Identification of cellular recognition sequence of epimorphin and critical role of cell/epimorphin interaction in lung branching morphogenesis

Biochemical and Biophysical Research Communications
S Koshida, Y Hirai

Abstract

A mesenchymal protein, epimorphin, is known to bind directly to the cell surface through its central portion and to act as a signaling molecule for epithelial morphogenesis. Utilizing several recombinant polypeptides and synthetic peptides, we identified the cellular recognition sequence of epimorphin in the central portion of this molecule (amino acids 105-123, NGNRTSVDLRIRRTQHSVL; termed NL-peptide sequence). Interestingly, although a model cell type bound to the NL-peptide as strong as to the full-length epimorphin, this peptide itself didn't induce the cellular functional responses so far tested. We found that the NL-peptide behaved as an antagonist for the endogenous epimorphin and severely perturbed lung branching morphogenesis in organ culture. These results not only revealed a part of the functional mechanism of epimorphin but also demonstrated that cell/ epimorphin interaction through the NL-peptide sequence is a critical step for lung epithelial morphogenesis.

References

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Citations

Jul 31, 2003·Trends in Cell Biology·Derek C RadiskyMina J Bissell
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