Serotonin and β-phenylethylamine deamination by semicarbazide-sensitive amine oxidase from Callista chione hepatopancreas

Amine oxidase activity against 5-HT and PEA has been studied in hepatopancreas homogenates of Callista chione (Mollusca, Bivalvia). Specific activity values were 3 pmoles/mg protein/min and 0.05 nmoles/mg protein/min with 5-HT and PEA, respectively. Values of activities measured with the two substrates were differently affected by variations of pH (6.5–8) and temperature (17°C–67°C). Monoamine osidase inhibitors such as clorgyline and deprenyl used at a concentration of 10¹⁴ M did not significantly affect 5-HT and PEA deamination. Semicarbazide 10⁴ M completely inhibited deamination of both substrates indicating that, at least under the experimental conditions adopted, 5-HT and PEA were deaminated by a semicarbazide-sensitive amine oxidase.     

Changes in monoamine oxidase activity by mitochondria isolated from late embryos of Bufo bufo

1. Monoamine oxidase activity has been assayed in mitochondria isolated from post-neural embryos (stages 14-25) of Bufo bufo, using 5-HT and PEA as substrates. 2. Mitochondria isolated from stages 19 to 25 show an increasing ability in deaminating monoamines, PEA being metabolized at a higher level with respect to 5-HT. 3. At all the examined stages 5-HT is metabolized by an enzyme corresponding to MAO A, while PEA, from stage 19, is largely deaminated by a semicarbazide-sensitive amine oxidase (SSAO). 4. The effect of Triton X-100 on MAO A activity appears remarkably different in mitochondria isolated from embryos at stages 14 and 25 respectively.     

Specificity of endogenous substrates for types A and B monoamine oxidase in rat striatum

Abstract: Studies were designed to evaluate specificity of the transmitter amines serotonin (5-hydroxytryptamine, 5-HT) and dopamine (DA), as well as the trace amines p -tyramine ( p -TA) and β -phenylethylamine (PEA) for types A and B monoamine oxidase (MAO) in rat striatum. 5-HT was found to be a specific substrate for the type A enzyme. However, the specificity of PEA for the type B enzyme was found to be concentration-dependent. When low concentrations of PEA and 5-HT were used to measure type B and type A activities, respectively, both clorgyline and deprenyl were highly selective for the sensitive form of MAO in vivo. However, as the concentration of PEA was increased, the type B inhibitor deprenyl became less effective in preventing deamination of PEA. Conversely, the type A inhibitor clorgyline became more effective in this regard. Kinetic analysis following selective in vivo inhibition showed PEA deamination by both forms of MAO with a 13-fold greater affinity for the type B enzyme. In vivo dose-response curves obtained with the common substrates DA and p -TA showed approximately 20% deamination by the B enzyme. Kinetic values for DA and p -TA deamination in in vivo -treated tissue possessing only type A or type B MAO activity, revealed a 2.5-fold greater affinity for the type A enzyme. These studies show the importance of concentration on substrate specificity in striatal tissue. The results obtained characterize the common substrate properties of DA and p -TA as well as of PEA in rat striatum. In addition, the presence of regional specificity for 5-HT deamination by only type A MAO is demonstrated.     

Inhibition of rabbit monoamine oxidase by doxepin and related drugs.

The psychotherapeutic agent, doxepin, inhibits both the B and A forms of rabbit lung mitochondrial monoamine oxidase (MAO). The K_i values for doxepin inhibition of phenylethylamine (PEA) and 5-hydroxytryptamine (5-HT) deamination is 3 × 10⁻⁵ and 2 × 10⁻⁴M, respectively. Doxepin is, thus, similar to other tricyclic antidepressant drugs in that it has a greater affinity for the B form of the rabbit oxidase. The ability of doxepin and imipramine and its mono and didesmethyl derivatives to inhibit rabbit MAO is decreased as the pH is raised above 8.0. However, results suggest that the basicity of the propylamine side chain has little or no influence on the ability of these drugs to inhibit the rabbit oxidase. In addition, it is demonstrated that 7 × 10⁻⁶M doxepin inhibits PEA deamination by human platelet MAO approximately 50%.     

