Feelisch M, Ostrowski J, Noack E
Institute of Pharmacology, Heinrich Heine University, Düsseldorf, F.R.G.
J Cardiovasc Pharmacol. 1989;14 Suppl 11:S13-22.
The vasodilator and antiaggregatory properties of sydnonimines like SIN-1 are thought to be due to their marked stimulatory action on soluble guanylate cyclase. Enzyme activation and consecutive cyclic GMP accumulation is mediated by the liberation of nitric oxide (NO) from the open-ring A forms of sydnonimines. The purpose of the present study was to investigate the mechanism of NO release from sydnonimines in direct comparison to their stimulatory effect at the target enzyme, soluble guanylate cyclase. All sydnonimines tested were found to spontaneously liberate NO, the rate of which closely correlated with the extent of enzyme activation. NO release occurred nonlinearly with time and became maximal at high sydnonimine concentration. The in vitro stability of the A forms neither correlated with the measured rate of NO release nor with enzyme activation, indicating that a direct stimulation of guanylate cyclase by the A forms is rather unlikely. Besides NO, all sydnonimines generated NO2- and NO3- at a nearly equimolar rate. The addition of cysteine induced a marked shift from NO3- to NO2- with a small reduction in NO release, which is paralleled by a weak rightward shift of the EC50 at the guanylate cyclase. All tested sydnonimines were found to consume molecular oxygen at rates that closely corresponded to the measured rates of NO formation. By a molar comparison, the amounts of consumed oxygen are clearly higher, as would be expected for the oxidative conversion of NO to NO2- and NO3-. Oxygen seems to be additionally involved in the induction of NO formation while being converted to superoxide (O2-). In accordance with an autocatalytic process, O2- further enhances sydnonimine decomposition, since in the presence of superoxide dismutase (SOD) the rate of SIN-1C and NO2-/NO3- formation from SIN-1A was reduced, whereas the rate of NO liberation seemingly increased. O2- has, however, no influence on the rate of hydrolysis of SIN-1 to SIN-1A. At the level of guanylate cyclase, the presence of SOD induced a leftward shift of the concentration-response curve to SIN-1, in agreement with an enhancement of efficacy of NO by blocking the NO-scavenging effect of O2-. An additional O2- generation markedly enhanced SIN-1A decomposition to NO2-/NO3- and reduced the apparent rate of NO formation. We conclude from our results that oxygen plays a key role in the decomposition of sydnonimines and thus in the formation of NO as their pharmacodynamically active principle. Oxygen attack most probably occurs by one-electron abstraction from the A form of the respective sydnonimine compound.(ABSTRACT TRUNCATED AT 400 WORDS)
像SIN - 1这样的西地那非类化合物的血管舒张和抗聚集特性被认为是由于它们对可溶性鸟苷酸环化酶有显著的刺激作用。酶的激活以及随后环鸟苷酸的积累是由西地那非类化合物开环A形式释放一氧化氮(NO)介导的。本研究的目的是直接比较西地那非类化合物释放NO的机制与其对靶酶可溶性鸟苷酸环化酶的刺激作用。所有测试的西地那非类化合物都被发现能自发释放NO,其释放速率与酶激活程度密切相关。NO的释放随时间呈非线性变化,在高浓度西地那非类化合物时达到最大值。A形式的体外稳定性既与测得的NO释放速率无关,也与酶激活无关,这表明A形式直接刺激鸟苷酸环化酶的可能性很小。除了NO,所有西地那非类化合物以几乎等摩尔的速率生成NO₂⁻和NO₃⁻。加入半胱氨酸会导致明显从NO₃⁻向NO₂⁻的转变,同时NO释放略有减少,这与鸟苷酸环化酶处的EC₅₀向右轻微移动相平行。所有测试的西地那非类化合物消耗分子氧的速率与测得的NO生成速率密切对应。通过摩尔比较,消耗的氧量明显更高,这是将NO氧化转化为NO₂⁻和NO₃⁻所预期的。氧似乎还参与了NO形成的诱导过程,同时被转化为超氧化物(O₂⁻)。根据自催化过程,O₂⁻进一步增强西地那非类化合物的分解,因为在超氧化物歧化酶(SOD)存在下,SIN - 1C由SIN - 1A形成以及NO₂⁻/NO₃⁻形成的速率降低,而NO释放速率似乎增加。然而,O₂⁻对SIN - 1水解为SIN - 1A的速率没有影响。在鸟苷酸环化酶水平,SOD的存在导致对SIN - 1的浓度 - 反应曲线向左移动,这与通过阻断O₂⁻的NO清除作用增强NO的效力一致。额外的O₂⁻生成显著增强SIN - 1A分解为NO₂⁻/NO₃⁻,并降低了NO形成的表观速率。我们从结果中得出结论,氧在西地那非类化合物的分解中起关键作用,从而在作为其药效学活性成分的NO形成中起关键作用。氧攻击很可能是通过从相应西地那非类化合物的A形式夺取一个电子发生的。(摘要截断于400字)