Lipid transport in the hypothyroid rat as reflected by the serum concentrations of free fatty acids, lipoproteins, lecithin-cholesterol acyltransferase and lipoprotein lipase activity in adipose tissue

1981 ◽  
Vol 4 (1) ◽  
pp. 75-80 ◽  
Author(s):  
Urban Rosenqvist ◽  
R. Mahler ◽  
L. A. Carlson
1978 ◽  
Vol 172 (2) ◽  
pp. 319-325 ◽  
Author(s):  
A Cryer ◽  
H M Jones

The lipoprotein lipase (clearing-factor lipase) activity of the white adipose tissue from rats aged between 1 and 145 days was determined. Five adipose-tissue sites (epididymal, uterine, subcutaneous, perirenal and intramuscular) together with serum concentrations of triacylglycerol, cholesterol and glucose were studied. The pattern of enzyme-activity change was remarkably similar in all the sites studied, although the growth of the tissues proceeded non-uniformly. After a peak of activity early in suckling, lipoprotein lipase activity fell to low values by 20 days of age. At weaning (21 days) the activity increased sharply and within 5 days high values were regained. The serum triacylglycerol and cholesterol concentrations were low at birth and reached peaks of concentration coincidentally with the minima of white-adipose-tissue lipoprotein lipase activities, seen late in suckling. The changes in enzyme activity were related to other metabolic changes in adipose tissue and with the known changes in plasma insulin concentrations occurring during development.


1978 ◽  
Vol 176 (3) ◽  
pp. 865-872 ◽  
Author(s):  
P Ashby ◽  
D P Bennett ◽  
I M Spencer ◽  
D S Robinson

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.


1993 ◽  
Vol 16 (1) ◽  
pp. 6-10 ◽  
Author(s):  
Hiroshi UEKI ◽  
Yusuke OHKURA ◽  
Toshio MOTOYASHIKI ◽  
Nobuaki TOMINAGA ◽  
Tetsuo MORITA

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