Branch of Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia.
Biochemistry (Mosc). 2014 Jan;79(1):1-7. doi: 10.1134/S0006297914010015.
Antibodies (immunoglobulins, Ig) are used by the immune system to identify and neutralize foreign objects and are responsible for antigen-binding and effector functions. Immunoglobulin G (IgG) is the major serum immunoglobulin of a healthy human (~75% of the total Ig fraction). The discovery in 1970 of the endogenous tetrapeptide tuftsin (Thr-Lys-Pro-Arg, fragment 289-292 of the C(H2)-domain of the heavy (H) chain of IgG), possessing both immunostimulatory and neurotrophic activities, was an impetus for the search for new biologically active peptides of immunoglobulin origin. As a result, fragments of the H-chain of IgG produced as a result of enzymatic cleavage of IgG within the antigen-antibody complex were discovered, synthesized, and studied. These fragments include rigin (341-344), immunorphin (364-373), immunocortin (11-20), and peptide p24 (335-358) and its fragments. In this review the properties of these peptides and their role in regulating the immune response are analyzed.
抗体（免疫球蛋白，Ig）被免疫系统用于识别和中和外来物体，并负责抗原结合和效应功能。免疫球蛋白 G（IgG）是健康人体中的主要血清免疫球蛋白（约占总 Ig 部分的 75%）。1970 年发现内源性四肽 tuftsin（Thr-Lys-Pro-Arg，IgG 重链（H）链 C（H2）结构域的片段 289-292），具有免疫刺激和神经营养活性，这推动了对新的具有生物活性的免疫球蛋白源性肽的研究。结果，发现了作为抗原-抗体复合物内 IgG 酶切产生的 IgG H 链片段，并对其进行了合成和研究。这些片段包括 rigin（341-344）、免疫吗啡（364-373）、免疫皮质素（11-20）和肽 p24（335-358）及其片段。在这篇综述中，分析了这些肽的性质及其在调节免疫反应中的作用。
