HGF, also known as scatter factor and hepatopoietin A, is a pleiotropic protein in the plasminogen subfamily of S1 peptidases. It is a multidomain molecule that includes an N-terminal PAN/APPLE‑like domain, four Kringle domains, and a serine proteinase-like domain that has no detectable protease activity (1 - 4). Canine HGF is secreted as an inactive 699 amino acid (aa) single chain propeptide. It is cleaved after the fourth Kringle domain by a serine protease to form bioactive disulfide-linked HGF with a 60 kDa alpha and 30 kDa beta chain. A variant of HGF with a 5 aa deletion in the first Kringle domain has been described in canine and other species (5). Canine HGF shares 97%, 99%, 93%, 93%, and 89% aa sequence identity with bovine, feline, human, mouse, and rat HGF, respectively. HGF binds heparan-sulfate proteoglycans and the widely expressed receptor tyrosine kinase, HGF R/c-MET (6, 7). HGF‑dependent c-MET activation is implicated in the development of many human cancers (8). HGF regulates epithelial morphogenesis by inducing cell scattering and branching tubulogenesis (9, 10). HGF induces the up‑regulation of integrin alpha 2 beta 1 in epithelial cells by a selective increase in alpha 2 gene transcription (11). This integrin serves as a collagen I receptor, and its blockade disrupts epithelial cell branching tubulogenesis (11, 12). HGF can also alter epithelium morphology by the induction of nectin‑1 alpha ectodomain shedding, an adhesion protein component of adherens junctions (13). In the thyroid, HGF induces the proliferation, motility, and loss of differentiation markers of thyrocytes and inhibits TSH-stimulated iodine uptake (14). HGF promotes the motility of cardiac stem cells in damaged myocardium (15).
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