ArticleLife science alliance2022
Dimerization of kringle 1 domain from hepatocyte growth factor/scatter factor provides a potent MET receptor agonist.
Article in Life science alliance, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- Towards Cost-Effective and Sustainable Media Formulations for Terrestrial and Aquatic Cellular Agriculture.Foods (Basel, Switzerland) · 2026Review
- Development, Expansion, and Histological Characterization of Patient-Derived Liver Organoids for Drug Screening and Disease Modeling.Bio-protocol · 2026Article
- Intervention Potential of a Recombinant Tarim Red Deer HGF Protein in a Mouse Model of Alcoholic Liver Disease.Biology · 2025Article
- Redox-Controlled Chemical Protein Synthesis: Sundry Shades of Latency.Accounts of chemical research · 2022Article
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Authors and funding
14 authors.
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Abstract
Hepatocyte growth factor/scatter factor (HGF/SF) and its cognate receptor MET play several essential roles in embryogenesis and regeneration in postnatal life of epithelial organs such as the liver, kidney, lung, and pancreas, prompting a strong interest in harnessing HGF/SF-MET signalling for regeneration of epithelial organs after acute or chronic damage. The limited stability and tissue diffusion of native HGF/SF, however, which reflect the tightly controlled, local mechanism of action of the morphogen, have led to a major search of HGF/SF mimics for therapy. In this work, we describe the rational design, production, and characterization of K1K1, a novel minimal MET agonist consisting of two copies of the kringle 1 domain of HGF/SF in tandem orientation. K1K1 is highly stable and displays biological activities equivalent or superior to native HGF/SF in a variety of in vitro assay systems and in a mouse model of liver disease. These data suggest that this engineered ligand may find wide applications in acute and chronic diseases of the liver and other epithelial organs dependent of MET activation.
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