Machaidze G G, Mikeladze D
Department of Biophysical Chemistry, Biozentrum, University of Basel, Switzerland.
Neurochem Res. 2001 May;26(5):457-62. doi: 10.1023/a:1010961808570.
The effects of the lectins concanavalin A, WGA, ricin, abrin, and the mistletoe lectins from Viscum album MLI, MLII, and MLIII on the binding of ligands of the NMDA and sigma receptors in rat hippocampus synaptic plasma membranes were investigated. Binding of [3H]MK-801, [3H]glutamate, [3H]5,7-DCKA, and [3H]glycine to the membranes was decreased by 40-60% after addition of galactose-specific lectins (mistletoe lectins MLI, MLII, ricin, abrin) at concentrations of 0.01 mg/ml, but was not affected by the glucose- and mannose-specific lectin Con A, an acetylglucosamine-specific lectin WGA, or an acetylgalactosamine-specific lectin MLIII. The binding of [3H]SKF 10047 was decreased only in the presence of MLIII and did not change after addition of the other lectins. It is suggested that lectin-sensitive ligand binding sites of sigma- and NMDA receptors are located separately, and that the carbohydrate side chains of the sigma receptor do not participate in the modulation of the NMDA-receptor.
研究了伴刀豆球蛋白A、小麦胚凝集素、蓖麻毒素、相思子毒素以及欧洲槲寄生中的槲寄生凝集素MLI、MLII和MLIII对大鼠海马突触质膜中N-甲基-D-天冬氨酸（NMDA）受体和σ受体配体结合的影响。在加入浓度为0.01mg/ml的半乳糖特异性凝集素（槲寄生凝集素MLI、MLII、蓖麻毒素、相思子毒素）后，[3H]MK-801、[3H]谷氨酸、[3H]5,7-二氯犬尿氨酸和[3H]甘氨酸与膜的结合减少了40%-60%，但葡萄糖和甘露糖特异性凝集素伴刀豆球蛋白A、N-乙酰葡糖胺特异性凝集素小麦胚凝集素或N-乙酰半乳糖胺特异性凝集素MLIII对此没有影响。[3H]SKF 10047的结合仅在MLIII存在时减少，加入其他凝集素后没有变化。这表明σ受体和NMDA受体的凝集素敏感配体结合位点是分开的，并且σ受体的碳水化合物侧链不参与NMDA受体的调节。
