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首页> 外文期刊>Neurochemistry International: The International Journal for the Rapid Publication of Critical Reviews, Preliminary and Original Research Communications in Neurochemistry >Arylamine and arylalkylamine N-acetyltransferases in retina, pineal gland, brain and liver of chicks: a comparative study.
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Arylamine and arylalkylamine N-acetyltransferases in retina, pineal gland, brain and liver of chicks: a comparative study.

机译：雏鸡视网膜，松果体，脑和肝中的芳胺和芳基烷基胺N-乙酰基转移酶：一项比较研究。

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摘要

Regulation of arylamine N-acetyltransferase (A-NAT) and arylalkylamine N-acetyltransferase (AA-NAT) was examined in retina, pineal gland, brain and liver of chicks. Enzyme activities were determined using as substrates p-phenetidine and procainamide for A-NAT, tryptamine and phenethylamine for AA-NAT. The activity of A-NAT in all tissues studied does not appear to be regulated by a light-dark cycle. On the other hand, AA-NAT showed distinct light-dark dependent changes (with high values at night) in the retina and pineal gland, but not in brain and liver. The nocturnal increase of retinal and pineal AA-NAT activity was prevented by cycloheximide; the drug did not affect A-NAT activity in these tissues. Treatment of light-adapted chicks with aminophylline significantly increased AA-NAT activity of the retina and pineal gland, without altering the enzyme activity in brain and liver. In these animals, the activity of A-NAT (procainamide) did not change in any tissue studied, whereas the enzyme activity measured using p-phenetidine as a substrate did decrease but only in the retina. A similar pattern of changes in retinal A-NAT and AA-NAT activities was observed after intraocular injection of d,b-cAMP. The rate of inactivation at 4 degrees C was significantly slower for AA-NAT than A-NAT. NATs from brain and liver displayed the highest and lowest, respectively, liability in the cold. The results indicate that the chick retina contains both A-NAT and AA-NAT. The two enzymes have distinct characteristics and the regulation of their activities is different. The retinal A-NAT is similar to A-NAT present in other tested tissues; however, AA-NAT can be induced at night only in the retina and pineal gland. It is suggested that there are two forms of retinal A-NAT, and that, under specified conditions, the activity of one form (A-NAT; p-phenetidine) may be regulated in an opposite manner to AA-NAT activity.
机译：在雏鸡的视网膜，松果体，大脑和肝脏中检查了芳基胺N-乙酰基转移酶（A-NAT）和芳基烷基胺N-乙酰基转移酶（AA-NAT）的调节。使用对甲基苯丙啶和普鲁卡因酰胺（对于A-NAT），色胺和苯乙胺（对于AA-NAT）作为底物来测定酶活性。研究的所有组织中A-NAT的活性似乎不受明暗循环的调节。另一方面，AA-NAT在视网膜和松果体中显示出明显的光暗依赖性变化（夜间具有较高的值），而在脑和肝中则没有。环己酰亚胺可防止夜间视网膜和松果AA-NAT活性的增加;该药物不影响这些组织中的A-NAT活性。用氨茶碱处理轻度适应的雏鸡，可显着增加视网膜和松果体的AA-NAT活性，而不会改变大脑和肝脏的酶活性。在这些动物中，A-NAT（普鲁卡因胺）的活性在任何研究的组织中均未改变，而使用对苯丙啶作为底物测得的酶活性确实降低了，但仅在视网膜中降低了。眼内注射d，b-cAMP后观察到视网膜A-NAT和AA-NAT活性的类似变化。对于AA-NAT，在4℃下的失活速率明显慢于A-NAT。在寒冷时，来自大脑和肝脏的NAT分别显示出最高和最低的责任。结果表明小鸡视网膜同时含有A-NAT和AA-NAT。这两种酶具有不同的特性，其活性调节也不同。视网膜A-NAT与其他测试组织中的A-NAT相似。然而，AA-NAT只能在晚上在视网膜和松果体中诱导。建议存在两种形式的视网膜A-NAT，并且在特定条件下，一种形式的活性（A-NAT;对苯乙啶）的活性可能与AA-NAT活性相反。

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