The Activators of HGF

HGF is secreted as the inactive single chain form of pro-HGF, and is unable to exert any biological influence until it has been activated, via site-specific proteolytic cleavage, into the biologically active form of HGF (11, 85, 86). Activation occurs through the extracellular hydrolysis of the Arg494-Val495 peptide bond of pro-HGF. This cleavage generates the active 2-chain form of mature HGF. Once converted to this hetero-dimeric form, HGF is able to stimulate numerous responses, via c-Met stimulation in the target cells. HGF activator (HGFA) was originally thought to be the main serine protease responsible for the active HGF conversion (93, 94); however, several other factors have since demonstrated pro-HGF converting abilities. These enzymes include the hepato-cyte growth factor-converting enzyme (95), blood coagulation factor XIIa (96) and, albeit weakly, both types of plasminogen activator, uPA (urokinase-type) and tPA (tissue-type) (89, 97). Although, it appears HGFA appears to be a far more potent converter of pro-HGF to HGF than these enzymes (88). In recent years several other proteases have revealed a more potent pro-HGF converting ability; these include the proteases known as matriptase and hepsin (88, 90). However, the predominant converters of pro-HGF in the breast tissues are HGFA and matriptase, as these serine proteases process pro-HGF at a similar rate (98).

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