Hydrolysis of Xenobiotic Fatty Acid Esters by Carboxylesterases of Human Skin
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.
KeywordsFatty Acid Ester Cutis Extract Butyl Ester Subcutis Extract Isopropyl Ester
Unable to display preview. Download preview PDF.
- 2.Skerrow, C.J. and Skerrow, D., A survey of methods for the isolation and fractionation of epidermal tissue and cells, in: “Methods in Skin Research’; Skerrow, D. and Skerrow, C.J., eds., John Wiley, Chichester (1985).Google Scholar
- 3.Peterson, G.L., Determination of total protein, Meth. Enzymol. 91: 1983; 95–119.Google Scholar
- 4.Durst, H.D., Milano, M., Kitka, J., Conelly, S.A., and Grushka, E., Phenacyl esters of fatty esters via crown ether catalysts for enhanced UV detection in liquid chromatography, Analyt. Chem. 47: 1975; 1797–1801.Google Scholar
- 5.Borch, R.F., Separation of long chain fatty acids as phenacyl esters by HPLC, Analyt. Chem. 47: 1975; 2437–2439.Google Scholar
- 9.Bergers, M., Verhagen, A.R., Jongerius, M., and Mier, P.D., A new approach to the measurement of phospholipase A2 in tissue homogenates and its application to skin, Biochim. Biophys. Acta 876: 1985; 327–332.Google Scholar
- 10.Bronaugh R.L. and Maibach, H.I., eds., “Percutaneous Absorption”, Marcel Dekker, New York (1985).Google Scholar
- 11.Heymann, E., Carboxylesterases and amidases, in: “Enzymatic Basis of Detoxication”, Vol. II, pp 291–323, Jakoby, W.B., ed., Academic Press, New York (1980).Google Scholar
- 13.Aldridge W.N. and Reiner, E., “Enzyme Inhibitors as Substrates. Interaction of Esterases with Esters of Organophosphorus and Carbamic Acids”, North Holland, Amsterdam (1972).Google Scholar