Abstract
Histidine decarboxylase (HDC, L -histidine carboxylyase, EC 4.1.1.22) catalyses the decarboxylation of L -histidine to histamine. It is the only enzyme that forms histamine (Schayer 1966, 1978). There have been a great number of papers on histamine (including more than ten monographs), but it is only recently that studies on HDC have been carried out at the molecular level (Watanabe and Wada 1983). The enzyme is very labile and the tissue content is extremely low, and it has therefore been difficult to purify (Aures et al. 1970; Aures and HÅkanson 1971). Most interest in HDC has centered on: (a) its inhibitors, which deplete tissues of histamine (Beaven 1982; Kollonitsch 1982) and may be useful clinically or in pharmacological research; and (b) its antibody, which may serve as a probe in the immunohistochemical identification of the histaminergic neurone system in the CNS (Watanabe et al. 1983, 1984; Pollard and Schwartz 1986), since histamine itself, unlike other monoamines, does not give strong, specific fluorescence suitable for its histochemical identification.
Keywords
- Mast Cell
- Histamine Content
- Histidine Decarboxylase
- Dopa Decarboxylase
- Aromatic Amino Acid Decarboxylase
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
The references cited in this review are mainly those published after the previous volume on this topic (Handbook of experimental pharmacology, Vol. 18(II), 1978), which cited references up to 1974. We regret that we have not cited many recent papers owing to limits of space.
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Watanabe, T., Taguchi, Y., Maeyama, K., Wada, H. (1991). Formation of Histamine: Histidine Decarboxylase. In: Uvnäs, B. (eds) Histamine and Histamine Antagonists. Handbook of Experimental Pharmacology, vol 97. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-75840-9_13
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