Monoamine oxidase and semicarbazide sensitive amine oxidase activities in toad liver mitochondria

1. The deamination of 5-HT and PEA has been assayed by a radiochemical method in mitochondria isolated from toad liver. 2. Time courses of 5-HT and PEA deamination indicate that when PEA is used as the substrate, higher specific activities are obtained. 3. 5-HT is deaminated by MAO A and partially by a SSAO-like enzyme. 4. PEA is deaminated exclusively by SSAO and, MAO B activity, at least under the adopted experimental conditions, is not detectable.     

Mitochondrial monoamine oxidase activity during preneural developmental stages of Bufo bufo

Monoamine oxidase specific activities against PEA and 5-HT have been measured in mitochondria isolated from early embryos of Bufo bufo. During the early development up to the neural fold stage, MAO activity undergoes a continuous decrease that is more evident when PEA is used as the substrate. The inhibition patterns of deprenyl and clorgyline demonstrate that, at the neural fold stage, both type A and B MAO are present. Both in eggs and embryos MAO type A activity appears slightly more sensitive to the inhibitory effect of various concentrations (0.1-2 M) of the denaturing agent urea.     

Monoamine Oxidase Activities in Catfish (Parasilurus Asotus) Tissues

Abstract

The substrate- and inhibitor-related characteristics of monoamine oxidase (MAO) were studied for catfish brain and liver. The kinetic constants for MAO in both tissues were determined using 5-hydroxytryptamine (5-HT), tyramine and β-phenylethylamine (PEA) as substrates. For both tissues, the V_max values were highest with 5-HT and lowest with PEA. The K_m value for the brain was highest with 5-HT, followed by tyramine and PEA; but for the liver its value was highest with PEA, followed by 5-HT and tyramine, although all values were in the same order of magnitude. The inhibition of MAO by clorgyline and deprenyl by use of 5-HT, tyramine and PEA as substrates showed that the MAO-A inhibitor clorgyline was more effective than the MAO-B inhibitor deprenyl for both catfish tissues; a single form was present since inhibition by clorgyline or deprenyl with 1000 μM PEA showed single phase sigmoid curves. It is concluded that catfish brain and liver contain a single form of MAO, relatively similar to mammalian MAO-A.     

Antagonism between long acting Monoamine Oxidase Inhibitors (MAOI) and MD780515, a new specific and reversible MAOI

The inhibition of type A and B monoamine oxidase (MAO A and B) in rat brain, liver and heart by MD780515, 3-[4-(3 cyanophenylmethoxy) phenyl]-5-(methoxymethyl)-2-oxazolidinone, has been investigated ex vivo with 5-hydroxytryptamine (5-HT) and β-phenylethylamine (PEA) as substrates. MAO A was strongly inhibited for four hours after oral administration of 10 mg/kg MD780515 (maximum inhibition : 72%, 86% and 83% in brain, liver and heart respectively. In contrast, in heart where PEA is deaminated by type A MAO, the predominant form of MAO in that tissue, the inhibition was 68% 30 minutes after administration of the compound. In all cases, MAO activities reached control values 24 hours after drug administration (10 mg/kg), whereas some inhibitory activity was still present 24 hours after oral administration of higher doses. The strong MAO A inhibition (68 to 83%) remaining in the three tissues 24 hours after oral administration of clorgyline (5 mg/kg) was completely removed by pretreatment with MD780515 (10 mg/kg). In the same conditions, MD780515 protected against the inhibition (53%) by clorgyline of PEA deamination in heart. Oral pretreatment with increasing doses of MD780515 (2.6 to 84 mg/kg) gradually removed brain MAO A inhibition caused by clorgyline (92%, 28.2 mg/kg) or tranylcypromine (88%, 4.8 mg/kg), the complete removal being observed at the dose of 21 mg/kg of MD780515 for clorgyline, and at 42 mg/kg for tranylcypromine. Inhibition of brain MAO B by tranylcypromine (96%) was not modified by pretreatment with the same range of oral doses of MD780515. The results are consistent with a specific and reversible inhibition of MAO A activity by MD780515 which can protect against long acting MAO A inhibitory effects of clorgyline and tranylcypromine. MD780515 enhances the selectivity of tranylcypromine.     

Oxidation of beta-phenylethylamine by both types of monoamine oxidase: effects of substrate concentration and pH.

