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A Kyushu University team reported that lipoic acid trisulfide (LASSS) more than doubled the binding affinity of the muscle-repair protein HGF for its receptor in laboratory experiments. The finding suggests a possible way to strengthen a signal used in muscle regeneration, but it does not show that LASSS repairs aging muscle in animals or people.

Researchers at Kyushu University in Japan found that a sulfur-containing compound called lipoic acid trisulfide (LASSS) more than doubled the binding affinity of a muscle-repair protein for its cell receptor in laboratory experiments. The result, reported in Scientific Reports, points to a possible way to strengthen a signal involved in muscle regeneration, but it does not establish that the compound can restore aging muscle in people.

The study focused on hepatocyte growth factor (HGF), a protein that helps activate satellite cells—specialized stem cells involved in repairing skeletal muscle. When HGF binds to the c-met receptor on those cells, it can prompt them to activate and take part in regeneration. The researchers examined whether chemical changes to HGF might weaken this signaling step.

The team had previously identified nitration at two locations on HGF, Y198 and Y250, both in a region involved in receptor binding. Nitration reduced the protein’s ability to connect with c-met. In the new experiments, researchers tested two compounds, glutathione trisulfide (GSSSG) and LASSS. Both reduced nitration at the examined sites, but that protection alone did not fully restore HGF binding.

When the researchers increased the amount of trisulfide relative to HGF, LASSS produced an additional effect: treated HGF showed more than twice the binding affinity for c-met compared with untreated HGF. The report also says LASSS helped limit the loss of function linked to nitration, particularly at Y198. These are laboratory findings about a protein-receptor interaction, not evidence of improved strength, mobility, or muscle repair in a living organism.

At a glance
reportWhen: Published November 4, 2026, in Scientif…
The developmentA Japanese research team found that LASSS increased HGF’s binding affinity for the c-met receptor by more than twofold in laboratory experiments.

A Stronger Signal for Muscle Repair

The result matters because muscle repair depends on signals reaching satellite cells, not simply on the presence of repair-related proteins. If age-related chemical changes make HGF less able to bind its receptor, protecting or improving that interaction could offer a research route toward understanding why regeneration becomes less effective over time.

However, the potential relevance remains preliminary. A stronger binding result in a lab assay does not show that LASSS reaches muscle tissue in the body, remains active there, or improves repair. Nor does it establish that the compound is safe or useful as a treatment. The study identifies a candidate mechanism for further investigation, rather than a ready-to-use intervention for age-related muscle loss.

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How HGF Activates Satellite Cells

Skeletal muscle can repair some damage through satellite cells, which normally remain inactive beside muscle fibers. Signals associated with injury or mechanical stimulation can release HGF from the material surrounding muscle fibers. HGF then binds c-met on satellite cells and helps activate the process that can contribute to muscle regeneration.

The researchers’ explanation centers on a possible weakening of this signal with age. As Professor Ryuichi Tatsumi described it, HGF may still be produced but can be chemically altered after it is made. The study tested whether trisulfides could affect that alteration and the protein’s receptor interaction. Its findings extend that line of laboratory research; they do not establish how much this mechanism contributes to muscle decline in people.

“HGF is not necessarily missing as we age. Rather, it can be chemically altered after it is made.”

— Professor Ryuichi Tatsumi, Kyushu University Faculty of Agriculture

From Binding Tests to Living Muscle

The reported evidence does not show whether LASSS can improve muscle regeneration in animals or humans. The supplied report describes laboratory experiments and a change in HGF’s binding affinity, but does not provide evidence of better muscle function, strength, or recovery in a whole organism. It also does not establish a safe or effective dose for people.

It remains unclear how LASSS produces the increase in binding, whether the effect holds under conditions inside muscle tissue, and whether other biological effects could limit its use. The extent to which HGF nitration contributes to age-related muscle decline also remains to be established. The finding should not be taken as evidence that supplements containing related compounds can prevent or reverse muscle loss.

Testing the Effect Beyond the Lab

The next research steps would need to determine how LASSS affects HGF and satellite-cell activity in more complex biological settings, followed by studies of muscle repair and safety in living organisms. Any later human research would need to test dose, delivery, risks, and measurable outcomes before the compound could be considered for clinical use.

The report does not specify a timetable for those studies. For now, the confirmed development is a laboratory result published in Scientific Reports: LASSS increased HGF’s binding affinity for c-met by more than twofold under the tested conditions. Whether that finding can translate into a practical approach to aging muscle repair remains open.

Key Questions

What did the researchers discover?

In laboratory experiments, LASSS-treated HGF showed more than twice the binding affinity for the c-met receptor compared with untreated HGF. HGF-c-met binding is part of a signal that helps activate muscle-repair satellite cells.

Does the study show that LASSS repairs aging muscles in people?

No. The reported finding concerns laboratory tests of protein binding. The source does not report evidence that LASSS improves muscle repair, strength, or mobility in people.

What is HGF’s role in muscle repair?

Hepatocyte growth factor (HGF) can bind to the c-met receptor on satellite cells. That interaction helps activate cells involved in skeletal-muscle regeneration.

What remains unknown about LASSS?

Researchers have not established from the reported experiments whether LASSS works in living muscle, what dose might be appropriate, or whether it is safe and effective for people. The role of HGF nitration in age-related muscle decline also needs further study.

Source: sciencedaily.com

Wellness content on this site is informational and not a substitute for professional medical guidance.
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