Long-chain acyl-CoA thioesterases (EC 3.1.2.2 ) are found in all organisms and cleave fatty acyl-CoAs into free fatty
acids and CoA. Isoforms are present in several cellular compartments, and there are membrane-bound and soluble
forms of the enzyme. In liver, the enzyme activity is induced in the cytosol and mitochondria by peroxisome
proliferators.
General function
Metabolism, Enzyme, Hydrolase
Comment
Cellular localization
Cytoplasmic, Mitochondrial
Comment
Ovarian function
Unknown
Comment
Expression regulated by
Comment
Ovarian localization
Luteal cells
Comment
This gene was found in a rat ovarian cDNA library (Unigene)
Follicle stages
Corpus luteum
Comment
The expression of cytosolic and mitochondrial type II acyl-CoA thioesterases is upregulated in the porcine corpus luteum during pregnancy.
Bostrom M, et a .
Acyl-CoA thioesterases hydrolyze acyl-CoAs to free fatty acids and CoASH, thereby regulating fatty acid metabolism. This activity is catalyzed by numerous structurally related and unrelated enzymes, of which several acyl-CoA thioesterases have been shown to be regulated via the peroxisome proliferator-activated receptor alpha, strongly linking them to fatty acid metabolism. Two protein families have recently been characterized, the type I acyl-CoA thioesterase gene family and the type II protein family, which are expressed in cytosol, mitochondria and peroxisomes. Still, only little is known about regulation of their expression and precise functions in vivo. In the present study, we have investigated the activity and expression of acyl-CoA thioesterase in the porcine ovary during different phases of the estrus cycle. The activity was low in homogenates obtained during the immature and follicular phases, increasing nearly 4-fold during the luteal phase, with the highest activity being found in the pregnant corpus luteum (about 7-fold higher than in immature follicles). The increase in homogenate activity in corpus luteum from pregnant pigs was due to a moderate increase in the cytosolic activity, and an approximately 20-25-fold increase in the mitochondrial fraction. Western blot analysis showed no detectable expression of the type I acyl-CoA thioesterases (CTE-I and MTE-I) and revealed that the increased activity in cytosol and mitochondria is due to increased expression of the type II acyl-CoA thioesterases (CTE-II and MTE-II). This apparent hormonal regulation of expression of the type II acyl-CoA thioesterase may provide new insights into the functions of these enzymes in the mammalian ovary.