Complete deficiency of glycophorin A in red blood cells from mice with targeted inactivation of the band 3 (AE1) gene
Complete deficiency of glycophorin A in red blood cells from mice with targeted inactivation of the band 3 (AE1) gene
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DOI：
10.1182/blood.v91.6.2146.2146_2146_2151
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发表时间：
1998-03-15
期刊：
影响因子：
20.3
通讯作者：
Chishti, AH
中科院分区：
文献类型：
--
作者：
Hassoun, H;Hanada, T;Chishti, AH
血型糖蛋白 A 是红细胞的主要跨膜唾液酸糖蛋白。它已被证明有助于 MN 和赖特血型抗原的表达，作为疟原虫恶性疟原虫和仙台病毒的受体，并且与阴离子转运蛋白带 3 一起可能有助于红细胞膜的机械特性。多项证据表明血型糖蛋白 A 和带 3 在生物合成过程中存在密切的相互作用。最近，我们培育了通过选择性失活AE1阴离子交换基因而完全消除带3表达的小鼠，从而使我们能够研究带3对红细胞膜蛋白表达的影响。在本报告中，我们表明带 3 -/- 红细胞含有蛋白 4.1、内收蛋白、脱蛋白、p55 和糖蛋白 C。相反，通过蛋白质印迹和免疫细胞化学技术评估，带 3 -/- 红细胞完全不含糖蛋白 A (GPA)，而聚合酶链式反应 (PCR) 证实了 GPA mRNA 的存在。脉冲标记和脉冲追踪实验表明，GPA 不会掺入膜中，而是在细胞质中快速降解。基于这些发现和其他已发表的证据，我们提出带 3 起着类似伴侣的作用，这对于将 GPA 募集到红细胞质膜是必需的。 (C) 1998 年，美国血液学会。
Glycophorin A is the major transmembrane sialoglycoprotein of red blood cells. It has been shown to contribute to the expression of the MN and Wright blood group antigens, to act as a receptor for the malaria parasite Plasmodium falciparum and Sendai virus, and along with the anion transporter, band 3, may contribute to the mechanical properties of the red blood cell membrane. Several lines of evidence suggest a close interaction between glycophorin A and band 3 during their biosynthesis. Recently, we have generated mice where the band 3 expression was completely eliminated by selective inactivation of the AE1 anion exchanger gene, thus allowing us to study the effect of band 3 on the expression of red blood cell membrane proteins. In this report, we show that the band 3 -/- red blood cells contain protein 4.1, adducin, dematin, p55, and glycophorin C. In contrast, the band 3 -/- red blood cells are completely devoid of glycophorin A (GPA), as assessed by Western blot and immunocytochemistry techniques, whereas the polymerase chain reaction (PCR) confirmed the presence of GPA mRNA. Pulse-label and pulse-chase experiments show that GPA is not incorporated in the membrane and is rapidly degraded in the cytoplasm. Based on these findings and other published evidence, we propose that band 3 plays a chaperone-like role, which is necessary for the recruitment of GPA to the red blood cell plasma membrane. (C) 1998 by The American Society of Hematology.