Live·Open questions in longevity research
All targets

Enzyme

Mast-cell chymase

An extracellular mast-cell enzyme whose catalytic sites are shared by substance P and VIP

Hypotheses on this target 1

Mast-cell chymaseInhibition. Hypotheses on this target 11Activation. Hypotheses on this target 0Lower level. Hypotheses on this target 0Higher level. Hypotheses on this target 0Replacement. Hypotheses on this target 0Protection from degradation. Hypotheses on this target 0Cofactor removal. Hypotheses on this target 0Synthesis suppression. Hypotheses on this target 0Function preservation. Hypotheses on this target 0
  • Inhibition1
  • Activation
  • Lower level
  • Higher level
  • Replacement
  • Protection from degradation
  • Cofactor removal
  • Synthesis suppression
  • Function preservation

Inhibition1

  • Suppressing substance P speeds loss of a vessel-relaxing peptide and reduces pressure tolerance

    Where this hypothesis actsSkin interstitial space, where substance P and VIP compete at physiological concentrations

    What is proposedLimit VIP access to chymase catalytic sites through substrate competition

    With whatProtein or peptide as the agent

    HowIntroduce a catalytically competitive substrate with no relevant neuronal or vascular receptor activity, subject to validation at physiological concentrations

    Possible resultPossible restoration of VIP persistence and pressure tolerance without restoring substance P signaling

    2026-09-21