Abstract
We have isolated cDNA clones from a Xenopus laevis embryo library that encode a predicted translation product of 342 amino acids containing a signal sequence for secretion. The predicted protein has 62-70% amino acid identity with the Xenopus oocyte cortical granule lectin (XCGL), the mouse intelectin, the human HL-1/intelectin and HL-2. Onset of gene expression occurs by gastrulation, and the transcripts localize in non-ciliated epidermal cells all over the tailbud embryos. The results suggest that the molecule, designated XEEL ( Xenopus embryonic epidermal lectin), is a novel XCGL family molecule secreted from the embryonic epidermis.
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