Identification of molting fluid carboxypeptidase A (MF-CPA) in Bombyx mori

Comp Biochem Physiol B Biochem Mol Biol. 2005 Jul;141(3):314-22. doi: 10.1016/j.cbpc.2005.04.005.

Abstract

Using microarray analyses, we identified carboxypeptidase A (MF-CPA), which was induced during pupal ecdysis in the wing discs of Bombyx mori. Here, we report the functional characterization of MF-CPA. MF-CPA has amino acid sequence similarities with the proteins in the carboxypeptidase A/B subfamily, from human to nematode. The MF-CPA gene is expressed during the molting periods in the epithelial tissues. MF-CPA is detected in the molting fluid, which fills the space between the old and new cuticle during molting. By Western blot analysis, we show that MF-CPA is secreted as a zymogen and processed in the molting fluid. Recombinant MF-CPA expressed in the insect cells has carboxypeptidase A activity. We propose that MF-CPA degrades the proteins from the old cuticle during the molting periods and contributes to recycling of the amino acids.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Baculoviridae
  • Bombyx / enzymology*
  • Bombyx / genetics
  • Bombyx / growth & development*
  • Carboxypeptidases A / genetics
  • Carboxypeptidases A / immunology
  • Carboxypeptidases A / metabolism*
  • Chromatography, High Pressure Liquid
  • Gene Expression Regulation, Developmental*
  • Larva / enzymology
  • Molecular Sequence Data
  • Molting / physiology*
  • Phylogeny
  • Rabbits
  • Recombinant Proteins / genetics
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism
  • Reverse Transcriptase Polymerase Chain Reaction
  • Sequence Homology, Amino Acid

Substances

  • Recombinant Proteins
  • Carboxypeptidases A