Erythrocytes attached to a wheat germ agglutinin coated surface display an altered phospholipid metabolism.

Erythrocytes attached to a wheat germ agglutinin coated surface display an altered phospholipid metabolism.
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附着在小麦胚芽凝集素涂层表面的红细胞显示出改变的磷脂代谢。

DOI:
10.1002/jcb.240380102
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发表时间:
1988
影响因子:
4
通讯作者:
Suzuki,T
Suzuki,T
中科院分区:
生物学2区
文献类型:
--
作者:
Dale,GL;Suzuki,T

文献摘要

相似文献

红细胞与凝集素包被的表面结合;与该表面的多价附着导致细胞严重变形和细胞磷脂代谢改变。使人红细胞在20°C下与包被有麦胚凝集素的聚苯乙烯珠(WGA珠)结合20分钟。然后裂解结合的红细胞以产生与WGA珠结合的基质。将对照基质和基质-WGA珠在37°C下与γ-32 P-ATP孵育,以检查磷脂标记模式。对照基质将32 P标记转化为磷脂酰肌醇-4-磷酸和磷脂酰肌醇-4,5-二磷酸,与早期研究一致。然而,基质-WGA珠显示除了磷酸肌醇中的32 P标记外,32 P标记还掺入磷脂酸中。在20 min试验期间产生的32 P-磷脂酸的量为3.23 ± 0.84(n = 7)皮摩尔/μg基质胆固醇;然而,合成量取决于用于制备基质-WGA珠的程序。如果红细胞在0°C而不是20°C下与WGA珠结合,则在随后的37°C γ-32 P-ATP测定期间产生的32 P-磷脂酸的量减少4.2倍;磷酸肌醇标记模式不变。此外,当完整红细胞与WGA珠结合的时间从1分钟变化到20分钟时,产生的32 P-磷脂酸的量呈时间依赖性增加。这种磷脂酸合成的诱导不能用液相WGA复制。因此,完整红细胞与WGA珠的多价结合导致磷脂代谢的改变。
Erythrocytes were bound to a lectin‐coated surface; the multivalent attachment to this surface resulted in a severe deformation of the cells and an alteration in the cellular phospholipid metabolism. Human erythrocytes were allowed to bind for 20 min at 20°C to polystyrene beads coated with wheat germ agglutinin (WGA beads). The bound erythrocytes were then lysed to produce stroma bound to WGA beads. Control stroma and stroma‐WGA beads were incubated at 37°C with γ‐32P‐ATP to examine the phospholipid labeling patterns. The control stroma incorporated32P‐label into phosphatidylinositol‐4‐phosphate and phosphatidylinositol‐4,5‐bisphosphate, in agreement with earlier studies. However, the stroma‐WGA beads showed incorporation of32P‐label into phosphatidic acid in addition to that in the phosphoinositides. The quantity of32P‐phosphatidic acid produced during the 20‐min assay was 3.23 ± 0.84 (n = 7) picomoles/μg stromal cholesterol; the amount synthesized, however, was dependent on the procedure used to prepare the stroma‐WGA beads. If the erythrocytes were bound to the WGA beads at 0°C instead of 20°C, the quantity of32P‐phosphatidic acid produced during the subsequent 37°C assay with γ‐32P‐ATP was decreased 4.2 fold; the phosphoinositide labeling pattern was unchanged. In addition, when the time for binding of intact erythrocytes to the WGA beads was varied from 1 to 20 minutes, there was a time‐dependent increase in the amount of32P‐phosphatidic acid produced. This induction of phosphatidic acid synthesis could not be duplicated with fluid phase WGA. Therefore, the multivalent binding of intact erythrocytes to WGA beads causes an alteration in phospholipid metabolism.