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Titolo:
PROTEOLYSIS AT THE SECRETASE AND AMYLOIDOGENIC CLEAVAGE SITES OF THE BETA-AMYLOID PRECURSOR PROTEIN BY ACETYLCHOLINESTERASE AND BUTYRYLCHOLINESTERASE USING MODEL PEPTIDE-SUBSTRATES
Autore:
DESERRES M; SHERMAN D; CHESTNUT W; MERRILL BM; VIVEROS OH; DILIBERTO EJ;
Indirizzi:
BURROUGHS WELLCOME CO,DIV PHARMACOL,DIV PHARMACOKINET & DRUG METAB,BIOANALYT CHEM METAB SECT RES TRIANGLE PK NC 27709 BURROUGHS WELLCOME CO,DIV ORGAN CHEM RES TRIANGLE PK NC 27709
Titolo Testata:
Cellular and molecular neurobiology
fascicolo: 3, volume: 13, anno: 1993,
pagine: 279 - 287
SICI:
0272-4340(1993)13:3<279:PATSAA>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRYPSIN-LIKE ACTIVITY;
Keywords:
ALZHEIMERS DISEASE; BETA-AMYLOID PRECURSOR PROTEIN; ACETYLCHOLINESTERASE; BETA/A4-PEPTIDE; SECRETASE; AMYLOIDOSIS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
9
Recensione:
Indirizzi per estratti:
Citazione:
M. Deserres et al., "PROTEOLYSIS AT THE SECRETASE AND AMYLOIDOGENIC CLEAVAGE SITES OF THE BETA-AMYLOID PRECURSOR PROTEIN BY ACETYLCHOLINESTERASE AND BUTYRYLCHOLINESTERASE USING MODEL PEPTIDE-SUBSTRATES", Cellular and molecular neurobiology, 13(3), 1993, pp. 279-287

Abstract

1. It was recently proposed that acetylcholinesterase (AChE), in addition to its esteratic activity, has proteolytic activity such that it may cleave the beta-amyloid precursor (beta-APP) within the beta-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 of beta-APP. 2. The ability ofvarious preparations of AChE and BuChE to hydrolyze two synthetic fragments of beta-APP695 as model substrates containing the normal and aberrant cleavage sites was studied. 3. Digestion of these synthetic substrates with commercial preparations of Electrophorus electricus AChE indicated the presence of a trypsin-like proteolytic activity cleavingeach 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 to beta-pancreatic trypsin. 6. These data indicate that the proteinase activity found in these commercial preparations of AChE is due to contamination with trypsin.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/11/20 alle ore 21:03:22