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Part of the book series: Serono Symposia USA Norwell, Massachusetts ((SERONOSYMP))

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Abstract

Hepatocyte growth factor (HGF) was originally detected in the circulation of hepatectomized animals on the basis of its ability to stimulate hepatocyte proliferation in another animal with an intact liver (1–3). It was purified from serum, plasma, or blood platelets in the form of a disulfide-linked heterodimer of ~ 60-kd heavy (alpha) and ~ 32-kd light (beta) polypeptide chains (1–3). HGF was independently isolated from the conditioned medium of cultured fibroblasts based on its mitogenic activity on a variety of cellular targets (4), or its ability to stimulate the dispersion of epithelial and vascular endothelial cells (5–7). These sources yielded a ~90-kd monomeric polypeptide that copurified with the aforementioned heterodimer (4–6). Analysis of these polypeptides and subsequent molecular cloning and recombinant expression of HGF revealed that it was synthesized and secreted in the monomeric ~90-kd form (4), and proteolytically converted to the disulfide-linked heterodimer. Several laboratories have shown that proteolytic conversion of the monomeric precursor to the heterodimer, which can occur in situ, is required for biologic activity (8–10). The strong affinity of HGF for heparin was exploited as a major enrichment step in many of the purification schemes (1–6, 11), and the interaction between HGF and this ubiquitous extracellular matrix component may play an important role in HGF sequestration and signaling, as has been demonstrated for members of the fibroblast growth factor family (reviewed in 12).

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Bottaro, D.P., Cioce, V., Chan, A.ML., Adams, D.H., Rubin, J.S. (1997). Hepatocyte Growth Factor. In: Ziegler, T.R., Pierce, G.F., Herndon, D.N. (eds) Growth Factors and Wound Healing. Serono Symposia USA Norwell, Massachusetts. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-1876-0_18

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  • DOI: https://doi.org/10.1007/978-1-4612-1876-0_18

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