorylation in mouse kidney.
Data suggest that cardiotrophin-1 (show CTF1 Proteins) up-regulates lipolysis in white adipocytes via 1) induction of perilipin (show PLIN1 Proteins), 2) activation of HSL (via phosphorylation by PKA), and 3) inactivation of adipose triglyceride lipase (show PNPLA2 Proteins) (via up-regulation of inhibitor G0S2 (show G0S2 Proteins)).
QRFP-43 attenuates lipolysis by preventing the formation of an active complex between perilipin A (show PLIN1 Proteins), caveolin-1 (show CAV1 Proteins), the catalytic subunit of protein kinase (show CDK7 Proteins) and hormone-sensitive lipase on lipid droplets.
PRIP (show NCOA6 Proteins) promotes the translocation of phosphatases to lipid droplets to trigger the dephosphorylation of HSL and perilipin A (show PLIN1 Proteins), thus reducing PKA-mediated lipolysis.
Whereas the catalytic function of HSL is necessary for spermatogenesis in mice, the presence of the N-terminal testis-specific (show AIF1 Proteins) fragment is not essential.
Changes in fatty acid metabolism observed in testes from HSL-knockout male mice may underlie the infertility observed in these animals.
HSL acts to drive cAMP/PKA-mediated regulation of StAR expression and steroidogenesis in mouse Leydig cells.
High-fat diet strongly reduced HSL phosphorylation at Ser660 in mouse skeletal muscle.
Despite reductions in intramyocellular lipolysis and HSL expression, overexpression of HSL did not rescue defects in insulin (show INS Proteins) action in skeletal myotubes from obese type 2 diabetic subjects.
Identification of a homozygous nonsense variant p.Ala507fsTer563 in hormone sensitive lipase as the likely cause of the lipodystrophy phenotype in siblings.
These findings indicate the physiological significance of HSL in adipocyte function and the regulation of systemic lipid and glucose homeostasis and underscore the severe metabolic consequences of impaired lipolysis.
Serum triglyceride was significantly up-regulated in men with the (CG + GG) genotype of HSL promoter polymorphism.
M. leprae suppresses lipid degradation through inhibition of HSL expression.
Enzyme promiscuity in the hormone-sensitive lipase family of proteins.
Resveratrol increased adipose triglyceride lipase (show PNPLA2 Proteins) gene and protein expressions, an effect that was not observed for hormone-sensitive lipase in human SGBS (show GPC3 Proteins) adipocytes.
LIPE C-60G variation can inhibit the decrease of LDL-C and the increases of HDL (show HSD11B1 Proteins)-C and apo A (show APOA Proteins)-I in young healthy males, and can inhibit the decrease of LDL-C and the increase of insulin (show INS Proteins) in young healthy females induced by a high-carbohydrate diet.
suggests that genetic variation of HSL may be a risk factor for male infertility
Data show that hormone-sensitive lipase activity is reduced in adipose tissue of patients with and without diabetes, while lipoprotein lipase (show LPL Proteins) activity is reduces only in patients with diabetes.
Polymorphisms in HSL might be one of important genetic factors that influence carcass yield and meat quality in beef cattle.
These results suggest that HSL was regulated by fatty acids and some hormones in mammary epithelial cells and thereby play an important role of lipid and energy metabolism.
The protein encoded by this gene has a long and a short form, generated by use of alternative translational start codons. 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.
, hormone-sensitive lipase
, hormone-sensitive lipase-like
, hormone - sensitive lipase testicular isoform
, lipase E
, hormone-sensitive lipase testicular isoform