Tzehoval E, Segal S, Stabinsky Y, Fridkin M, Spirer Z, Feldman M
Proc Natl Acad Sci U S A. 1978 Jul;75(7):3400-4. doi: 10.1073/pnas.75.7.3400.
The immunoglobulin heavy-chain-associated tetrapeptide, tuftsin (Thr-Lys-Pro-Arg), known for its phagocytosis-stimulating activity, was found to augment the antigen-specific, macrophage-dependent education of T lymphocytes. The investigation of stereospecific characteristics of the tetrapeptide, by use of structural analogs with different modifications, revealed strict structural requirements for eliciting the immunogenic activity of macrophages. It was found that the most important moiety for its activity is the dipeptide Pro-Arg. This finding is of interest in view of the appearance of this particular dipeptide in other bioregulatory peptides, including many of the peptide hormones. The significance of the appearance of a common structure in such molecules, which may act through specific receptors on different target cells, is discussed.
免疫球蛋白重链相关四肽——促吞噬素（苏氨酸-赖氨酸-脯氨酸-精氨酸），因其具有刺激吞噬作用而闻名，现已发现它能增强T淋巴细胞的抗原特异性、巨噬细胞依赖性的诱导作用。通过使用具有不同修饰的结构类似物对该四肽的立体特异性特征进行研究，揭示了引发巨噬细胞免疫原活性的严格结构要求。结果发现，其活性最重要的部分是二肽脯氨酸-精氨酸。鉴于这种特定二肽在其他生物调节肽（包括许多肽类激素）中的出现，这一发现很有意思。本文讨论了这类可能通过不同靶细胞上的特异性受体起作用的分子中出现共同结构的意义。
