Reduced activity of hepatic microsomal fatty acid chain elongation synthesis in clofibrate-fed rats

1977 ◽  
Vol 26 (15) ◽  
pp. 1401-1404 ◽  
Author(s):  
Clemente Landriscina ◽  
Francesca M. Ruggiero ◽  
Gabriele V. Gnoni ◽  
Ernesto Quagliariello
Keyword(s):  
Fatty Acid ◽  
Chain Elongation ◽  
Fatty Acid Chain ◽  
Reduced Activity

scholarly journals Inhibition of rat liver microsomal fatty acid chain elongation by gemfibrozil in vitro

FEBS Letters ◽  
1992 ◽  
Vol 300 (1) ◽  
pp. 89-92 ◽  
Author(s):  
R.M. Sánchez ◽  
M. Viñals ◽  
M. Alegret ◽  
M. Vázquez ◽  
T. Adzet ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Rat Liver ◽  
Chain Elongation ◽  
Fatty Acid Chain

scholarly journals The synthesis and hydrolysis of long-chain fatty acyl-coenzyme A thioesters by soluble and microsomal fractions from the brain of the developing rat

1976 ◽  
Vol 160 (2) ◽  
pp. 247-251 ◽  
Author(s):  
P J Brophy ◽  
D E Vance
Keyword(s):  
Fatty Acid ◽  
Microsomal Fraction ◽  
Specific Activity ◽  
Arachidic Acid ◽  
Fatty Acyl ◽  
Chain Elongation ◽  
Fatty Acid Chain ◽  
Specific Activities ◽  
Coa Hydrolase ◽  
Long Chain

1. The specific activities of long-chain fatty acid-CoA ligase (EC6.2.1.3) and of long-chain fatty acyl-CoA hydrolase (EC3.1.2.2) were measured in soluble and microsomal fractions from rat brain. 2. In the presence of either palmitic acid or stearic acid, the specific activity of the ligase increased during development; the specific activity of this enzyme with arachidic acid or behenic acid was considerably lower. 3. The specific activities of palmitoyl-CoA hydrolase and of stearoyl-CoA hydrolase in the microsomal fraction decreased markedly (75%) between 6 and 20 days after birth; by contrast, the corresponding specific activities in the soluble fraction showed no decline. 4. Stearoyl-CoA hydrolase in the microsomal fraction is inhibited (99%) by bovine serum albumin; this is in contrast with the microsomal fatty acid-chain-elongation system, which is stimulated 3.9-fold by albumin. Inhibition of stearoyl-CoA hydrolase does not stimulate stearoyl-CoA chain elongation. Therefore it does not appear likely that the decline in the specific activity of hydrolase during myelogenesis is responsible for the increased rate of fatty acid chain elongation. 5. It is suggested that the decline in specific activity of the microsomal hydrolase and to a lesser extent the increase in the specific activity of the ligase is directly related to the increased demand for long-chain acyl-CoA esters during myelogenesis as substrates in the biosynthesis of myelin lipids.

Fibrates modify rat hepatic fatty acid chain elongation and desaturation in vitro

1993 ◽  
Vol 46 (10) ◽  
pp. 1791-1796 ◽  
Author(s):  
Rosa M. Sánchez ◽  
Marisa Viñals ◽  
Marta Alegret ◽  
Manuel Vázquez ◽  
Tomás Adzet ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Chain Elongation ◽  
Hepatic Fatty Acid ◽  
Fatty Acid Chain
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