Kyushu: LASSS more than doubles HGF muscle-repair binding
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- Ryuichi Tatsumi of Kyushu University led a team that found lipoic acid trisulfide (LASSS) more than doubles HGF's ability to bind c-met receptors — creating what the researchers call a 'Super HGF' form.
- The researchers tested two trisulfide compounds at a 1:8000 HGF-to-trisulfide ratio, and only LASSS produced the enhanced binding; glutathione trisulfide (GSSSG) reduced nitration but did not boost receptor connection.
- The study, published July 24, 2026 in Scientific Reports, targets a specific aging mechanism: HGF undergoes nitration at sites Y198 and Y250, which prevents the protein from activating satellite cells that rebuild muscle.
- Tatsumi's team hypothesizes LASSS induces a structural change in HGF rather than simply acting as an antioxidant, since the protein became both stronger-binding and more resistant to nitration damage.
- In mice with tail-suspension-induced muscle atrophy, those pretreated with LASSS had significantly lower HGF nitration levels than untreated mice — the first in vivo confirmation beyond laboratory protein experiments.
- The researchers stress additional aging-animal studies are still required to confirm safety and efficacy before any human trials; the team suggests the approach could eventually extend to humans, cats, and dogs.
Why it matters: Age-related muscle loss threatens strength and independence in older adults; the researchers stress LASSS still needs aging-animal safety studies before human trials can begin, but a compound that more than doubles HGF receptor binding gives drug developers a concrete molecular handle on the problem.
