HCE, a constituent of the hatching enzymes of Oryzias latipes embryos, releases unique proline‐rich polypeptides from its natural substrate, the hardened chorion
- 21 February 1994
- journal article
- Published by Wiley in FEBS Letters
- Vol. 339 (3) , 281-284
- https://doi.org/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 γ-glutamyi ϵ-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.Keywords
This publication has 10 references indexed in Scilit:
- Isolation of cDNAs for LCE and HCE, two constituent proteases of the hatching enzyme of Oryzias latipes, and concurrent expression of their mRNAs during developmentDevelopmental Biology, 1992
- Molecular and Cellular Basis of Formation, Hardening, and Breakdown of the Egg Envelope in FishPublished by Elsevier ,1992
- Analysis of Hardening of the Egg Envelope (Chorion) of the Fish, Oryzias latipesDevelopment, Growth & Differentiation, 1991
- The major structural proteins of cod (Gadus morhua) eggshells and protein crosslinking during teleost egg hardeningDevelopmental Biology, 1990
- A unique proteolytic action of HCE, a constituent protease of a fish hatching enzyme: Tight binding to its natural substrate, egg envelopeBiochemical and Biophysical Research Communications, 1989
- Isolation and Some Properties of Low Choriolytic Enzyme (LCE), a Component of the Hatching Enzyme of the Teleost, Oryzias latipes1The Journal of Biochemistry, 1989
- Purification and Partial Characterization of High Choriolytic Enzyme (HCE), a Component of the Hatching Enzyme of the Teleost, Oryzias latipes1The Journal of Biochemistry, 1989
- Major glycoproteins solubilized from the teleostean egg membrane by the action of the hatching enzymeBiochimica et Biophysica Acta (BBA) - Protein Structure, 1976
- Zum Vorkommen von Isopeptidbindungen in der Eihülle der Regenbogenforelle(Salmo gairdneriRich.)Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1976
- Isolation of a choriolytic enzyme (hatching enzyme) of the teleost, Oryzias latipesDevelopmental Biology, 1972