Lipoprotein Lipase Activity and Common Gene Variants in Severely Hypertriglyceridemic Patients with and without Diabetes

2003 ◽  
Vol 60 (2) ◽  
pp. 61-67 ◽  
Author(s):  
Rita Chadarevian ◽  
Luc Foubert ◽  
Isabel Beucler ◽  
Marie-Laure Kottler ◽  
Alain Raisonnier ◽  
...  
Keyword(s):  
Lipoprotein Lipase ◽  
Lipase Activity ◽  
Gene Variants ◽  
Lipoprotein Lipase Activity ◽  
Common Gene

scholarly journals Retention of glucose by N-linked oligosaccharide chains impedes expression of lipoprotein lipase activity: effect of castanospermine.

1992 ◽  
Vol 33 (9) ◽  
pp. 1343-1349
Author(s):  
H Masuno ◽  
EJ Blanchette-Mackie ◽  
CJ Schultz ◽  
AE Spaeth ◽  
RO Scow ◽  
...  
Keyword(s):  
Lipoprotein Lipase ◽  
Lipase Activity ◽  
Lipoprotein Lipase Activity ◽  
Activity Effect

scholarly journals Post-translational regulation of lipoprotein lipase activity in adipose tissue

1978 ◽  
Vol 176 (3) ◽  
pp. 865-872 ◽  
Author(s):  
P Ashby ◽  
D P Bennett ◽  
I M Spencer ◽  
D S Robinson
Keyword(s):  
Adipose Tissue ◽  
Lipoprotein Lipase ◽  
Lipase Activity ◽  
Translational Regulation ◽  
Progressive Increase ◽  
Lipoprotein Lipase Activity ◽  
Dependent Part ◽  
Adipose Tissue Lipoprotein Lipase ◽  
Energy Dependent

Changes in adipose-tissue lipoprotein lipase activity that are independent of protein synthesis were investigated in an incubation system in vitro. Under appropriate conditions at 25 degrees C a progressive increase in the enzyme activity occurs that is energy-dependent. Part of the enzyme is rapidly inactivated when the tissue is incubated with adrenaline or adrenaline plus theophylline. The mechanism of this inactivation appears to be distinct from, and to follow, the activation of the enzyme. A hypothesis is presented to account for the results in terms of an activation of the enzyme during obligatory post-translational processing and a catecholamine-regulated inactivation of the enzyme as an alternative to secretion from the adipocyte.

Lipoprotein lipase-suppressing mediator in serum of endotoxin-treated rats

1986 ◽  
Vol 251 (4) ◽  
pp. E470-E476 ◽  
Author(s):  
G. J. Bagby ◽  
C. B. Corll ◽  
J. J. Thompson ◽  
L. A. Wilson
Keyword(s):  
Lipoprotein Lipase ◽  
Exposure Time ◽  
Lipase Activity ◽  
Significant Suppression ◽  
Lipoprotein Lipase Activity ◽  
Activity Maximum ◽  
A Cell

The conditions under which lipoprotein lipase-suppressing mediator is present in serum of endotoxin-treated rats was determined in this study. The suppression of lipoprotein lipase activity in 3T3-L1 cells was used as a bioassay for mediator in serum. Endotoxin (0.1-10 micrograms/ml) and serum from control rats did not suppress lipoprotein lipase activity. Maximum suppression of cell lipoprotein lipase activity (70%) by serum from endotoxic rats required a cell exposure time of 5 h. At the highest dose of endotoxin used (1 mg/100 g), significant suppression was achieved when cells were incubated with 0.5% serum from endotoxic rats (P less than 0.05). Serum obtained 2-3 h after endotoxin injection possessed the maximal ability to suppress lipase activity, but suppressing activity was not present in serum collected 8 h after endotoxin. Rats rendered tolerant to endotoxin by 5 daily injections (0.1 mg/100 g) did not contain detectable levels of mediator in serum after endotoxin injection. The results demonstrate that the presence of lipoprotein lipase activity-suppressing mediator is transitory after in vivo exposure of naive rats to endotoxin, but does not appear in serum of endotoxin tolerant rats.

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