Effect of Pitressin on lipolysis and on phosphorylase activity in rat adipose tissue

1964 ◽  
Vol 207 (5) ◽  
pp. 1166-1168 ◽  
Author(s):  
Martha Vaughan
Keyword(s):  
Hormone Sensitive Lipase ◽  
Prostaglandin E ◽  
Glycerol Release ◽  
Similar Concentration ◽  
Phosphorylase Activity ◽  
Hormone Sensitive ◽  
Rat Adipose Tissue ◽  
Release Of Glycerol ◽  
Synthetic Oxytocin

Pitressin, a mixture of arginine and lysine vasopressins, stimulates the release of glycerol and of free fatty acids from rat epididymal fat pads in vitro. This effect is inhibited by prostaglandin E1, which has previously been shown to interfere with the analogous effects of catecholamines, ACTH, TSH, and glucagon. Like these latter hormones, Pitressin, added for a few minutes after tissues have been incubated in the absence of hormones, significantly increases the activity of phosphorylase and of the hormone-sensitive lipase. (The activity of both of these enzymes declines during the period of incubation before the hormone is added.) No effects of synthetic oxytocin at similar concentration on glycerol release or on phosphorylase activity were demonstrated.

scholarly journals Amber Extract Reduces Lipid Content in Mature 3T3-L1 Adipocytes by Activating the Lipolysis Pathway

Molecules ◽  
2021 ◽  
Vol 26 (15) ◽  
pp. 4630
Author(s):  
Erica Sogo ◽  
Siqi Zhou ◽  
Haruna Haeiwa ◽  
Reiko Takeda ◽  
Kazuma Okazaki ◽  
...  
Keyword(s):  
Glucose Uptake ◽  
Lipid Droplets ◽  
Hormone Sensitive Lipase ◽  
Physiological Effects ◽  
Glycerol Release ◽  
Rosin Acids ◽  
Genes Encoding ◽  
Triglyceride Content ◽  
Hormone Sensitive ◽  
Release Of Glycerol

Amber—the fossilized resin of trees—is rich in terpenoids and rosin acids. The physiological effects, such as antipyretic, sedative, and anti-inflammatory, were used in traditional medicine. This study aims to clarify the physiological effects of amber extract on lipid metabolism in mouse 3T3-L1 cells. Mature adipocytes are used to evaluate the effect of amber extract on lipolysis by measuring the triglyceride content, glucose uptake, glycerol release, and lipolysis-related gene expression. Our results show that the amount of triacylglycerol, which is stored in lipid droplets in mature adipocytes, decreases following 96 h of treatment with different concentrations of amber extract. Amber extract treatment also decreases glucose uptake and increases the release of glycerol from the cells. Moreover, amber extract increases the expression of lipolysis-related genes encoding perilipin and hormone-sensitive lipase (HSL) and promotes the activity of HSL (by increasing HSL phosphorylation). Amber extract treatment also regulates the expression of other adipocytokines in mature adipocytes, such as adiponectin and leptin. Overall, our results indicate that amber extract increases the expression of lipolysis-related genes to induce lipolysis in 3T3-L1 cells, highlighting its potential for treating various obesity-related diseases.

scholarly journals Hormone-sensitive lipase of rat adipose tissue. Purification and some properties.

1981 ◽  
Vol 256 (12) ◽  
pp. 6311-6320
Author(s):  
G. Fredrikson ◽  
P. Strålfors ◽  
N.O. Nilsson ◽  
P. Belfrage
Keyword(s):  
Adipose Tissue ◽  
Hormone Sensitive Lipase ◽  
Hormone Sensitive ◽  
Rat Adipose Tissue

Molecular mechanisms regulating hormone-sensitive lipase and lipolysis

2003 ◽  
Vol 31 (6) ◽  
pp. 1120-1124 ◽  
Author(s):  
C. Holm
Keyword(s):  
Lipid Droplet ◽  
Molecular Mechanisms ◽  
Hormone Sensitive Lipase ◽  
Glucose Disposal ◽  
Triacylglycerol Lipase ◽  
Insulin Resistant ◽  
Lipolytic Action ◽  
Key Enzyme ◽  
Hormone Sensitive

HSL (hormone-sensitive lipase) is a key enzyme in the mobilization of fatty acids from acylglycerols in adipocytes as well as non-adipocytes. In adipocytes, catecholamines stimulate lipolysis mainly through PKA (protein kinase A)-mediated phosphorylation of HSL and perilipin, a protein coating the lipid droplet. The anti-lipolytic action of insulin is mediated mainly via lowered cAMP levels, accomplished through activation of phosphodiesterase 3B. Phosphorylation of HSL by PKA occurs at three sites, the serines 563, 659 and 660, both in vitro and in primary rat adipocytes. Phosphorylation of Ser-659 and -660 is required for in vitro activation as well as translocation from the cytosol to the lipid droplet, whereas the role of the third PKA site remains elusive. Adipocytes isolated from homozygous HSL-null mice, generated in our laboratory, exhibit completely blunted catecholamine-induced glycerol release and reduced fatty acid release, suggesting the presence of additional, although not necessarily hormone-activatable, triacylglycerol lipase(s). Basal hyperinsulinaemia, release of exaggerated amounts of insulin during glucose challenges and retarded glucose disposal during insulin tolerance tests suggest that HSL-null mice are insulin resistant. Liver, adipose tissue and skeletal muscle appear all to be sites of impaired insulin sensitivity in HSL-null mice.

