A homologue of cysteine-rich secretory proteins induces premature degradation of vitelline envelopes and hatching of Xenopus laevis embryos
Research output: Contribution to journal › Research article › Contributed › peer-review
Contributors
Abstract
We cloned Xenopus laevis CRISP, XCRISP, a homologue of the mammalian family of cysteine-rich secretory proteins (CRISPs), which has been previously identified as a Wnt3a/noggin responsive gene in an expression screen [Mech. Dev. 87 (1999) 21]. We detected XCRISP expression exclusively in the hatching gland. XCRISP enters the secretory pathway and accumulates on the surface of presumptive hatching gland cells. Overexpression studies of XCRISP and XCRISP-mutants show that XCRISP induces premature hatching of embryos preceded by degradation of the vitelline envelope. A deletion mutant that lacks a 35 amino acid domain even accelerates hatching, while further deletion of the carboxy-terminus reverses these effects. From our studies, we conclude that XCRISP is sufficient to induce degradation of vitelline envelopes and that this activity maps to the most C-terminal amino acids, while the adjacent domain regulates XCRISP activity.
Details
Original language | English |
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Pages (from-to) | 937-948 |
Number of pages | 12 |
Journal | Mechanisms of Development |
Volume | 120 |
Issue number | 8 |
Publication status | Published - Aug 2003 |
Peer-reviewed | Yes |
Externally published | Yes |
External IDs
PubMed | 12963113 |
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ORCID | /0000-0002-4482-6010/work/142251045 |
Keywords
ASJC Scopus subject areas
Keywords
- Cysteine-rich secretory proteins, Hatching gland, Xenopus laevis CRISP