β-Phenylethylamine (PEA) was characterized as substrate for both type A and type B monoamine oxidase (MAO) in rat brain mitochondria at different substrate concentrations and at different pHs of the reaction media. The experiments on sensitivity to clorygline and deprenyl showed that the inhibition patterns with PEA as substrate differed markedly at different substrate concentrations: at 10 μM, PEA acted as a specific substrate for type B MAO, but at 50–1000 μM it became a common substrate for both types of MAO. The inhibition patterns were also affected markedly by a small change in pH of the reaction medium, especially when PEA concentrations were 50 and 100 μM: the change in pH from 7.2 to 7.8 resulted in the incresse in the proportion of type A MAO by 20–30 per cent. To investigate the mechanisms of such changes in substrate specificity of PEA, kinetic analyses were carried out at pH 7.2 and 7.8 with the uninhibited, the clorgyline-treated (type B) and the deprenyl-treated (type A) enzyme. The Lineweaver-Burk plots for the uninhibited MAO showed strong substrate inhibition for both pHs, which is more marked at pH 7.8 than at pH 7.2. Pretreatment of the enzyme with 10^?7 M clorgyline resulted in generally similar K_m values for PEA to those of the uninhibited enzyme, and the substrate inhibition at pH 7.8 was also stronger than that at pH 7.2. After pretreatment with 10^?7 M deprenyl, the K_m values were higher and the V_max values were lower than those of the uninhibited or the clorgyline-treated enzyme; there was no or only slight substrate inhibition in these curves. These results suggest that the remarkable changes in substrate specificity observed at different PEA concentrations and at different pHs may be due to the strong substrate inhibition of type B MAO.     

Monoamine oxidase activity in embryos of pike (Esox lucius)

1. Mitochondrial MAO specific activity was measured in eggs and early embryos of the teleostean fish Esox lucius using tryptamine, 5-hydroxytryptamine (5-HT) and phenylethylamine (PEA) as substrates. 2. Tryptamine is the most readily deaminated substrate in mitochondria isolated from unfertilized eggs and embryos at the stages of cleavage, blastula and gastrula. 3. Monoamine oxidase activity gradually decreases during development and at the gastrula stage it is respectively 80% (tryptamine), 70% (5-HT) and 50% (PEA) of that found in the egg using the corresponding substrate. 4. The inhibition of egg MAO activity by clorgyline and deprenyl measured in E. lucius eggs using tryptamine as substrate, indicates the presence of a single form of MAO not corresponding to the MAO A and MAO B described in terrestrial vertebrates.     

NONEXISTENCE OF A TYPE C MONOAMINE OXIDASE IN RAT BRAIN

Abstract— The possible existence of type C MAO, distinct from type A and type B, in circumventricular structures of rat brain was examined by histological studies on the inhibitory effects of clorgyline. a preferential type A MAO inhibitor and deprenyl, a preferential type B inhibitor, on enzyme. Brain slices were preincubated with the inhibitors and then incubated with 5-HT, the substrate for type A MAO, and stained for MAO activity. Deposits of the product formazan were detected in circumventricular structures of slices of brain preincubated with clorgyline and deprenyl at concentrations of 10^-7–10^-4m at room temperature for 5 min. When the slices were preincubated with either of these inhibitors at room temperature for 60 min, strong activity was observed in this region, whereas when they were preincubated with either 10^-5m -clorgyline or 10^-5m -deprenyl for 20 and 30 min at 37°C, no MAO activity was seen in any region of the brain. Thus, at the higher preincubation temperature, lower concentrations of each inhibitor and a shorter preincubation period were required for inhibition of the enzyme. Preincubation for 60 min at 37°C with a combination of 10^-7m -clorgyline and 10^-8m -deprenyl did not inhibit the enzyme in the circumventricular region completely, but at the same temperature, concentrations of 10^-7m of both inhibitors inhibited the enzyme completely in 10min, Thus the effects of the inhibitors are synergistic. These results indicate that the inhibitory effects of the two inhibitors on the enzyme in circumventricular structures of the brain is time- and temperature-dependent. Moreover, the activity seems to be sensitive to deprenyl even when 5-HT is used as substrate. The results do not support the idea of the existence of type C MAO, distinct from type A and type B MAO.     

