Peptide analogs of thymopentin distinguish distinct thymopoietin receptor specificities on two human T cell lines
| Autor: | George Heavner, Tapan Audhya, Gideon Goldstein |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
Physiology
T-Lymphocytes T cell Clinical Biochemistry Guanosine Monophosphate Thymopoietins Peptide Biology Biochemistry Pentapeptide repeat Cell Line Cellular and Molecular Neuroscience Endocrinology hemic and lymphatic diseases medicine Humans Thymopentin Thymopoietin Receptor chemistry.chemical_classification Tetrapeptide Ligand (biochemistry) Guanine Nucleotides Peptide Fragments Thymus Hormones medicine.anatomical_structure chemistry biology.protein medicine.drug |
| Zdroj: | Regulatory Peptides. 27:257-262 |
| ISSN: | 0167-0115 |
| Popis: | Thymopoietin, a polypeptide hormone of the thymus, and the synthetic pentapeptide thymopentin, corresponding to thymopoietin 32–36 , both induced elevations of intracellular cyclic GMP in two human T cell lines, CEM and MOLT-4. In contrast, the closely related polypeptide thysplenin, which differs from thymopoietin at position 34, induced intracellular cyclic GMP elevation in MOLT-4 but not in CEM. We synthesized a series of penta- and tetrapeptide analogs of amino acids 32–36 of human thymopoietin and thysplenin, and now show that distinct patterns of activity can be obtained in these small peptides, with selectivity for cyclic GMP elevation in MOLT-4 alone or CEM alone. This suggests that the thymopoietin receptors (TPR) on these two human T cell lines are distinguishable by their differing ligand specificities, and we have termed them α TPR and β TPR for CEM and MOLT-4 receptors, respectively. |
| Databáze: | OpenAIRE |
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