TCDD (2,3,7,8-tetrachlorodibenzo-p-dioxin) reduces lipoprotein lipase activity in the adipose tissue of the guinea pig

1984 ◽  
Vol 122 (2) ◽  
pp. 810-817 ◽  
Author(s):  
David W. Brewster ◽  
Fumio Matsumura
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

1973 ◽  
Vol 132 (3) ◽  
pp. 633-635 ◽  
Author(s):  
P. de Gasquet ◽  
E. Péquignot ◽  
D. Lemonnier ◽  
A. Alexiu

The lipoprotein lipase activity per adipocyte was increased in the genetically obese rat (fa/fa). However, there was no difference between obese and lean animals when the enzyme activities were related to adipocyte surface area. The possible implications of the findings are discussed.


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