In Vitro Effects of Tp5 Analogs on E-Rosette Formation and Cell Division

Autor:	Karoly Lapis, I. Schön, O. Nyéki, J. Major, L Szporny, L. Dénes, L Kisfaludy, Hajós G, J Ember, Béla Szende
Rok vydání:	1987
Předmět:	Pharmacology chemistry.chemical_classification Dipeptide Arginine biology Cell growth Immunology Lysine General Medicine Toxicology In vitro Amino acid chemistry.chemical_compound chemistry Biochemistry biology.protein medicine Immunology and Allergy Thymopentin Thymopoietin medicine.drug
Zdroj:	Immunopharmacology and Immunotoxicology. 9:1-18
ISSN:	1532-2513 0892-3973
DOI:	10.3109/08923978709035198
Popis:	The effects of seventeen synthetic analogs of thymopentin (TP-5) have been studied in the active and azathioprine-inhibited E-rosette tests. Thymopentin was gradually shortened from the C terminus to peptides and single amino acids. Thymopoietin 32-34 (Arg-Lys-Asp-RGH-0205-TP-3) (II) and thymopoietin 32-35 (Arg-Lys-Asp-Val-RGH-0206-TP-4) (I) were the most active peptides. Dipeptide Arg-Lys produced significant stimulatory effect on azathioprine (ED75) inhibited E-receptor. Treatment of azathioprine (ED75)-inhibited E-rosette forming cells (ERFC) with arginine or especially lysine increased the number of ERFC. Some of TP-4 analogs decreased further the number of ERFC decreased by azathioprine ED30. These "suppressive" peptides as well as TP-3 caused a partial arrest of K 562 cell proliferation up to 96 hours. Results suggest that TP-5 is not the smallest active fragment of thymopoietins, since peptides (TP-3 and TP-4) exhibit similar or higher T-cell membrane activation on E-receptor. Arginine, lysine, and acidic aspartyl residue seem to be a necessary basic structure to produce a cumulative chemical signal on the activity of T-lymphocytes.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::17b62437960756f12a64b81f3bf9cb61 https://doi.org/10.3109/08923978709035198 Zobrazit plný text záznamu