| Registro completo |
| Provedor de dados: |
BJMBR
|
| País: |
Brazil
|
| Título: |
A new brain metalloendopeptidase which degrades the Alzheimer ß-amyloid 1-40 peptide producing soluble fragments without neurotoxic effects
|
| Autores: |
Carvalho,K.M.
França,M.S.F.
Camarão,G.C.
Ruchon,A.F.
|
| Data: |
1997-10-01
|
| Ano: |
1997
|
| Palavras-chave: |
Brain metalloendopeptidase
Alzheimer ß-amyloid 1-40 peptide
Alzheimer's disease
|
| Resumo: |
A new metalloendopeptidase was purified to apparent homogeneity from a homogenate of normal human brain using successive steps of chromatography on DEAE-Trisacryl, hydroxylapatite and Sephacryl S-200. The purified enzyme cleaved the Gly33-Leu34 bond of the 25-35 neurotoxic sequence of the Alzheimer ß-amyloid 1-40 peptide producing soluble fragments without neurotoxic effects. This enzyme activity was only inhibited by divalent cation chelators such as EDTA, EGTA and o-phenanthroline (1 mM) and was insensitive to phosphoramidon and captopril (1 µM concentration), specific inhibitors of neutral endopeptidase (EC 3.4.24.11) and angiotensin-converting enzyme (EC 3.4.15.1), respectively. The high affinity of this human brain endopeptidase for ß-amyloid 1-40 peptide (Km = 5 µM) suggests that it may play a physiological role in the degradation of this substance produced by normal cellular metabolism. It may also be hypothesized that the abnormal accumulation of the amyloid ß-protein in Alzheimer's disease may be initiated by a defect or an inactivation of this enzyme.
|
| Tipo: |
Info:eu-repo/semantics/article
|
| Idioma: |
Inglês
|
| Identificador: |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1997001000002
|
| Editor: |
Associação Brasileira de Divulgação Científica
|
| Relação: |
10.1590/S0100-879X1997001000002
|
| Formato: |
text/html
|
| Fonte: |
Brazilian Journal of Medical and Biological Research v.30 n.10 1997
|
| Direitos: |
info:eu-repo/semantics/openAccess
|