scholarly journals Growth Hormone and Dexamethasone Stimulate Lipolysis and Activate Adenylyl Cyclase in Rat Adipocytes by Selectively Shifting Giα2 to Lower Density Membrane Fractions*

Endocrinology ◽  
1999 ◽  
Vol 140 (3) ◽  
pp. 1219-1227 ◽  
Author(s):  
Rupert Guk-Chor Yip ◽  
H. Maurice Goodman
Keyword(s):  
Adenylyl Cyclase ◽  
Active Form ◽  
Competitive Inhibitor ◽  
Hormone Sensitive Lipase ◽  
Western Analysis ◽  
Tissue Extracts ◽  
Dense Membrane ◽  
Hormone Sensitive ◽  
A Chain ◽  
Rat Adipose Tissue

Abstract GH, in the presence of glucocorticoid, produces a delayed increase in lipolysis in rat adipose tissue, but the biochemical mechanisms that account for this action have not been established. Other lipolytic agents rapidly activate adenylyl cyclase (AC) and the resulting production of cAMP initiates a chain of reactions that culminates in the activation of hormone-sensitive lipase. We compared responses of segments of rat epididymal fat or isolated adipocytes to 30 ng/ml GH and 0.1 μg/ml dexamethasone (Dex) with 0.1 ng/ml isoproterenol (ISO), which evoked a similar increase in lipolysis. All measurements were made during the fourth hour after the addition of GH+Dex or immediately after the addition of ISO to cells or tissues that had been preincubated for 3 h without hormone. Although no significant increases in cAMP were discernible in homogenates of GH+Dex-treated tissues, RP-cAMPS (RP-adenosine 3′5′-phosphothioate), a competitive inhibitor of cAMP, was equally effective in decreasing lipolysis induced by GH+Dex or ISO. The proportion of PKA that was present in the active form was determined by measuring the incorporation of 32P from[γ -32P]ATP into kemptide in the absence and presence of saturating amounts of cAMP. GH+Dex and ISO produced similar increases in protein kinase A activity in tissue extracts. Treatment with GH+Dex did not change the total forskolin-stimulated AC present in either a crude membrane pellet sedimented at 16K × g or a less dense membrane pellet sedimented at 100K × g, but doubled the AC activity in the 16K pellet when assayed in the absence of forskolin. To evaluate possible effects on G proteins, pellets obtained from centrifugation of adipocyte homogenates at 16K × g and 100K × g were solubilized and subjected to PAGE and Western analysis. GH+Dex decreased Giα2 by 44% (P < 0.02) in the 16K pellets and increased it by 52% (P < 0.01) in the 100K pellets. Gsα in the 16K pellet was unaffected by GH+Dex and was decreased (P < 0.05) in the 100K pellet. Sucrose density fractionation of the 16K pellets revealed a similar GH+Dex-dependent shift of Giα2 to less dense fractions as determined by both Western analysis and[ 32P]NAD ribosylation catalyzed by pertussis toxin. No such changes were seen in the distribution of Gsα or 5′-nucleotidase. Colchicine (100 μm) blocked the GH+Dex-dependent shift of Giα2 from the 16K to the 100K pellet and blocked the lipolytic effects of GH+Dex, but not those of ISO. We conclude that by modifying the relationship between AC and Giα2, GH+Dex relieves some inhibition of cAMP production and consequently increases lipolysis.

In vitro SAR of (5-(2H)-isoxazolonyl) ureas, potent inhibitors of hormone-sensitive lipase

2004 ◽  
Vol 14 (12) ◽  
pp. 3155-3159 ◽  
Author(s):  
Derek B. Lowe ◽  
Steven Magnuson ◽  
Ning Qi ◽  
Ann-Marie Campbell ◽  
James Cook ◽  
...  
Keyword(s):  
Hormone Sensitive Lipase ◽  
Hormone Sensitive

scholarly journals Crotonis Fructusand Its Constituent, Croton Oil, Stimulate Lipolysis in OP9 Adipocytes

2014 ◽  
Vol 2014 ◽  
pp. 1-5
Author(s):  
Mi-Seong Kim ◽  
Ha-Rim Kim ◽  
Hong-Seob So ◽  
Young-Rae Lee ◽  
Hyoung-Chul Moon ◽  
...  
Keyword(s):  
Positive Control ◽  
Hormone Sensitive Lipase ◽  
Dependent Manner ◽  
Glycerol Release ◽  
Croton Oil ◽  
Croton Tiglium ◽  
Hormone Sensitive ◽  
Main Component ◽  
Culture Supernatants ◽  
Dose Dependent

Introduction. Crotonis fructus (CF) is the mature fruit ofCroton tigliumL. and has been used for the treatment of gastrointestinal disturbance in Asia. It is well known that the main component of CF is croton oil (CO). The present study is to investigate the effects of CF extracts (CFE) and CO on lipolysis in OP9 adipocytes.Methods. Glycerol release to the culture supernatants was used as a marker of adipocyte lipolysis.Results. Treatment with various concentrations of CFE and CO stimulates glycerol release in a dose-dependent manner. The increase in glycerol release by CFE is more potent than isoproterenol, which is aβ-adrenergic agonist as a positive control in our system. The increased lipolysis by CFE and CO was accompanied by an increase of phosphorylated hormone sensitive lipase (pHSL) but not nonphosphorylated HSL protein and mRNA. Pretreatment with H89, which is a protein kinase A inhibitor, significantly abolished the CFE- and CO-induced glycerol release in OP9 adipocytes. These results suggest that CFE and CO may be a candidate for the development of a lipolysis-stimulating agent in adipocytes.

Sign in / Sign up

Export Citation Format

Share Document