[亮氨酸1]促吞噬肽与天然促吞噬肽促吞噬素的比较研究。

A comparative study of [Leu1]Tuftsin and tuftsin, a natural phagocytosis-stimulating peptide.

Nishioka K, Hurr K J, Dessens S E, Rodriguez T

Department of General Surgery, University of Texas M. D. Anderson Cancer Center, Houston 77030.

Int J Biochem. 1991;23(5-6):627-30. doi: 10.1016/0020-711x(87)90058-9.

Abstract

[Leu1]tuftsin was reported to have greater phagocytosis-stimulating activity than tuftsin (Thr-Lys-Pro-Arg). 2. However, a study on inactivation of tuftsin by polymorphonuclear leukocytes (PMNs) demonstrated that leucine aminopeptidase, an ecto-enzyme, located on PMN surface was responsible for this mechanism. 3. Since leucine aminopeptidase is known to cleave Leu more easily than Thr at the N-terminal position of peptides, this suggested to us that [Leu1]tuftsin might then be inactivated by PMNs more easily than tuftsin, and thus this analog might be less active than tuftsin. 4. In addition, many tuftsin preparations used in earlier studies were not fully active, as high-performance liquid chromatography was not available to separate out many contaminating diastereomers. 5. In view of this, we have synthesized and purified [Leu1]tuftsin and compared its phagocytosis-stimulating activity with tuftsin. 6. Our results indicate that [Leu1]tuftsin is not as active as tuftsin in stimulating phagocytosis.

摘要

据报道，[亮氨酸1]促吞噬肽比促吞噬肽（苏氨酸-赖氨酸-脯氨酸-精氨酸）具有更强的刺激吞噬作用。2. 然而，一项关于多形核白细胞（PMN）使促吞噬肽失活的研究表明，位于PMN表面的一种胞外酶——亮氨酸氨肽酶参与了这一机制。3. 由于已知亮氨酸氨肽酶在肽的N端比苏氨酸更容易切割亮氨酸，这使我们推测[亮氨酸1]促吞噬肽可能比促吞噬肽更容易被PMN失活，因此这种类似物的活性可能比促吞噬肽低。4. 此外，早期研究中使用的许多促吞噬肽制剂活性并不完全，因为当时没有高效液相色谱法来分离许多污染性的非对映异构体。5. 鉴于此，我们合成并纯化了[亮氨酸1]促吞噬肽，并将其刺激吞噬作用的活性与促吞噬肽进行了比较。6. 我们的结果表明，[亮氨酸1]促吞噬肽在刺激吞噬作用方面不如促吞噬肽活跃。