Histaminase (diamine oxidase) activity in human tumors: an expression of a mature genome.

Publisher Website
Google Scholar
Abstract
High histaminase [amine:oxygen oxidoreductase (deaminating)(pyridoxal-containing), EC 1.4.3.6] activity is found in certain human tumors and in the placenta of most mammals. The present study explores the relationship of tumor histaminase to histaminases found in placenta and other human, pig and rat tissues. The electrophoretic mobility and Km for the deamination of histamine and putrescine were identical for histaminases from human placenta and medullary thyroid carcinoma. An antibody was raised in rabbits against human placental histaminase that was highly purified by a new affinity procedure. In separate studies, using inhibitory concentrations of antibody and a 2nd antibody precinitation technique, identical patterns of immunoreactivity were found for histaminases from human placenta, kidney, medullary thyroid carcinoma and small cell lung carcinoma. Human intestinal histaminase cross reacted well but less strongly than enzymes from these other tissues. Histaminases from pig kidney, pig intestine and rat intestine showed no cross reaction. Histaminases from rat thymus and adrenal gland showed minimal cross reactivity. The findings suggest that placental histaminase activity is not a unique product of a fetal or trophoblastic genome. The presence of histaminase in malignancies does not appear to be an example of ectopic tumor production of a placental trophoblastic protein.