Immunolocalization of semicarbazide-sensitive amine oxidase in human dental pulp and its activity towards serotonin
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Published on: September 23, 2015
M O'Sullivan1, K F Tipton, W E McDevitt
1Department of Restorative Dentistry and Periodontology, School of Dental Science, Trinity College, Dublin 2, Ireland.
Abstract:
The semicarbazide-sensitive amine oxidase (EC 1.4.3.6; SSAO) from crude homogenates of human dental pulp was shown to catalyse the oxidative deamination of 5-hydroxytryptamine (serotonin; 5-HT) with a K(m) of 318+/-52 microM. In this respect the human enzyme resembles that in pig dental pulp, but differs from SSAO in all other tissues studied, which are inactive towards 5-HT. A method is described for obtaining intact dental pulp in which the anatomical details are preserved. Extracted teeth are frozen in dry ice and later defrosted rapidly before being fractured in a mechanical vice, facilitating pulp removal. Immunohistochemistry showed SSAO in the odontoblast layer, nerve fibres and blood vessels. The presence of SSAO in nerves in dental pulp appears to be unique. Tryptophan hydroxylase, a key enzyme in 5-HT synthesis, was also demonstrated in nerves and the odontoblast layer of human dental pulp.