Developmental changes in the activity and substrate specificities of mouse brain monoamine oxidase

Developmental changes in monoamine oxidase (MAO) activity in the mouse brain were investigated with the substrates -phenylethylamine (PEA), tryptamine, and 5-hydroxytryptamine (5-HT). In the newborn brain, MAO activity towards PEA was found to be much lower than the adult and to be inhibited by clorgyline in a double-sigmoidal fashion. The inhibition curve shifted to a single-sigmoidal pattern with age. MAO activity towards 5-HT as substrate was inhibited by 90% and in a single-sigmoidal manner by clorgyline throughout the postnatal life. Lineweaver-Burk plots with PEA as substrate presented two linear lines (apparentK _m: 28.6 and 4.1 M) for the newborn and one line (apparentK _m: 11.4 M) for the adult, respectively. The plot with highK _m value for the newborn brain disappeared in a clorgyline-treated preparation. These findings suggest that age-dependent alterations in the ratio of MAO-A/MAO-B activity affect the substrate specificity of the enzyme.     

Serotonin Metabolism by Monoamine Oxidase in Rat Primary Astrocyte Cultures

The oxidative deamination of serotonin (5-HT) to 5-hydroxyindoleacetic acid (5-HIAA) by rat primary astrocyte cultures was investigated in intact cells using HPLC. All detectable 5-HIAA accumulated in the extracellular medium, and its rate of production was proportional to the 5-HT concentration over the tested range of 5 x 10(-7) to 10(-4) M. At 5 x 10(-7) M 5-HT, intracellular 5-HT was detectable only in astrocytes treated with monoamine oxidase (MAO) inhibitors. These findings are consistent with the idea that 5-HT taken up into astrocytes is not stored for re-release, but is rapidly metabolized to 5-HIAA, which is then extruded from the cell. At 5 x 10(-7) M 5-HT, 5-HIAA formation in intact cells was blocked 63% by the selective high-affinity 5-HT uptake inhibitor fluoxetine. 5-HT oxidation to 5-HIAA is carried out principally by MAO-A, because clorgyline was more effective at inhibiting the production of 5-HIAA than was pargyline. Radioenzymatic determinations of MAO activity in cell homogenates supported these findings, because under these conditions clorgyline was 1,000-fold more effective than pargyline at inhibiting MAO activity toward 14C-labelled 5-HT. However, the relatively selective MAO-B substrate beta-phenylethylamine (PEA) was also oxidized, showing that these cultures also contained MAO-B activity; the Km values for MAO-A oxidation of 5-HT and MAO-B oxidation of PEA were 135 and 45 microM, and Vmax values were 88 and 91 nmol/mg of total cell protein/h, respectively. Higher concentrations of PEA (greater than 20 microM) were oxidized by both MAO-A and MAO-B isozymes.(ABSTRACT TRUNCATED AT 250 WORDS)     

Monoamine oxidase: To B or not to B?

That the enzyme, monoamine oxidase (E.C. 1.4.3.4. amine: O₂ oxidoreductase, MAO) exists in multiple forms was first suggested by Johnston (1) who studied the effects of the irreversible inhibitor clorgyline on MAO. It has been proposed that MAO can be classified into two types, A and B, according to their inhibitor sensitivity and substrate specificity. Type A MAO was found to be solely responsible for the deamination of 5-hydroxytryptamine (5-HT) and shows high sensitivity to clorgyline, while type B MAO metabolizes 2-phenethylamine (PEA) and benzylamine (BA) and is less sensitive to clorgyline. Subsequently, it was shown that type B MAO is highly sensitive to the irreversible inhibitor deprenyl (2).Recently, the “multiple forms” concept has been questioned (3–5) mainly because of increasing evidence which is contradictory to some earlier findings. As an alternative, another hypothesis was put forward insinuating that MAO is an enzyme with multiple binding sites but only one molecular entity (3,4,6,7). This account will focus on some experimental findings accumulated mainly since 1978 and which, although equivocal, strongly support the “one molecular entity” hypothesis of MAO.     

Some characteristics of mitochondrial monoamine oxidase activity in eggs of carp (Cyprinus carpio) and rainbow trout (Salmo gairdneri)

1. Monoamine oxidase (MAO) activity towards tryptamine, 5-hydroxytryptamine (5-HT) and phenylethylamine (PEA) has been measured in mitochondria isolated from carp and trout eggs. 2. In carp eggs all the tested substrates are metabolized and the highest affinity is found with tryptamine. In trout eggs a consistent level of MAO activity is obtained using tryptamine. 3. The inhibition dose-response curves of clorgyline and deprenyl indicate that both in carp and trout eggs there is only one form of mitochondrial MAO, distinct from MAO A and B which have been described in vertebrate tissues. 4. Both in carp and trout egg mitochondria a semicarbazide-sensitive amine oxidase is not involved in the deamination of the used substrates. 5. MAO found in carp and trout eggs might be involved in metabolism of some neurotransmitter monoamines during early developmental stages.     

