急性膵炎早期における分子状水素の保護効果にMAPKsおよびHsc70が果たす役割
To clarify the molecular basis of H2-mediated protection against acute pancreatitis (AP), proteomic profiling of pancreatic cells identified 73 differentially expressed proteins, from which protein-protein interaction networks highlighted mitogen-activated protein kinases (MAPKs) and heat shock cognate 71 kDa protein (Hsc70) as key candidates. In vitro experiments demonstrated that H2 suppressed phosphorylation of ERK, JNK, and p38 MAPK, reduced NF-κB activation and the expression of TNF-α and IL-1β, and blocked nuclear translocation of the phosphorylated MAPK forms. Concurrently, Hsc70 expression was elevated following H2 administration. These findings were reproduced in animal models of AP. The data collectively indicate that H2 attenuates early-phase pancreatic inflammation by downregulating MAPK signaling cascades and upregulating Hsc70.
H2 inhibits phosphorylation and nuclear translocation of ERK, JNK, and p38 MAPK, thereby reducing NF-κB activation and downstream TNF-α and IL-1β expression, while simultaneously upregulating Hsc70 to dampen early inflammatory responses in acute pancreatitis.
This study combines multiple delivery routes. As a general principle, the most efficient route for routine hydrogen intake is inhalation. Inhalation carries explosion risk (empirical LFL of 10%; high-concentration devices are documented in the Consumer Affairs Agency accident database and are not recommended).
See also:
https://h2-papers.org/en/papers/26683671