ArticleThe Biochemical journal2005
Activation of hepatocyte growth factor by urokinase-type plasminogen activator is ionic strength-dependent.
Article in The Biochemical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- The Adipokine Hypothesis of Heart Failure With a Preserved Ejection Fraction: A Novel Framework to Explain Pathogenesis and Guide Treatment.Journal of the American College of Cardiology · 2025Review
- Role of mitogens in normal and pathological liver regeneration.Hepatology communications · 2025Review
- E4 engages uPAR and enolase-1 and activates urokinase to exert antifibrotic effects.JCI insight · 2021Article
- Ah Receptor Pathway Intricacies; Signaling Through Diverse Protein Partners and DNA-Motifs.Toxicology research · 2015Article
- Herbal compound triptolide synergistically enhanced antitumor activity of amino-terminal fragment of urokinase.Molecular cancer · 2013Article
- Coexpression of Smad7 and UPA attenuates carbon tetrachloride-induced rat liver fibrosis.Medical science monitor : international medical journal of experimental and clinical research · 2012Article
- Regulation of proteinases during mouse peri-implantation development: urokinase-type plasminogen activator expression and cross talk with matrix metalloproteinase 9.Reproduction (Cambridge, England) · 2011Article
- Urokinase-type plasminogen activator supports liver repair independent of its cellular receptor.BMC gastroenterology · 2006Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The hepatocyte growth factor (HGF) is a multifunctional cytokine that is produced as latent scHGF (single chain HGF). Various proteases reportedly cleave scHGF to generate the active two-chain form (HGF), including u-PA (urokinase-type plasminogen activator), t-PA (tissue-type plasminogen activator), kallikrein, Factor XIa, Factor XIIa, HGF activator and matriptase. Considerable evidence indicates that, in vivo, u-PA activates scHGF in the liver; however, the in vivo results have not been uniformly supported by in vitro experiments. We now report that cleavage of scHGF by high-molecular-mass u-PA (abbreviated u-PA throughout) is sensitive to ionic strength. scHGF cleavage by u-PA was accelerated as the ionic strength was decreased. This result was equivalent irrespective of whether the predominant anion was chloride or acetate. Lmw-u-PA (low-molecular-mass u-PA) was ineffective at cleaving scHGF, regardless of ionic strength. Although scHGF shares homology with plasminogen, EACA (-amino-caproic acid) did not regulate u-PA-mediated scHGF cleavage. Soluble HGF receptor (MET) and soluble u-PAR (u-PA receptor) inhibited the scHGF cleavage. These results support a model in which the ability of u-PA to activate scHGF in vivo may be highly dependent on local conditions within the extracellular space.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.