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ENZYMATIC HISTAMINE DEGRADATION BY HUMAN SKIN
Author(s) -
FRANCIS D.,
GREAVES M.W.,
YAMAMOTO S.
Publication year - 1977
Publication title -
british journal of pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.432
H-Index - 211
eISSN - 1476-5381
pISSN - 0007-1188
DOI - 10.1111/j.1476-5381.1977.tb07538.x
Subject(s) - histamine , diamine oxidase , histamine n methyltransferase , enzyme , dermis , human skin , chemistry , enzyme assay , biochemistry , amine oxidase (copper containing) , transferase , in vitro , endocrinology , biology , histamine h2 receptor , anatomy , receptor , genetics , antagonist
1 Degradation of histamine by homogenized human skin in vitro , in the presence of the cofactor S‐adenosyl methionine, indicates the presence of the histamine metabolizing enzyme histamine‐ N ‐methyl transferase in human skin. Under the experimental conditions described, no significant histamine degradation by diamine oxidase was observed. 2 The enzyme activity is temperature‐sensitive with an optimum at 37°C. The enzyme is stable in intact excised skin at −20°C, but unstable in homogenized skin at this temperature. 3 Little or no enzyme activity is present in mid‐ or deep dermis, but the distribution of the enzyme between superficial papillary dermis and epidermis is uncertain. 4 The presence of a potent histamine degrading mechanism raises the possibility that histamine‐ N ‐methyl transferase activity may be an important modulating factor in histamine‐mediated skin disorders