Binding of vasoactive intestinal polypeptide to dispersed enterocytes results in rapid removal of the NH2-terminal histidyl residue

Roland Nau, Manfred Ballmann, J. Michael Conlon

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)

Abstract

Specific binding sites for 125I-labelled vasoactive intestinal polypeptide (VIP) (half-maximal inhibition at 1.5 ± 0.2 nM VIP) were identified on dispersed porcine enterocytes. Radioactivity bound to the cell surface was internalized. At 37 ° C, a steady state was achieved after 45 min with a ratio of internalized to cell surface-bound radioactivity of approximately 1:2 but at 10 ° C, no radioactivity appeared intracellularly. Incubation of VIP with cells in the absence of inhibitors of proteolysis for as short a time as 30 s at 37 °C led to the formation of [des-His1]VIP by the action of amastatin- and bestatin-sensitive aminopeptidase(s). This metabolite was formed in the presence of sodium azide and when incubations were performed at 10°C suggesting that internalization was not a prerequisite for degradation. As [des-His1]-VIP has only 1% of the bioactivity of VIP, formation of this metabolite will effectivily terminate the action of VIP in the epithelial layer of the intestine.

Original languageEnglish
Pages (from-to)97-103
Number of pages7
JournalMolecular and Cellular Endocrinology
Volume52
Issue number1-2
DOIs
Publication statusPublished - Jul 1987
Externally publishedYes

Keywords

  • Aminopeptidase
  • Endopeptidase 24.11
  • Enterocyte

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Endocrinology

Fingerprint

Dive into the research topics of 'Binding of vasoactive intestinal polypeptide to dispersed enterocytes results in rapid removal of the NH2-terminal histidyl residue'. Together they form a unique fingerprint.

Cite this