A homologue of cysteine-rich secretory proteins induces premature degradation of vitelline envelopes and hatching of Xenopus laevis embryos.
Mech Dev
; 120(8): 937-48, 2003 Aug.
Article
em En
| MEDLINE
| ID: mdl-12963113
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.
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Base de dados:
MEDLINE
Assunto principal:
Membrana Vitelina
/
Xenopus laevis
/
Glicoproteínas de Membrana
/
Proteínas de Xenopus
Idioma:
En
Ano de publicação:
2003
Tipo de documento:
Article
País de afiliação:
Alemanha