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(2005) 8(6A):67394
The nonenzymatic functions of GSTs involve their interactions with cellular proteins, such as, Jun N-terminal kinase,(JNK), tumor necrosis factor receptor-associated factor-2 (TRAF2), apoptosis-signal-regulating kinase 1 (ASK), serine/threonine kinases (PKA, PKC), and tissue transglutaminase 2 (TGM2), during which, either the interacting protein partner undergoes functional alteration or the GST protein itself is post-translationally modified and/or functionally altered [53], [74]
These combined modifications reduce IGF-1 LR3's binding affinity for IGFBPs by approximately 100-1000 fold compared to native IGF-1, meaning that a much higher proportion of IGF-1 LR3 exists in the free, bioactive state capable of directly engaging IGF-1 receptors on target cells
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