REGULATION OF ADIPOSE TISSUE LIPOLYSIS. PURIFICATION AND PROPERTIES OF HORMONE-SENSITIVE LIPASE

1981 ◽  
Vol 9 (2) ◽  
pp. 237P-237P
Author(s):  
Gudrun Fredrikson ◽  
Staffan Nilsson ◽  
Per Belfrage
Keyword(s):  
Adipose Tissue ◽  
Hormone Sensitive Lipase ◽  
Purification And Properties ◽  
Hormone Sensitive ◽  
Adipose Tissue Lipolysis

scholarly journals The contribution of hormone sensitive lipase to adipose tissue lipolysis and its regulation by insulin in periparturient dairy cows

2018 ◽  
Vol 8 (1) ◽  
Author(s):  
Jenne De Koster ◽  
Rahul K. Nelli ◽  
Clarissa Strieder-Barboza ◽  
Jonas de Souza ◽  
Adam L. Lock ◽  
...  
Keyword(s):  
Adipose Tissue ◽  
Dairy Cows ◽  
Hormone Sensitive Lipase ◽  
Hormone Sensitive ◽  
Adipose Tissue Lipolysis

scholarly journals The presence and role of hormone-sensitive lipase in heart muscle

1989 ◽  
Vol 258 (1) ◽  
pp. 67-72 ◽  
Author(s):  
C A Small ◽  
A J Garton ◽  
S J Yeaman
Keyword(s):  
Adipose Tissue ◽  
Heart Muscle ◽  
Lipolytic Activity ◽  
Hormone Sensitive Lipase ◽  
Energy Store ◽  
Dependent Protein ◽  
Hormone Sensitive ◽  
Rat Myocytes ◽  
Adipose Tissue Lipolysis

Hormone-sensitive lipase (HSL) catalyses the initial, rate-limiting, reaction in adipose-tissue lipolysis. Hormone-stimulated lipolytic activity has also been observed in the heart, where endogenous triacylglycerol is the major energy store. However, the identity of the intracellular lipase responsible has yet to be established. We have partially purified a neutral lipase from bovine heart muscle and compared its properties with those of HSL from bovine adipose tissue. The heart lipase has the same subunit Mr as HSL, is immunoprecipitated by antiserum raised against purified HSL and is phosphorylated by cyclic AMP-dependent protein kinase, apparently at the same site as HSL (as judged by h.p.l.c. of tryptic phosphopeptides). Phosphorylation of the heart lipase was found to result in increased enzyme activity, demonstrating the lipase's potential to respond to hormonal stimuli. The heart lipase was shown to be present in myocytes by its immunoprecipitation from homogenates of rat myocytes by anti-HSL antiserum. These findings are consistent with the conclusion that HSL is responsible for intracellular lipolysis in heart.

scholarly journals An Epistatic Interaction between Pnpla2 and Lipe Reveals New Pathways of Adipose Tissue Lipolysis

Cells ◽  
2019 ◽  
Vol 8 (5) ◽  
pp. 395 ◽  
Author(s):  
Xiao Zhang ◽  
Cong Cong Zhang ◽  
Hao Yang ◽  
Krishnakant G. Soni ◽  
Shu Pei Wang ◽  
...  
Keyword(s):  
Adipose Tissue ◽  
Epistatic Interaction ◽  
Hydrolase Activity ◽  
Hormone Sensitive Lipase ◽  
Adipose Triglyceride Lipase ◽  
Monoglyceride Lipase ◽  
Genetic Deficiency ◽  
Hormone Sensitive ◽  
Adipose Tissue Lipolysis ◽  
Hydrolysis Of

White adipose tissue (WAT) lipolysis contributes to energy balance during fasting. Lipolysis can proceed by the sequential hydrolysis of triglycerides (TGs) by adipose triglyceride lipase (ATGL), then of diacylglycerols (DGs) by hormone-sensitive lipase (HSL). We showed that the combined genetic deficiency of ATGL and HSL in mouse adipose tissue produces a striking different phenotype from that of isolated ATGL deficiency, inconsistent with the linear model of lipolysis. We hypothesized that the mechanism might be functional redundancy between ATGL and HSL. To test this, the TG hydrolase activity of HSL was measured in WAT. HSL showed TG hydrolase activity. Then, to test ATGL for activity towards DGs, radiolabeled DGs were incubated with HSL-deficient lipid droplet fractions. The content of TG increased, suggesting DG-to-TG synthesis rather than DG hydrolysis. TG synthesis was abolished by a specific ATGL inhibitor, suggesting that ATGL functions as a transacylase when HSL is deficient, transferring an acyl group from one DG to another, forming a TG plus a monoglyceride (MG) that could be hydrolyzed by monoglyceride lipase. These results reveal a previously unknown physiological redundancy between ATGL and HSL, a mechanism for the epistatic interaction between Pnpla2 and Lipe. It provides an alternative lipolytic pathway, potentially important in patients with deficient lipolysis.

scholarly journals Regulation of adipose tissue lipolysis: phosphorylation of hormone-sensitive lipase in intact rat adipocytes

FEBS Letters ◽  
1980 ◽  
Vol 111 (1) ◽  
pp. 120-124 ◽  
Author(s):  
Per Belfrage ◽  
Gudrun Fredrikson ◽  
Nils Östen Nilsson ◽  
Peter Strålfors
Keyword(s):  
Adipose Tissue ◽  
Hormone Sensitive Lipase ◽  
Rat Adipocytes ◽  
Hormone Sensitive ◽  
Adipose Tissue Lipolysis
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