α2-Macroglobulin Activators consist of a range of chemical compounds that underpin the enhancement of α2-Macroglobulin's activity through different biochemical mechanisms. Epigallocatechin gallate (EGCG) and curcumin bolster α2-Macroglobulin by tempering the NF-κB pathway, which results in an indirect upsurge in its anti-inflammatory action. Resveratrol augments the protein's activity by enlisting SIRT1, leading to increased antioxidant defense, while Trolox, through its antioxidative capacity, buttresses α2-Macroglobulin's activity by mitigating oxidative stress. Ascorbic acid contributes to the maintenance of α2-Macroglobulin, ensuring its protease inhibition capability is uncompromised. Retinoic acid, via modulation of immune-related gene expression, and zinc sulfate, through its role as a structural cofactor, both serve to reinforce the protein's protease regulatory function. Selenium is pivotal in maintaining the protein's structure, thereby enhancing its binding affinity to proteases and cytokines.
Furthermore, N-Acetylcysteine (NAC) indirectly supports α2-Macroglobulin's protease inhibitory role by amplifying cellular antioxidative defenses. Silymarin ensures the protein's activity by shielding it from oxidative damage, thereby preserving its protease inhibition capacity. Likewise, lipoic acid sustains α2-Macroglobulin's activity by maintaining a reduced intracellular environment conducive to its function. Omega-3 fatty acids like EPA and DHA modulate cellular membrane composition and signaling processes, which could lead to a heightened expression or stability of α2-Macroglobulin. Through these varied but convergent mechanisms, these activators collectively enhance the functional activity of α2-Macroglobulin, ensuring its efficacy in its role as a protease inhibitor and mediator of the immune response without necessitating a direct increase in gene expression or translation.
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