Abstract
Human skin contains carboxylesterases capable of degrading amphiphilic xenobiotic esters. Most of these activities are found in the subcutaneous fat tissue and are of the serine hydrolase type, but activation experiments with Ca2+ point to a possible involvement of epidermal phospholipase A2 in the hydrolysis of myristoyl esters and especially of sorbitan trioleate. Fatty acid ethyl and propyl esters, and 4hydroxy-benzoic acid esters are degraded both in the epidermis and in the subcutis. With simple fatty acid esters an extract from stratum granulosum/stratum corneum exhibits optimal activity with an acyl chain length of 14, whereas the optimum is at shorter acyl residues with the other skin compartments.
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© 1994 Springer Science+Business Media New York
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Heymann, E., Noetzel, F., Retzlaff, R., Schnetgöke, G., Westie, S. (1994). Hydrolysis of Xenobiotic Fatty Acid Esters by Carboxylesterases of Human Skin. In: Mackness, M.I., Clerc, M. (eds) Esterases, Lipases, and Phospholipases. NATO ASI Series, vol 266. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-0993-0_8
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DOI: https://doi.org/10.1007/978-1-4899-0993-0_8
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