Affordable Access

The molt-inhibiting hormone in the American crayfish Procambarus clarkii: its chemical synthesis and biological activity.

Authors
  • Sonobe, H
  • Nishimura, T
  • Sonobe, M
  • Nakatsuji, T
  • Yanagihara, R
  • Kawakami, T
  • Aimoto, S
Type
Published Article
Journal
General and comparative endocrinology
Publication Date
Feb 01, 2001
Volume
121
Issue
2
Pages
196–204
Identifiers
PMID: 11178885
Source
Medline
License
Unknown

Abstract

The molt-inhibiting hormone of the American crayfish Procambarus clarkii (Prc-MIH), a 75-residue polypeptide containing three disulfide bridges, was synthesized by chemical ligation of two peptides, i.e., synthetic Prc-MIH(1-39) and Prc-MIH(40-75)-NH(2), and by subsequent folding to form the native disulfide-containing peptide molecule. The synthetic peptide was comparable to the natural Prc-MIH in inhibiting ecdysteroid secretion by in vitro bioassay and shared features with the natural Prc-MIH in some biochemical analyses. These results indicate that the chemical ligation method can be used for the synthesis of Prc-MIH. Furthermore, it was demonstrated that synthetic Prc-MIH has hyperglycemic activity, although the activity was weaker than that of the authentic crustacean hyperglycemic hormone in the American crayfish. To examine the structural requirement of the Prc-MIH for eliciting biological activity, an antibody raised against the C-terminal region (residues 55-75) and two synthetic peptides, i.e., a core region (residues 1-54) containing three disulfide bridges and the C-terminal region, were utilized. It is suggested that Prc-MIH exerts its activities through coordination between the core region and the C-terminal region.

Report this publication

Statistics

Seen <100 times