Updated
Updated · Earth.com · Aug 1
Kyushu University Finds LASSS Doubles HGF Binding, Shielding Muscle-Repair Signal
Updated
Updated · Earth.com · Aug 1

Kyushu University Finds LASSS Doubles HGF Binding, Shielding Muscle-Repair Signal

1 articles · Updated · Earth.com · Aug 1

Summary

  • LASSS restored nitrated HGF and, at an 8,000-to-1 dose ratio, made it bind the c-met receptor more than twice as strongly as undamaged HGF in lab tests.
  • The finding targets a repair failure seen with aging: HGF remains abundant but nitration at Y198 and Y250 blocks its docking to c-met, leaving satellite cells dormant.
  • Filtered samples kept the binding boost after excess LASSS was removed, suggesting the trisulfide alters HGF itself rather than acting only as an antioxidant; GSSSG and ordinary lipoic acid did not replicate the effect.
  • In young male mice given LASSS in drinking water for 3 days before 5 days of tail suspension, nitrated HGF accumulated in untreated calf muscle but not in the LASSS group.
  • The study, published in Scientific Reports, stops short of showing therapeutic benefit: it used 3 to 4 mice per group, measured nitration rather than strength, and has not yet tested aged animals or sarcopenia.

Insights

Could a simple sulfur compound be the key to unlocking super HGF and reversing age-related muscle decline?
If this compound permanently alters muscle repair proteins, what are the hidden risks of supercharging cellular regeneration?