Abstract
Acylases catalyze the hydrolysis of a range ofS-substitutedN-acetyl-l-cysteines. The hydrolysis ofN-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 ofN-acetyl-l-cysteine and several haloalkene-derived mercapturates have been recently identified: acylase I catalyzes the deacetylation ofN-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.
Footnotes
-
Send reprint requests to: M. W. Anders, Dept. of Pharmacology and Physiology, University of Rochester Medical Center, 601 Elmwood Ave., Box 711, Rochester, NY 14642. E-mail:mw_anders{at}urmc.rochester.edu
-
↵1 Present address: Astra Arcus USA, Worcester, MA 01605.
-
This research was supported by National Institute of Environmental Health Sciences Grants ES03127 (M.W.A.) and ES01247 (R.B.B.).
- Abbreviations used are::
- NAC
- N-acetyl-l-cysteine
- β-lyase
- cysteine conjugate β-lyase
- PBS-X
- phosphate-buffered saline containing Triton X-100
- Received September 27, 1999.
- Accepted February 17, 2000.
- The American Society for Pharmacology and Experimental Therapeutics
DMD articles become freely available 12 months after publication, and remain freely available for 5 years.Non-open access articles that fall outside this five year window are available only to institutional subscribers and current ASPET members, or through the article purchase feature at the bottom of the page.
|