Processing of hepatocyte growth factor to the heterodimeric form is required for biological activity

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Abstract
Hepatocyte growth factor is a plasminogen‐like molecule with diverse biological effects. Although it is synthesized as a single chain polypeptide, it was originally purified as a disulfide‐linked haterodimer which was generated by an internal proteolytic event. Subsequent work indicated that preparations consisting largely of the monomeric form also exhibited potent activity. By using a combination of protease inhibition and site‐directed mutagenesis, we established that conversion of the single chain polypeptide to the hoterodimer occurred during the bioassay and was required ror mitogenic and motogenic activity.