The epidermal growth factor receptor (EGFR) is an important receptor tyrosine kinase member in animals, which plays versatile functions in development, growth, tissue regeneration etc. Current knowledge on EGFR is poor in bivalve mollusks. In this study, we cloned and analyzed an EGFR gene from the Pacific oyster Crassostrea gigas (cgegfr). A 5,731 bp full-length cDNA of cgegfr was obtained, encoding a peptide with 1,494 amino acids which exhibited a typical EGFR structure, including an extracellular region, a single transmembrane region and an intracellular region. A conserved tyrosine kinase domain was predicted in the intracellular region, while the extracellular region responsible for ligand binding showed ... More
The epidermal growth factor receptor (EGFR) is an important receptor tyrosine kinase member in animals, which plays versatile functions in development, growth, tissue regeneration etc. Current knowledge on EGFR is poor in bivalve mollusks. In this study, we cloned and analyzed an EGFR gene from the Pacific oyster Crassostrea gigas (cgegfr). A 5,731 bp full-length cDNA of cgegfr was obtained, encoding a peptide with 1,494 amino acids which exhibited a typical EGFR structure, including an extracellular region, a single transmembrane region and an intracellular region. A conserved tyrosine kinase domain was predicted in the intracellular region, while the extracellular region responsible for ligand binding showed comparatively poor conservation. Expression analysis revealed that cgefgr was expressed widely in C. gigas tissues and a highest expression level was observed in adductor tissue. Expression of cgegfr was revealed to be up-regulated during wound healing of mantle, indicating that EGFR might function in the cell proliferation and migration during wound healing. Further functional analysis of cgegfr was conducted in mouse myoblast cell line C2C12, in which different parts of cgegfr were expressed and their effects were measured. The results revealed that cgegfr was able to accelerate cell proliferation of C2C12 cells and the transmembrane region was necessary for self-activation of truncated cgegfr. Our results would provide supports for further studies on the roles of cgegfr in development and growth in C. gigas.
