Immunohistochemical Localization of the Acylases that Catalyze the Deacetylation of N-Acetyl-l-cysteine and Haloalkene-Derived Mercapturates

Acylases catalyze the hydrolysis of a range of S -substituted N -acetyl- l -cysteines. The hydrolysis of N -acetyl- l -cysteine is catalyzed by cytosolic acylase I, and activity is present in human endothelial cells and rat lung, intestinal, and liver homogenates. Many haloalkenes are metabolized to...

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Published inDrug metabolism and disposition Vol. 28; no. 6; pp. 625 - 632
Main Authors Uttamsingh, V, Baggs, R B, Krenitsky, D M, Anders, M W
Format Journal Article
LanguageEnglish
Published United States American Society for Pharmacology and Experimental Therapeutics 01.06.2000
Subjects
Acetylation
Acetylcysteine - chemistry
Acetylcysteine - metabolism
Alkenes - chemistry
Alkenes - metabolism
Amidohydrolases - analysis
Amidohydrolases - metabolism
Animals
Humans
Immunohistochemistry
Kidney - chemistry
Kidney - enzymology
Kidney - metabolism
Male
Rats
Rats, Inbred F344
Sulfonium Compounds - metabolism
Tissue Distribution
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Summary:Acylases catalyze the hydrolysis of a range of S -substituted N -acetyl- l -cysteines. The hydrolysis of N -acetyl- l -cysteine is catalyzed by cytosolic acylase I, and activity is present in human endothelial cells and rat lung, intestinal, and liver homogenates. Many haloalkenes are metabolized to mercapturates, which also undergo acylase-catalyzed hydrolysis. The acylases that catalyze the deacetylation of N -acetyl- l -cysteine and several haloalkene-derived mercapturates have been recently identified: acylase I catalyzes the deacetylation of N -acetyl- l -cysteine and some haloalkene-derived mercapturates whereas an acylase purified from rat kidney cytosol catalyzes the deacetylation of a distinct set of substrates, including several haloalkene-derived mercapturates. The objective of these studies was to examine the tissue and subcellular localization of acylase I and purified rat kidney acylase. Immunoblotting showed the presence of immunoreactive acylase I and purified rat kidney acylase in rat kidney, liver, lung, and brain. Both acylases were identified by immunohistochemistry in several rat organs, including kidney, liver, lung, brain, stomach, intestines, adrenals, pancreas, and testis, indicating that acylase activity is widespread in rat tissues.
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ISSN:0090-9556
1521-009X