Degradation of human atrial natriuretic peptide by human brain membranes.

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 Int

authors

Deschodt-Lanckman M,Vanneste Y,Michaux F

doi

10.1016/0197-0186(88)90176-3

subject

Has Abstract

pub_date

1988-01-01 00:00:00

pages

367-73

issue

3

eissn

0197-0186

issn

1872-9754

pii

0197-0186(88)90176-3

journal_volume

12

pub_type

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