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凝集素对蝗虫肌肉谷氨酸受体脱敏作用的影响。

The effect of lectins on desensitisation of locust muscle glutamate receptors.

作者信息

Evans M L, Usherwood P N

出版信息

Brain Res. 1985 Dec 9;358(1-2):34-9. doi: 10.1016/0006-8993(85)90945-x.

Abstract

At the excitatory neuromuscular junction of the locust, Schistocerca gregaria, desensitisation to L-glutamate is blocked by the lectin concanavalin A (Con A). In this study a range of lectins has been used to assess the influence of simple sugar binding specificity on desensitisation block. Pea and lentil lectins have similar simple sugar specificities (mannose/glucose) to Con A and block desensitisation in a similar manner. Soybean and wheatgerm lectins have other simple sugar specificities and do not block desensitisation of the locust muscle glutamate receptor. Native Con A is a tetramer at pH 7 but at lower pH or following succinylation (S-Con A) it becomes a dimer, with reduced biological activity. S-Con A does not block desensitisation but it does bind to locust muscle and protects the glutamate receptor from the desensitisation block caused by Con A. When Con A is applied to a desensitised neuromuscular junction the ongoing desensitisation is not blocked. It appears that desensitisation block by Con A, pea and lentil lectins is dependent on lectin binding to mannose or glucose moieties on or in the region of the glutamate receptor, and that these moieties are masked from lectin when the receptor is in its desensitised state.

摘要

在沙漠蝗(Schistocerca gregaria)的兴奋性神经肌肉接头处,对L-谷氨酸的脱敏作用被凝集素伴刀豆球蛋白A(Con A)所阻断。在本研究中,一系列凝集素被用于评估简单糖结合特异性对脱敏阻断的影响。豌豆凝集素和扁豆凝集素与Con A具有相似的简单糖特异性(甘露糖/葡萄糖),并以相似的方式阻断脱敏作用。大豆凝集素和麦胚凝集素具有其他简单糖特异性,不会阻断蝗虫肌肉谷氨酸受体的脱敏作用。天然Con A在pH 7时是四聚体,但在较低pH或琥珀酰化后(S-Con A)它变成二聚体,生物活性降低。S-Con A不会阻断脱敏作用,但它确实能结合蝗虫肌肉,并保护谷氨酸受体免受Con A引起的脱敏阻断。当将Con A应用于脱敏的神经肌肉接头时,正在进行的脱敏作用不会被阻断。看来,Con A、豌豆凝集素和扁豆凝集素引起的脱敏阻断依赖于凝集素与谷氨酸受体上或其区域内的甘露糖或葡萄糖部分结合,并且当受体处于脱敏状态时,这些部分会对凝集素产生屏蔽作用。

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