Inhibition of angiotensin converting enzyme by N-terminal fragments of substance P
| Autor: | Fraser M. Rogerson, Bruce G. Livett, D Scanlon, Frederick A. O. Mendelsohn |
|---|---|
| Rok vydání: | 1989 |
| Předmět: |
Male
Neuropeptide Peptide Substance P Angiotensin-Converting Enzyme Inhibitors Biology Peptide hormone Inhibitory postsynaptic potential Isozyme Cellular and Molecular Neuroscience chemistry.chemical_compound Endocrinology Animals Lung chemistry.chemical_classification Dose-Response Relationship Drug Endocrine and Autonomic Systems Angiotensin-converting enzyme Rats Inbred Strains General Medicine Corpus Striatum Peptide Fragments Rats Enzyme Neurology Biochemistry chemistry biology.protein |
| Zdroj: | Neuropeptides. 14(4) |
| ISSN: | 0143-4179 |
| Popis: | A range of N-terminal fragments of substance P (SP) were evaluated for inhibitory activity against angiotensin converting enzyme (ACE) from rat lung and brain (striatum). SP inhibited the enzyme from both sources in a concentration dependent manner (IC 50 30 μM). The N-terminal fragments SP[1–7], SP[1–6], SP[1–4] and SP[3–4] were equipotent with SP for both sources of the enzyme. However, SP[1–3] showed a difference in its activity, being more active than SP (IC 50 10 μM) in inhibiting the brain enzyme, but inactive against lung ACE. These results suggest that the inhibitory action of SP on ACE resides in the N-terminus of the peptide. The difference in reactivity towards SP[1–3] lends support to the idea that lung and brain ACE are different isozymes. |
| Databáze: | OpenAIRE |
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