Abstract：
:Human atrial natriuretic peptide (Ser 99-Tyr 126) was rapidly degraded by both choroid plexus and hypothalamic membranes with a complex pattern of cleavage. The use of protease inhibitors allowed a preliminary characterization of the enzymes involved in the hydrolysis of the Ser-Phe and Phe-Arg bonds of iodine-labelled atrial natriuretic peptide. The C-terminal tripeptide was generated by three different enzymatic activities acting on the Ser-Phe bond: endopeptidase 24.11, a phosphoramidon-insensitive metallopeptidase and a thiol protease. Peptides like substance P, neurotensin, bradykinin inhibited the cleavage of the Ser-Phe bond of atrial natriuretic peptide. The C-terminal tripeptide was further degraded by aminopeptidases. Cleavage of the C-terminal dipeptide was inhibited by aprotinin, suggesting the contribution of brain kallikrein in the formation of this metabolite. These results show that many different proteases were involved in the hydrolysis of the C-terminal sequence of atrial natriuretic peptide, at least in vitro and underline the complexity of neuropeptide catabolism by brain preparations.
journal_name
Neurochem Intjournal_title
Neurochemistry internationalauthors
Deschodt-Lanckman M,Vanneste Y,Michaux Fdoi
10.1016/0197-0186(88)90176-3subject
Has Abstractpub_date
1988-01-01 00:00:00pages
367-73issue
3eissn
0197-0186issn
1872-9754pii
0197-0186(88)90176-3journal_volume
12pub_type
杂志文章abstract：:The present study was carried out to clarify whether the imidazolines clonidine, moxonidine and cirazoline as well as the guanidine aganodine inhibit noradrenaline release in the rat and rabbit brain via imidazoline receptors, alpha 2-adrenoceptors and/or histamine H3 receptors. Slices or synaptosomes from the rat or ...
journal_title：Neurochemistry international
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journal_title：Neurochemistry international
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