Suzuki-Nishimura T, Nagaya K, Matsuda K, Uchida M K, Aoki J, Umeda M, Inoue K
Department of Molecular Pharmacology, Meiji College of Pharmacy, Tokyo, Japan.
Jpn J Pharmacol. 1991 Sep;57(1):79-90. doi: 10.1254/jjp.57.79.
The histamine release induced by compound 48/80, bradykinin or polyethylenimine with a molecular weight of 600 (PEI6) was inhibited by wheat germ agglutinin (WGA) and phytohemagglutinin E-subunits (PHA-E4), and the inhibition was specifically reversed by N-acetyl glucosamine and N-acetyl galactosamine, respectively. Concanavalin A (Con A) and phytohemagglutinin L-subunits (PHA-L4) did not inhibit the histamine release induced by compound 48/80, bradykinin or PEI6. The histamine release induced by substance P was also inhibited sugar-specifically by WGA and PHA-E4. The binding sites for compound 48/80, bradykinin, PEI6 and substance P, therefore, seemed to especially overlap each other. These binding sites were found to be glycoproteins having affinities to WGA and PHA-E4, but not to Con A and PHA-L4. The binding of WGA and PHA-E4 to the glycoproteins resulted in inhibition of the interaction between the basic secretagogues including bradykinin and substance P and their binding sites on the mast cells. The bindings of five lectins to mast cell glycoproteins were examined by lectin-blotting. Several glycoproteins, which had specific affinities to WGA and PHA-E4, but not to Con A and PHA-L4 were detected. We assumed that the binding sites for basic secretagogues which are coupled with histamine-releasing mechanisms exist among these glycoproteins. A 41-kDa protein (alpha-subunit of pertussis toxin-sensitive G protein) was not detected by WGA, suggesting that the binding sites for the basic secretagogues were not G proteins.
化合物48/80、缓激肽或分子量为600的聚乙烯亚胺（PEI6）诱导的组胺释放受到麦胚凝集素（WGA）和植物血凝素E亚基（PHA-E4）的抑制，且这种抑制作用分别被N-乙酰葡糖胺和N-乙酰半乳糖胺特异性逆转。刀豆球蛋白A（Con A）和植物血凝素L亚基（PHA-L4）并未抑制化合物48/80、缓激肽或PEI6诱导的组胺释放。P物质诱导的组胺释放也被WGA和PHA-E4以糖特异性方式抑制。因此，化合物48/80、缓激肽、PEI6和P物质的结合位点似乎特别相互重叠。这些结合位点被发现是对WGA和PHA-E4有亲和力，但对Con A和PHA-L4没有亲和力的糖蛋白。WGA和PHA-E4与糖蛋白的结合导致包括缓激肽和P物质在内的碱性促分泌剂与其在肥大细胞上的结合位点之间的相互作用受到抑制。通过凝集素印迹法检测了五种凝集素与肥大细胞糖蛋白的结合情况。检测到几种对WGA和PHA-E4有特异性亲和力，但对Con A和PHA-L4没有亲和力的糖蛋白。我们推测，与组胺释放机制相关的碱性促分泌剂的结合位点存在于这些糖蛋白之中。WGA未检测到一种41 kDa的蛋白质（百日咳毒素敏感G蛋白的α亚基），这表明碱性促分泌剂的结合位点不是G蛋白。
