2002
DOI: 10.1007/s00418-002-0381-7
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Immunohistochemical localization of acyl-CoA hydrolase/thioesterase multigene family members to rat epithelia

Abstract: Acyl-CoA hydrolases cleave acyl-CoA thioesters to free fatty acids and coenzyme A. The potency of these enzymes may serve to modulate cellular levels of acyl-CoAs to affect various cellular functions, including lipid metabolism. In this study, we investigated the tissue distribution of this multigene family of enzymes, focusing on cytosolic (CTE-I) and mitochondrial acyl-CoA thioesterases (MTE-I) in adult rats, using an anti-CTE-I antibody which recognizes both the isoforms. Western blotting detected them main… Show more

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Cited by 14 publications
(1 citation statement)
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“…The acyl-CoA thioesterase 2 (Acot2), also known as MTE-I, PTE2 and ARTISt/p43 [20], is a member of the acyl-CoA thioesterase (Acots) family [21]. It is highly expressed in the mammalian kidney, heart, liver, brain, brown adipose tissue, skeletal muscles and steroid tissues [23,24,25]. In the rodent model of the diet-induced obesity, and compared with the low-fat diet group, the expression of the Acot2 protein in the heart and soleus muscle of the rats that were fed with high-fat diet increased by 2.0 and 7.6 times, respectively [26].…”
Section: Introductionmentioning
confidence: 99%
“…The acyl-CoA thioesterase 2 (Acot2), also known as MTE-I, PTE2 and ARTISt/p43 [20], is a member of the acyl-CoA thioesterase (Acots) family [21]. It is highly expressed in the mammalian kidney, heart, liver, brain, brown adipose tissue, skeletal muscles and steroid tissues [23,24,25]. In the rodent model of the diet-induced obesity, and compared with the low-fat diet group, the expression of the Acot2 protein in the heart and soleus muscle of the rats that were fed with high-fat diet increased by 2.0 and 7.6 times, respectively [26].…”
Section: Introductionmentioning
confidence: 99%