Angiotensin IV displays only low affinity for native insulin-regulated aminopeptidase (IRAP).
Fundam Clin Pharmacol
; 26(2): 194-7, 2012 Apr.
Article
em En
| MEDLINE
| ID: mdl-21477268
ABSTRACT
Radioligand binding studies revealed that Ang IV binds to insulin-regulated aminopeptidase (IRAP)/'AT(4) receptors' with high affinity. Yet, as these experiments were routinely carried out in the presence of chelators, only the catalytic zinc-depleted apo-form of IRAP was labelled. While the chelators remove the catalytic zinc from IRAP and protect Ang IV from proteolytic degradation, the aminopeptidase N selective inhibitor '7B' only exerts the latter effect. By using 7B along with the new stable Ang IV-analog [(3) H]AL-11, we here show that the native enzyme is only a low-affinity target for Ang IV.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Compostos Organofosforados
/
Cistinil Aminopeptidase
/
Tirosina
/
Angiotensina II
/
Quelantes
Limite:
Animals
Idioma:
En
Revista:
Fundam Clin Pharmacol
Assunto da revista:
FARMACOLOGIA
Ano de publicação:
2012
Tipo de documento:
Article
País de afiliação:
Bélgica