Immunohistochemical localization of acyl-CoA hydrolase/thioesterase multigene family members to rat epithelia

Histochemistry and Cell Biology
Yu KuramochiJ Yamada

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 mainly in organs closely related to fatty acid oxidation, of which kidney contained the highest levels of both enzymes. Immunohistochemistry localized the enzymes primarily in the proximal tubules, where a large energy demand is expected and fatty acids represent a major fuel, correlating well with the intrarenal distribution of peroxisomal beta-oxidation. In situ hybridization suggested colocalization of CTE-I and MTE-I in the kidney. The immunoreactivity was also found in various epithelial tissues in the body, including Harderian gland and sebaceous gland. These results demonstrated the distribution of CTE-I and MTE-I in a wide variety of rat tissues, primarily characterized by an epithelial localization, being consistent w...Continue Reading

Citations

Feb 7, 2013·Histochemistry and Cell Biology·Takayuki OhtomoJunji Yamada
Nov 21, 2007·Journal of Mammary Gland Biology and Neoplasia·Michael C RudolphSteven M Anderson
May 18, 2010·Progress in Lipid Research·Brenda KirkbyJade K Forwood
Mar 8, 2008·Molecular Reproduction and Development·Kazuyuki HiratsukaJunji Yamada
Nov 26, 2010·Biochemical and Biophysical Research Communications·Atsushi MomoseJunji Yamada
Dec 17, 2002·Histochemistry and Cell Biology·Esther Asan
Feb 4, 2006·Archives of Biochemistry and Biophysics·Mitsuhiro TakagiJunji Yamada

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