fig2

Figure 2. (A) Structure of HGF consisting of a α-chain (69 kDa) including four Kringle domains and a β-chain (43 kDa) including a serine proteinase homology (SPH) domain, linked by disulfide bonds (S). High affinity binding sites are located at the N-terminal domain and the first Kringle domain of the α-chain; (B) Structure and basic functions of the Met receptor consisting of a α-chain (50 kDa) and a β-chain (140 kDa) linked by disulfide bonds. HGF binds to the Met receptor resulting in tyrosine phosphorylation leading to the activation of a number of biological activities including those listed plus anti-neuroinflammation and oxidative stress, increased cerebral blood flow and synaptogenesis, and facilitated long-term potentiation and memory. HGF: hepatocyte growth factor