Schambony A, Hefele J, Gentzel M, Wilm M, Wedlich D (2003)
Publication Type: Journal article, Original article
Subtype: other
Publication year: 2003
Publisher: Elsevier Ireland Ltd
Book Volume: 120
Pages Range: 937-948
Journal Issue: 8
DOI: 10.1016/S0925-4773(03)00162-X
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.
APA:
Schambony, A., Hefele, J., Gentzel, M., Wilm, M., & Wedlich, D. (2003). A homologue of cysteine-rich secretory proteins induces premature degradation of vitelline envelopes and hatching of Xenopus laevis embryos. Mechanisms of Development, 120(8), 937-948. https://doi.org/10.1016/S0925-4773(03)00162-X
MLA:
Schambony, Alexandra, et al. "A homologue of cysteine-rich secretory proteins induces premature degradation of vitelline envelopes and hatching of Xenopus laevis embryos." Mechanisms of Development 120.8 (2003): 937-948.
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