Super-HGF: Kyushu University modifies growth factor HGF

Researchers at Kyushu University in Japan, led by Professor Ryuichi Tatsumi, found a compound that protects hepatocyte growth factor (HGF) from chemical modification and increases its binding to a cell receptor, NUR.KZ reported on 5 November 2026, citing ScienceDaily. nur.kz The results were published in Scientific Reports. nur.kz

HGF is a signaling protein that triggers the division of quiescent muscle satellite cells. It is released under mechanical load or tissue damage and binds the c-met receptor, which starts the regeneration of muscle fibers. nur.kz

Nitration of HGF with age

With age, the protein undergoes chemical modification: nitration at the critical positions Y198 and Y250. nur.kz This disrupts its structure; the authors compare it to a deformed key that no longer fits the receptor lock. nur.kz

To prevent the damage, the group tested sulfur trisulfide compounds with strong antioxidant properties: glutathione trisulfide (GSSSG) and lipoic acid trisulfide (LASSS). nur.kz

Super-HGF and tests in mice

In the experiments, LASSS at a molar ratio of 1:8000 neutralized nitration and also caused a subtle rearrangement of the three-dimensional structure of the molecule. nur.kz The resulting modified form, named “Super-HGF” by the authors, bound to the c-met receptor more than twice as efficiently as the natural protein. nur.kz

The protective effect was also confirmed in experiments on mice with muscle atrophy. nur.kz The researchers hope that the finding will help develop a therapy for sarcopenia in older people and in patients with low mobility. The material does not report tests in humans.

Kyushu University: Super-HGF, a modified growth factor, binds c-met over twice as well; effect seen in mice

Nitration of HGF with age

Super-HGF and tests in mice

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