HCE, a constituent of the hatching enzymes of Oryzias latipes embryos, releases unique proline-rich polypeptides from its natural substrate, the hardened chorion

FEBS Lett. 1994 Feb 21;339(3):281-4. doi: 10.1016/0014-5793(94)80431-1.

Abstract

HCE, a constituent protease of the hatching enzymes of Oryzias latipes embryos [1,2], releases unique proline-rich polypeptides from its natural substrate, the hardened chorion. The polypeptides consist of repeats of Pro-X-Y, mainly Pro-Glx-X. In addition, the polypeptides contain abundant gamma-glutamyl epsilon-lysine isopeptides which are regarded to be responsible for chorion hardening. These findings suggest that HCE recognizes specific site(s) of the chorion, releases the proline-rich polypeptides from it, and makes the substrate accessible to LCE, another protease of the hatching enzymes.

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / analysis
  • Animals
  • Chorion / metabolism*
  • Chromatography, Gel
  • Metalloendopeptidases / metabolism*
  • Molecular Sequence Data
  • Molecular Weight
  • Oryzias / embryology*
  • Peptides / analysis
  • Peptides / chemistry
  • Peptides / metabolism*
  • Proline / analysis*
  • Repetitive Sequences, Nucleic Acid

Substances

  • Amino Acids
  • Peptides
  • Proline
  • Metalloendopeptidases
  • envelysin