Purification from human plasma of a hexapeptide that potentiates the sulfation and mitogenic activities of insulin-like growth factors
| Autor: | Pierre Nabet, Brigitte Dousset, J. Capiaumont, J. Straczek, Fatima Maachi, Dung Le Nguyen, Francine Belleville, Christine Jacob |
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| Rok vydání: | 1998 |
| Předmět: |
medicine.medical_treatment
Biophysics Peptide Tripeptide Chick Embryo Biology Biochemistry Pentapeptide repeat Mass Spectrometry Sulfation Somatomedins Small peptide medicine Animals Humans Insulin-Like Growth Factor I Growth Substances Molecular Biology chemistry.chemical_classification Sulfates Insulin Embryo Cell Biology Complement C3 Peptide Fragments Cartilage chemistry Human plasma Complement C3b Mitogens Peptides Sequence Analysis |
| Zdroj: | Biochemical and biophysical research communications. 247(3) |
| ISSN: | 0006-291X |
| Popis: | The human plasma contains small peptide molecules known as low molecular weight growth factors synergistically increasing certain biological actions of insulin-like growth factors. In the present work we isolated and characterized a hexapeptide with HWESAS as structure. This purified peptide was absolutely necessary for the sulfation activity of insulin-like growth factor-I on chick embryo pelvic cartilages and improved the mitogenic activity of both insulin-like growth factors. The effects of this hexapeptide were confirmed by using the homologous synthetic peptide, that exhibited similar biological effects. Other synthetic peptides with structure derived from hexapeptide were shown to be active: the pentapeptide HWESA appeared more potent than the tripeptide HWE, which is about 170 to 200 times less active than the hexapeptide. The sequence of hexapeptide HWESAS is identified in only one human protein that is C3f, a fragment of C3 complement. |
| Databáze: | OpenAIRE |
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