Diamine oxidase and cadaverine metabolism.
نویسندگان
چکیده
We have recently presented evidence that diamine oxidase is rcsponsiblc for a portion of the metabolism of histamine in several species (1, 2). This evidence is largely based on the alteration of histamine metabolism produced by compounds which are known to inhibit diamine oxidase in vitro. The inhibitors used were isonicotinylhydrazine (3) and aminoguanidine. The latter is reported to be the most powerful inhibitor in vitro known (4). In order to investigate further this apparent inhibition of diamine oxidase in viva, it seemed desirable to use as a substrate some compound with a structure suggesting metabolism by diamine oxidase only. The compound selected was cadaverine (1,5-diamino-n-pentane). Cadaverine is the most frequently used substrate for diamine oxidase in vitro and is reported to be the compound most readily attacked by diamine oxidase (5). We have prepared cadaverine labeled with radioactive carbon and have shown that it is largely metabolized by diamine oxidase in mice and rats. The action of aminoguanidine and isonicotinylhydrazine in preventing the destruction of cadaverine parallels their effect on histamine metabolism. This provides further evidence that diamine oxidase is one of the enzymes involved in histamine metabolism in rats and mice.
منابع مشابه
Spermidine oxidase in human pregnancy serum
Diamine oxidase was previously measured in human pregnancy serum with putrescine or histamine as substrate. We have now documented the presence of spermidine oxidase activity in pregnancy serum by means of a specific radioactive assay with l '4Clspermidine as substrate and Dowex 50 cation-exchange chromatography to separate products from substrate. The apparent Km of a partially purified prepar...
متن کاملPathological changes in platelet histamine oxidases in atopic eczema
Increased plasma histamine levels were associated with significantly lowered diamine and type B monoamine oxidase activities in platelet-rich plasma of atopic eczema (AE) patients. The diamine oxidase has almost normal cofactor levels (pyridoxal phosphate and Cu(2+)) but the cofactor levels for type B monoamine oxidase (flavin adenine dinucleotide and Fe(2+)) are lowered. The biogenic amines pu...
متن کاملCell-Free Synthesis of the Alkaloids Ammodendrine and Smipine
The bipiperidyl alkaloid ammodendrine was detected in 28 plant species as a minor alkaloid besides quinolizidine alkaloids. Cadaverine serves as a precursor for both quinolizidine alkaloids and for ammodendrine, since labelled cadaverine is incorporated into both rings of amm oden drine. Cell-free extracts of Lupinus arboreus and of Pisum sativum, which contain an active diamine oxidase form a...
متن کاملCadaverine, an Essential Diamine for the Normal Root Development of Germinating Soybean (Glycine max) Seeds.
When the polyamine content of soybean (Glycine max) seeds was examined during the early stages of germination, the major polyamine in the cotyledons was found to be spermidine, followed by spermine; while very low concentrations of cadaverine were found. In the embryonic axes, however, cadaverine was the main polyamine and its content markedly increased 24 hours after the start of germination. ...
متن کاملRole of diamine oxidase during the treatment of tumour-bearing mice with combinations of polyamine anti-metabolites.
Treatment of mice bearing L1210 leukaemia with 2-difluoromethylornithine, a specific inhibitor of ornithine decarboxylase (EC 4.1.1.17), produced a profound depletion of putrescine and spermidine in the tumour cells. Sequential combination of methylglyoxal bis(guanylhydrazone), an inhibitor of adenosylmethionine decarboxylase (EC 4.1.1.50), with difluoromethylornithine largely reversed the poly...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 206 1 شماره
صفحات -
تاریخ انتشار 1954