Formation of acetyl-Ser-Asp-Lys-Pro, a new regulator of the hematopoietic system, through enzymatic processing of thymosin beta 4
| Autor: | K.-J. Rieger, M. Lenfant, D. Sotty, Catherine Grillon, Joanna Wdzieczak-Bakala |
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| Přispěvatelé: | Institut de Chimie des Substances Naturelles (ICSN), Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC), inconnu, Inconnu |
| Jazyk: | angličtina |
| Rok vydání: | 1991 |
| Předmět: |
[SDV]Life Sciences [q-bio]
Molecular Sequence Data Regulator Cleavage (embryo) Flavobacterium General Biochemistry Genetics and Molecular Biology History and Philosophy of Science Bone Marrow Endopeptidases medicine Animals Amino Acid Sequence Peptide sequence Chromatography High Pressure Liquid chemistry.chemical_classification Tetrapeptide General Neuroscience Serine Endopeptidases Hematopoiesis Thymosin beta-4 Thymosin Haematopoiesis Kinetics Enzyme medicine.anatomical_structure Biochemistry chemistry Bone marrow Rabbits Prolyl Oligopeptidases Oligopeptides |
| Zdroj: | Annals of the New York Academy of Sciences Annals of the New York Academy of Sciences, Wiley, 1991, 628, pp.115-25 |
| ISSN: | 0077-8923 1749-6632 |
| Popis: | International audience; The demonstration that AcSDKP, a new regulator of the hematopoietic system, is formed in the bone marrow by a one-step enzymatic maturation processing of thymosin beta 4 (T beta 4) is presented. AcSDKP and T beta 4 were both detected in bone marrow cells (BMC). Incubation of [3H]T beta 4 with either intact or lysed BMC led to the formation of [3H]AcSDKP, whereas the labeled tetrapeptide was not degraded under these conditions. Model enzymatic degradation of T beta 4 carried out with bacterial enzymes suggests that a mammalian endoproteinase Asp-N might be involved in the formation of AcSDKP through the specific cleavage of the Pro4-Asp5 peptidic bond of T beta 4. In contrast, alpha-prolyl-endopeptidase was ineffective in carrying out a similar processing. |
| Databáze: | OpenAIRE |
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