The Lipoprotein Lipase (Clearing-Factor Lipase) Activity of Bovine Subcutaneous Adipose Tissue and Isolated Adipocytes

1978 ◽  
Vol 6 (3) ◽  
pp. 596-598 ◽  
Author(s):  
HEDWIG A. K. PLAAS ◽  
RICHARD HARWOOD ◽  
ANTHONY CRYER
1974 ◽  
Vol 47 (6) ◽  
pp. 631-634
Author(s):  
B. Persson

1. In 126 normotriglyceridaemic and in seventy-three hypertriglyceridaemic subjects there was a similar seasonal variation of adipose tissue lipoprotein lipase activity, the lowest activity being noted during the summer months. 2. There was no seasonal variation of the serum triglyceride or free fatty acid concentrations in the normotriglyceridaemic group. 3. In the same group the highest blood acetoacetate concentration was noted in March–April, the lowest in November–December. 4. There was no seasonal variation of the blood glucose concentration for women, but for men the lowest concentration was noted in July–August.


1976 ◽  
Vol 50 (4) ◽  
pp. 315-318
Author(s):  
Y. Giudicelli ◽  
R. Pecquery ◽  
B. Agli ◽  
C. Jamin ◽  
J. Quevauvilliers

1. Lipoprotein lipase activity and hormone-sensitive lipase activity were investigated in subcutaneous lipomas removed from two patients and compared with the enzyme activities in subcutaneous adipose tissue from two normal subjects. 2. Confirmation was obtained of the presence of lipoprotein lipase activity in lipomas with an activity fifteen to forty-five times that in the two control samples. 3. Hormone-sensitive lipase activity was demonstrated in lipomas under basal conditions of assay as well as in the presence of adrenaline plus theophylline. However, compared with the non-lipomatous fat samples, these activities were lower, as was the magnitude of the lipolytic response to adrenaline plus theophylline. 4. The significance of these measurements of enzyme activity and their role in the pathogenesis of lipomas are briefly discussed.


2007 ◽  
Vol 293 (4) ◽  
pp. E958-E964 ◽  
Author(s):  
Gregory R. Steinberg ◽  
Bruce E. Kemp ◽  
Matthew J. Watt

We have investigated the gene and protein expression of adipose triglyceride lipase (ATGL) and triglyceride (TG) lipase activity from subcutaneous and visceral adipose tissue of lean and obese subjects. Visceral and subcutaneous adipose tissue was obtained from 16 age-matched lean and obese subjects during abdominal surgery. Tissues were analyzed for mRNA expression of lipolytic enzymes by real-time quantitative PCR. ATGL protein content was assessed by Western blot and TG lipase activity by radiometric assessment. Subcutaneous and visceral adipose tissue of obese subjects had elevated mRNA expression of PNPLA2 (ATGL) and other lipases including PNPLA3, PNPLA4, CES1, and LYPLAL1 ( P < 0.05). Surprisingly, ATGL protein expression and TG lipase activity were reduced in subcutaneous adipose tissue of obese subjects. Immunoprecipitation of ATGL reduced total TG lipase activity in adipose lysates by 70% in obese and 83% in lean subjects. No significant differences in the ATGL activator CGI-58 mRNA levels ( ABHD5) were associated with obesity. These data demonstrate that ATGL is important for efficient TG lipase activity in humans. They also demonstrate reduced ATGL protein expression and TG lipase activity despite increased mRNA expression of ATGL and other novel lipolytic enzymes in obesity. The lack of correlation between ATGL protein content and in vitro TG lipase activity indicates that small decrements in ATGL protein expression are not responsible for the reduction in TG lipase activity observed here in obesity, and that posttranslational modifications may be important.


2004 ◽  
Vol 286 (1) ◽  
pp. E8-E13 ◽  
Author(s):  
Jens M. Bruun ◽  
Aina S. Lihn ◽  
Atul K. Madan ◽  
Steen B. Pedersen ◽  
Kirsten M. Schiøtt ◽  
...  