5-HYDROXYTRYPTAMINE CATABOLISM IN THE RAT BRAIN DURING ONTOGENESIS

Although the serotoninergic innervation is immature in the brains of young rats, the 5-HIAA content is similar to that found in adults. As indicated by the ratio of 5-HIAA to 5-HT levels in the brain stem and the forebrain, the catabolism of the indolamine was more rapid during the first 3 postnatal weeks than in adults. This was contirmed by measuring the total formation of [³H]5-HIAA from [³H]5-HT newly synthesized from L-[³H]tryptophan in brain stem slices of young and adult rats. Electrolytic lesions of midbrain raphe nuclei (B7 and B8) performed on the 5th postnatal day resulted in parallel decreases in brain 5-HT and 5-HIAA levels; this ruled out the possibility that 5-HIAA might be formed from 5-HT synthesized outside serotoninergic neurons, using peripheral 5-hydroxytryptophan. Inhibition of 5-HT storage by reserpine pretreatment did not alter the higher capacity of newborn tissues to catabolize exogenous [³H]5-HT. Therefore, possible differences in 5-HT binding in serotoninergic neurons between newborn and adult rats were not likely to account for the differences in 5-HT catabolism. Estimation of the rate of 5-HIAA efflux from the brain after MAO inhibition did not reveal marked changes with age. The activity of MAO type A, the enzyme involved in 5-HT catabolism, was higher during early life than later on. This could be shown by using 5-HT as substrate and clorgyline as a selective inhibitor. An opposite pattern of development was seen for MAO B, measured with benzylamine as substrate and deprenyl as selective inhibitor. These results suggest that the high 5-HIAA levels found in the brains of young rats can be attributed mainly to the presence of high MAO A activity during early life.     

[3H]HARMALINE AS A SPECIFIC LIGAND OF MAO A—I. PROPERTIES OF THE ACTIVE SITE OF MAO A FROM RAT AND BOVINE BRAINS

A high-affinity (K_d= 5.9 nM) specific binding site for [³H]harmaline was detected in membranes from rat and bovine brains. Studies of the regional and subcellular distributions of this binding indicated its close association with monoamine oxidase type A activity (MAO A) measured with [³H]serotonin ([³H]5-HT) as the substrate. Maximal binding capacity and MAO A activity were found in mitochondrial enriched fractions. Mitochondria of synaptosomal or extra-synaptosomal origin exhibited very similar properties with respect to [³H]harmaline binding characteristics and MAO A activity. Among psychoactive drugs, only monoamine oxidase inhibitors (MAO I) prevented the specific binding of [₃H]harmaline. Logit-log inhibition curves of binding by MAO I gave only one slope which was not significantly different from 1.0, suggesting the existence of only 1 category of specific sites for [³H]harmaline in the membrane preparations from rat and bovine brains. Consistent with the preferential inhibition of MAO A by harmaline, other MAO I of this class, i.e. clorgyline and Lilly 51641, were 10²-2 × 10³ times more efficient than deprenyl and pargyline, two inhibitors of MAO type B, in displacing [³H]harmaline from its specific binding site. K_i and IC₅₀ values for the inhibition of [³H]harmaline binding by MAO I and MAO substrates (tryptamine, 5-HT, norepinephrine) were almost identical with those characterizing their action on MAO A activity with [³H]5-HT as the substrate. In conclusion, the specific binding site for [³H]harmaline exhibited all the expected properties of the active site of MAO A. Like the technique of precipitation with a specific antibody, binding of [³H]harmaline should be of great help for studying the structural characteristics of the active site of MAO A and determining the number of MAO molecules in tissues under various physiological conditions.     

