Role of the first N-terminal basic cluster of human lactoferrin (R2R3R4R5) in the interactions with the Jurkat human lymphoblastic T-cells.
Role of the first N-terminal basic cluster of human lactoferrin (R2R3R4R5) in the interactions with the Jurkat human lymphoblastic T-cells.
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人乳铁蛋白第一个 N 端基本簇 (R2R3R4R5) 在与 Jurkat 人淋巴细胞 T 细胞相互作用中的作用。
DOI：
10.1007/978-1-4757-9068-9_6
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发表时间：
1998
影响因子：
--
通讯作者：
Geneviève Spik
中科院分区：
文献类型：
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作者：
Dominique Legrand;P. V. Berkel;Valérie Salmon;H. Veen;M. Slomianny;J. Nuijens;Geneviève Spik
我们之前对 Jurkat 人淋巴细胞 T 细胞上的人乳铁蛋白 (hLf) Mr 105,000 受体进行了表征。为了描述 hLf R2R3R4R5 在与细胞相互作用中的作用，我们研究了通过胰蛋白酶解（hLf-2N、hLF-3N 和 hLf-4N）或通过诱变（rhLf-5N）获得的 hLf 变体的结合。从 hLf 中连续去除 N 端精氨酸残基逐渐增加了结合亲和力，但减少了细胞上的结合位点数量。牛 Lf 和天然 hLf 的结合参数没有差异，而鼠 Lf 的结合参数与 rhLf-5N 相似。在抑制硫酸化的氯酸盐存在下培养 Jurkat 细胞会减少天然 hLf 和 hLf-3N 的结合位点数量，但不会减少 rhLf-5N 的结合位点数量，表明 hLf 结合位点包括硫酸化分子。结果表明，hLf 与每个 Jurkat 细胞约 80,000 个结合位点（主要是硫酸化分子）的相互作用依赖于 R2R3R4，但不依赖于 R5。每个细胞与大约 20,000 个结合位点（可能是 hLf 受体）的相互作用不需要 hLf 的第一个 N 端基本簇。我们得出的结论是，从 hLf 中删除 R2-R5 可能有助于调节其与细胞结合的性质，从而调节其对细胞生理学的影响。
We previously characterized a receptor of Mr 105,000 for human lactoferrin (hLf) on Jurkat human lymphoblastic T-cells. To delineate the role of R2R3R4R5 of hLf in the interaction with cells, we studied the binding of hLf variants obtained either by tryptic proteolysis (hLf-2N, hLF-3N and hLf-4N) or by mutagenesis (rhLf-5N). Consecutive removal of N-terminal arginine residues from hLf progressively increased the binding affinity but decreased the number of binding sites on the cells. The binding parameters of bovine Lf and native hLf did not differ, whereas the binding parameters of murine Lf resembled those of rhLf-5N. Culture of Jurkat cells in the presence of chlorate, which inhibits sulfation, reduced the number of binding sites for both native hLf and hLf-3N but not for rhLf-5N indicating that the hLf binding sites include sulfated molecules. The results suggest that the interaction of hLf with about 80,000 binding sites per Jurkat cell, mainly sulfated molecules, is dependent on R2R3R4, but not on R5. Interaction with about 20,000 binding sites per cell, presumably the hLf receptor, does not require the first N-terminal basic cluster of hLf. We conclude that the deletion of R2-R5 from hLf may serve to modulate the nature of its binding to cells and thereby its effects on cellular physiology.
DOI：
10.1006/abbi.1995.1139
发表时间：
1995
期刊：
Archives of biochemistry and biophysics.
影响因子：
--
作者：
Wu,HF;Monroe,DM;Church,FC
通讯作者：
Church,FC