Peptidyl dipeptidase A-catalyzed metabolism of delta sleep-inducing peptide in bovine brain microvessel endothelial cells: a cell culture model of the blood brain barrier
| Autor: | Ronald T. Borchardt, Augustijns Pf, Williams Tm, Ng Ky |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
Dipeptidase
Molecular Sequence Data Biophysics Peptide Tripeptide Peptidyl-Dipeptidase A Spectrometry Mass Fast Atom Bombardment Blood–brain barrier Biochemistry Tripeptidase activity Delta Sleep-Inducing Peptide medicine Animals Amino Acid Sequence Molecular Biology Microvessel Peptide sequence Cells Cultured Chromatography High Pressure Liquid chemistry.chemical_classification biology Microcirculation Models Cardiovascular Cell Biology Molecular biology Peptide Fragments medicine.anatomical_structure chemistry Blood-Brain Barrier Cerebrovascular Circulation biology.protein Delta sleep-inducing peptide Cattle Endothelium Vascular |
| Zdroj: | Biochemical and biophysical research communications. 210(3) |
| ISSN: | 0006-291X |
| Popis: | Previous studies have shown that the metabolism of delta sleep-inducing peptide (DSIP) in the blood-brain barrier (BBB) is catalyzed by amino-peptidases. In this study, we have shown that peptidyl dipeptidase A in cultured bovine brain microvessel endothelial cells (BBMEC), a model of the BBB, and a purified form of this enzyme can also metabolize DSIP by sequential hydrolyses of dipeptides or tripeptides from the carboxyl terminus of this nonapeptide. Both the dipeptidase and tripeptidase activity associated with peptidyl dipeptidase A can be inhibited by captopril. Total stabilization of DSIP to metabolism in BBMEC could be achieved by inclusion of an inhibitor of peptidyl dipeptidase A (e.g., captopril) and an inhibitor of aminopeptidases (e.g., bestatin). |
| Databáze: | OpenAIRE |
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