Proteolysis at the secretase and amyloidogenic cleavage sites of the beta-amyloid precursor protein by acetylcholinesterase and butyrylcholinesterase using model peptide substrates
| Autor: | Barbara M. Merrill, Emanuel J. Diliberto, M. de Serres, O. H. Viveros, D. Sherman, W. G. Chestnut |
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| Rok vydání: | 1993 |
| Předmět: |
Proteolysis
Molecular Sequence Data Peptide Chromatography Affinity Cellular and Molecular Neuroscience chemistry.chemical_compound Amyloid beta-Protein Precursor Affinity chromatography Endopeptidases medicine Animals Trypsin Amino Acid Sequence Butyrylcholinesterase chemistry.chemical_classification biology medicine.diagnostic_test Cell Biology General Medicine Acetylcholinesterase Peptide Fragments Enzyme chemistry Biochemistry Electrophorus biology.protein Amyloid Precursor Protein Secretases Artifacts Amyloid precursor protein secretase Sequence Alignment medicine.drug |
| Zdroj: | Cellular and molecular neurobiology. 13(3) |
| ISSN: | 0272-4340 |
| Popis: | 1. It was recently proposed that acetylcholinesterase (AChE), in addition to its esteratic activity, has proteolytic activity such that it may cleave theβ-amyloid precursor (β-APP) within theβ-amyloid sequence. The purpose of this paper was to examine further whether AChE or butyrylcholinesterase (BuChE) had associated proteinase activity that was involved in the metabolism ofβ-APP. 2. The ability of various preparations of AChE and BuChE to hydrolyze two synthetic fragments ofβ-APP695 as model substrates containing the normal and aberrant cleavage sites was studied. 3. Digestion of these synthetic substrates with commercial preparations ofElectrophorus electricus AChE indicated the presence of a trypsin-like proteolytic activity cleaving each peptide at the carboxy-terminal side of an internal lysine residue. 4. Purification of the trypsin-like proteinase activity by aminobenzamidine affinity chromatography yielded a preparation that was devoid of AChE activity but retained all of the proteinase activity. 5. Amino-terminal sequence analysis of this preparation showed that the first 13 amino acid residues were identical toβ-pancreatic trypsin. 6. These data indicate that the proteinase activity found in these commercial preparations of AChE is due to contamination with trypsin. |
| Databáze: | OpenAIRE |
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