IL-8 is released from human adipose tissue. Circulating IL-8 is increased in obese compared with lean subjects and is associated with measures of insulin resistance, development of atherosclerosis, and cardiovascular disease. We studied 1) the production and release of IL-8 in vitro from paired samples of subcutaneous (SAT) and visceral (VAT) adipose tissue and 2) the production of IL-8 from whole adipose tissue, isolated adipocytes, and nonfat cells of adipose tissue. IL-8 release from VAT was fourfold higher than from SAT ( P < 0.05), and IL-8 mRNA was twofold higher in VAT compared with SAT ( P < 0.01). Dexamethasone (50 nM) attenuated IL-8 production by 50% ( P < 0.05), and IL-1β (2 μg/l) increased IL-8 production up to 15-fold ( P < 0.001). IL-8 release from whole SAT explants correlated with body mass index (BMI; r = 0.78; P < 0.001), as did IL-8 release from nonfat cells ( r = 0.79; P < 0.001). However, no correlation was found between IL-8 release from the fraction of isolated adipocytes and BMI ( r = 0.01). In conclusion, we demonstrated an increased release of IL-8 from VAT compared with SAT. Furthermore, our data suggest that the observed elevation in circulating levels of IL-8 in obese subjects is due primarily to the release of IL-8 from nonfat cells from adipose tissue. The high levels of IL-8 release from human adipose tissue and accumulation of this tissue in obese subjects may account for some of the increase in circulating IL-8 observed in obesity.


1996 ◽  
Vol 270 (4) ◽  
pp. E718-E722 ◽  
Author(s):  
S. W. Coppack ◽  
T. J. Yost ◽  
R. M. Fisher ◽  
R. H. Eckel ◽  
J. M. Miles

An assay for plasma lipoprotein lipase activity was used without prior injection of heparin to study arteriovenous differences of lipases across skeletal muscle and adipose tissue of normal male volunteers. Lipoprotein lipase (LPL) and hepatic triglyceride lipase (HTGL) activities and triglyceride?concentrations were measured in arterial plasma and in venous effluent plasma from forearm skeletal muscle and subcutaneous abdominal adipose tissue, in the postabsorptive state and after a mixed meal. Triglyceride clearance by the tissues was greater across adipose tissue than across muscle. There were no arteriovenous differences for HTGL activity. In the postabsorptive state skeletal muscle released LPL activity, but adipose tissue did not. Postprandially the arterial LPL and HTGL activities did not change. LPL activity in adipose tissue venous effluent rose, whereas that in muscle venous effluent decreased. These results show that the release of LPL from subcutaneous adipose and forearm tissues is regulated differently, reflecting in vivo differences in LPL regulation at the tissue level.


1988 ◽  
Vol 47 (2) ◽  
pp. 263-270 ◽  
Author(s):  
P. A. Sinnett-Smith ◽  
J. A. Woolliams

ABSTRACTAdipocyte volume rates of fatty acid synthesis, acylglycerol glycerol synthesis and lipolysis (basal and noradrenaline stimulated) along with the activities of acetyl CoA carboxylase and lipoprotein lipase were determined in subcutaneous adipose tissue, sampled by biopsy, from the rump of four breeds of sheep differing in growth and body characteristics.Significant differences among breeds were observed for adipocyte volume, fatty acid synthesis, stimulated lipolysis rates, initial and total acetyl CoA carboxylase activity and lipoprotein lipase activity, but not for acylglycerol glycerol synthesis.Differences in adipocyte volume did not appear to be related to the previously reported carcass fatnesses of the breeds. Similarly differences in adipocyte volume were not related to differences in either de novo fatty acid synthesis or lipolysis rates. Across breeds there was a trend toward higher acylglycerol glycerol synthesis rates associated with greater adipocyte volume although the source of fatty acids for esterification varied greatly.Breed variation in fatness in sheep therefore appears to be a consequence of different balances of anabolic and catabolic processes in adipose tissue, with a unique pattern for each breed. Further elucidation of these patterns may lead to the identification of key sites for genetic manipulation. In addition these breed differences provide an alternative, complementary and qualitatively different, model for the study of the control of fat metabolism to that provided by nutritional or hormonal manipulations.


Sign in / Sign up

Export Citation Format

Share Document