Full-length and N-terminally truncated chicken intestinal diazepam- binding inhibitor. Purification, structural characterization and influence on insulin release

Zheng Wang Chen, Tomas Bergman, Hans Jörnvall, Valentina Bonetto, Åke Norberg, Viktor Mutt, Patrizia Longone, Erminio Costa, Suad Efendic, Claes Göran Östenson

Research output: Contribution to journalArticle

Abstract

Two forms of diazepam-binding inhibitor (DBI) have been purified from chicken intestine and identified as the intact avian polypeptide (residues 1- 86) and a truncated variant (residues 35-86). At 10 nM concentration, both the intact and the truncated peptide suppress in vitro-monitored glucose induced insulin release by 50 (p <0.02) and 64% (p <0.01), respectively. The truncation starts at a segment, -Thr-Val-Gly-Asp-, that is strictly conserved between characterized DBI species, indicating special restrictions on the structure. However, overall DBI conservation appears to be complex. A number of differently bioactive fragments with separate processings and tissue distributions have been observed, suggesting multiple functions of DBI and its sub-segments.

Original languageEnglish
Pages (from-to)63-68
Number of pages6
JournalRegulatory Peptides
Volume69
Issue number2
DOIs
Publication statusPublished - Mar 26 1997

Keywords

  • Avian DBI
  • Insulin release
  • Peptide multiplicity
  • Polymer
  • Processed peptide

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology
  • Physiology
  • Neuroscience(all)

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