A study of an erythrocyte membrane protein that contributes to inhibition of agglutination of feline erythrocytes in glucose solution

K. Namikawa, Yumi Sato, T. Maruo, F. Sunaga, K. Sakaguchi, J. Suzuki
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Abstract

Due to the negative charges on their surface membrane, erythrocytes usually do not agglutinate each other in vivo. However, when mixed with 5% glucose solution in a test tube, some feline erythrocytes exhibit agglutination. To investigate the reasons for this phenomenon, we extracted erythrocyte membrane proteins from these cells and subjected them to sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). In samples in which agglutination did not occur, a band was seen at the 36-kDa position, whereas in samples showing agglutination, this band disappeared or has lower intensity. The 36-kDa position corresponds to glycophorin A in the human erythrocyte membrane, but no immunochemical cross-reaction with this band was seen. We therefore conducted mass spectrometry in order to investigate the composition, and found a partial amino acid sequence, His-Ile-Thr-Ser-Tyr-Pro-Glu-Thr-His-Glu-Gly. Furthermore, although no protein showing this sequence was found in any database, this protein was confirmed to be an acidic glycoprotein, therefore it is thought to be a glycophorin-like molecule in the feline erythrocyte membrane that could contribute to inhibition of agglutination.
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一种在葡萄糖溶液中抑制猫红细胞凝集的红细胞膜蛋白的研究
由于红细胞表面膜上的负电荷,红细胞在体内通常不会相互凝集。然而,当在试管中与5%葡萄糖溶液混合时,一些猫红细胞表现出凝集。为了研究这种现象的原因,我们从这些细胞中提取红细胞膜蛋白,并对其进行十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(SDS-PAGE)。在未发生凝集的样品中,在36kda位置可见条带,而在显示凝集的样品中,该条带消失或强度较低。36kda的位置与人红细胞膜上的糖蛋白A对应,但未见与该条带的免疫化学交叉反应。因此,我们通过质谱分析来研究其组成,并发现了一个部分氨基酸序列,His-Ile-Thr-Ser-Tyr-Pro-Glu-Thr-His-Glu-Gly。此外,虽然没有在任何数据库中发现显示该序列的蛋白,但该蛋白被证实是一种酸性糖蛋白,因此它被认为是猫红细胞膜中的糖蛋白样分子,可能有助于抑制凝集。
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