Comparative study of lipoprotein lipase in white and brown fat of rat (Rattus norvegicus)

Author(s):  
Daniel Guerrier ◽  
Helene Pellet
1993 ◽  
Vol 21 (3) ◽  
pp. 310S-310S ◽  
Author(s):  
RACHEL M. HOWARD ◽  
KAREN A. ORFALI ◽  
MARY C. SUGDEN

1966 ◽  
Vol 14 (5) ◽  
pp. 385-395 ◽  
Author(s):  
C. W. M. ADAMS ◽  
Y. H. ABDULLA ◽  
O. B. BAYLISS ◽  
R. O. WELLER

A histochemical method for triglyceride esters is described that depends on hydrolysis of triglycerides to fatty acids by pancreatic lipase, precipitation of the released fatty acid as calcium soap and formation of lead sulphide by the conventional Gomori technique. The specificity of the lipase for triglyceride was investigated by chromatography and activation-inhibition studies. The enzyme preparation used hydrolyzed triglycerides and waxes but did not split cholesterol esters or phosphoglycerides. Positive histochemical reactions were obtained with this pancreatic lipase method in medium sized and fine lipid droplets in frozen sections. Positive reactions were observed in rat brown fat; in various adipose tissues in man, rabbit and rat; in the spermatogonia of rat testis; in human epidermis and sebaceous glands; in solitary unidentified adrenocortical cells in man and rat; in human fatty liver and in fine droplets in senile human myocardium. A slight variable reaction was obtained in human atherosclerotic plaques. The reaction of brown fat was also investigated with the electron microscope. No triglyceride was demonstrated in unfixed tissue sectons when an active preparation of lipoprotein lipase was used in place of pancreatic lipase. This failure was probably due to diffusion of lipoprotein from unfixed sections. Lipoprotein lipase is inactive against serum lipoproteins fixed with formaldehyde or glutaraldehyde.


1989 ◽  
Vol 257 (5) ◽  
pp. R1123-R1127 ◽  
Author(s):  
M. Klingenspor ◽  
S. Klaus ◽  
H. Wiesinger ◽  
G. Heldmaier

Activation of lipoprotein lipase (LPL) in brown fat of the Djungarian hamster ensures substrate supply for nonshivering thermogenesis. Cold acclimation [5 degrees C ambient temperature (Ta)] in long photoperiod [light-dark (LD) 16:8] increased brown fat LPL activity from 4.7 to 22.7 nmol oleate.mg-1.min-1 within 1 day. Slight reduction of this high LPL activity was observed during prolonged cold exposure for up to 4 wk. Deacclimation (transfer from 5 to 23 degrees C Ta) caused total inactivation of brown fat LPL within 4 days. Short photoperiod (LD 8:16) also stimulates brown fat LPL activity. Its effect can be summarized by three different observations. At thermoneutrality short photoperiod elevated LPL activity to 7.1 instead of 4.7 nmol.mg-1.min-1 observed in long photoperiod. Second, at low ambient temperature short photoperiod reinforces the effect of cold acclimation. Maximum LPL activity of cold-exposed Djungarian hamsters averaged 23.7 nmol.mg-1.min-1 in long photoperiod and was elevated to 35.5 nmol.mg-1.min-1 in short photoperiod. Third, inactivation of LPL during deacclimation was delayed in short photoperiod. These results demonstrate that photoperiod as well as ambient temperature may be cooperatively used as environmental cues for seasonal acclimation of brown fat substrate supply for nonshivering thermogenesis.


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