Early changes in mitochondrial monoamine oxidase activity of rat liver during 2-acetylaminofluorene feeding

The activities of mitochondrial type A and B monoamine oxidase were determined in the liver of rats fed a diet containing 2-acetylaminofluorene (AAF). Three days after the initiation of AAF-feeding, there was a significant decrease of type B monoamine oxidase activity without affect on type A enzyme. The decreased activity of type B monoamine oxidase, which reached a minimum after three weeks, was sustained for as long as AAF-feeding was continued. Sex-related difference in response to AAF was seen in the rat with respect to the onset and the intensity of the decreased type B monoamine oxidase activity, male rats being more sensitive to the carcinogen than female rats. In contrast to the in vivo effect, AAF showed a potent inhibitory effect on type A monoamine oxidase, rather than on type B enzyme, when added in vitro. The pI₅₀ values were estimated to be 7.5 against type A monoamine oxidase and 4.1 against type B enzyme, respectively. The in vitro inhibition of both types of monoamine oxidase by AAF was competitive. The K_i values for AAF were calculated to be 9.51 · 10^?9 M for type A monoamine oxidase and 1.30 · 10^?5 M for type B enzyme, respectively. In accordance with the potent inhibitory effect of AAF on type A monoamine oxidase in vitro, a single administration of the carcinogen, at a dose of 50 mg/kg, resulted in a marked and temporal decrease of the enzyme activity in the mitochondria of male rat liver. Recovery of the decreased type B monoamine oxidase activity was slow, and the enzyme activity did not return to control levels, even if rats were fed the basal diet for 2 or 4 weeks after the cessation of AAF-feeding.     

Human brain monoamine oxidase: solubilization and kinetics of inhibition by octylglucoside

Complete solubilization of both the A and B forms of human brain monoamine oxidase (MAO) occurred when crude mitochondria were incubated in the presence of 50 mM octylglucoside (OG). Upon removal of this nonionic detergent by dialysis, approximately 100% of the starting activity was present in the dialysate. The effects of solubilization were examined by comparison of several properties of the membrane-bound and OG-treated oxidases. The percentage inhibition of phenylethylamine (PEA) and the 5-hydroxytryptamine (5-HT) deamination by deprenyl and clorgyline were identical. The Km values obtained for the deamination of PEA, a B-selective substrate, 5-HT, an A-selective substrate, and tyramine (TYR), a nonselective substrate, were also comparable. OG was found to inhibit type A (I50 = 8.1 mM) and B (I50 = 4.7 mM) MAO activities at concentrations at least 10-fold below those used to solubilize the oxidases. Kinetic studies revealed that OG was an apparent competitive inhibitor of PEA deamination whereas OG produced a mixed-type pattern of inhibition when 5-HT was the variable substrate. Inhibition of TYR deamination by either the A or B form of MAO produced a mixed pattern of inhibition. The findings herein suggest that solubilization of the A and B forms of MAO by OG does not significantly alter the substrate and inhibitor specificity of the oxidases following removal of detergent. However, in the presence of concentrations of OG 50 times less than the critical micellar concentration of this detergent, marked inhibition of deamination by both forms of human brain MAO is observed. Accordingly, the usefulness of OG is limited to situations where the detergent is completely removed before quantitation of MAO activity.     

Monoamine oxidase A mediates iodotyrosine formation induced by monoamines in bovine thyroid particulate fraction

Monoamines are able to increase the thyroid iodine organification in vitro. A predominance of the A form of monoamine oxidase (MAO) has been previously demonstrated to exist in bovine thyroid tissue. In the present study we have investigated the form of MAO that could be involved in the iodotyrosine formation induced by tyramine, 5-hydroxytryptamine (5-HT) and beta-phenylethylamine (PEA) in a bovine thyroid subcellular fraction. The relative capacity of these monoamines to generate H2O2 and to incorporate iodine into tyrosine has also been studied. The MAO A inhibitor clorgyline (10(-9) M) produced a strong inhibition on the iodotyrosine formation induced by tyramine, 5-HT and PEA. In contrast, only a slight reduction was observed with deprenyl as MAO B inhibitor. Among the three monoamines, tyramine produced the highest H2O2 generation and iodotyrosine formation. The lowest Km value obtained was for 5-HT and the highest for PEA. Regarding the Vmax, the lowest value was for 5-HT and the highest for tyramine. The amount of iodine incorporated to tyrosine was not equivalent to the H2O2 generated by the monoamines nor to that exogenously added. Our results indicate that in bovine thyroid tissue mainly the A form of MAO is involved in the monoamine metabolism.