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Pregnancy specific glycoproteins: structure, functions and biologically active peptidesстатья
- Авторы: Terentiev A.A., Mokhosoev I.M., Moldogazieva N.T.
- Сборник: В книге: Human Placenta: Structure and Development, Circulation and Functions
- Глава в коллективной монографии
- Год издания: 2010
- Первая страница: 125
- Последняя страница: 144
- Аннотация: Chapter IV. Pregnancy-specific glycoproteins (PSGs) are secreted proteins which are produced by the rodent and primate placenta and play a critical role in pregnancy success. Genes which encode PSGs belong to carcinoembryonic antigen (CEA) gene family, which is included in immunoglobulin (Ig) gene superfamily. In humans, to date there are 11 protein products of these genes which are designated as PSG1−11. In rodents there are 17 PSGs, which are designated as PSG16−32. Human PSGs were first discovered in serum of pregnant women and were initially named as trophoblast-specific beta globulins (TBGs). Little later they were isolated from placental extracts and also revealed in serum of patients with trophoblastic tumors. Biological role of PSGs is not fully elucidated to date. However a number of experimental data and clinical observations allow supposing their critical role in the maintenance of pregnancy. Low PSG levels in the maternal circulation are associated with threatened abortions, intrauterine retardation and fetal hypoxia. It has been shown that PSGs function as immunomodulatory proteins which regulate activity of T-lymphocytes and secretion of cytokines by monocytes and macrophages. Also, PGSs may participate in maternal vasculature remodeling through influencing on secretion of pro-angiogenic agents such as transforming growth factor-beta-1 (TGF-β1) and vascular endothelial growth factor (VEGF) by different cell types involved in the development of placenta. Several functional domains have been described in PSG structures. For example, tripeptide RGD has been revealed in N-terminal immunoglobulin (Ig)-like domain of most of human PSGs. It is proposed that RGD motif of PSGs is involved in binding to integrin receptors. Binding of mouse PSGs to integrin-associated receptor CD9 has been demonstrated. In our laboratory some human PSG-derived oligopeptide fragments have been shown to possess biological activity. This chapter is devoted to summarizing and analyzing of data on structure and function of PSGs known to date. Also, relatively recent data of PSG-derived biologically active peptides are described.
- Добавил в систему: Молдогазиева Нурбубу Тентиевна