Activators of KRTAP10-3 work primarily through pathways that modulate intracellular second messengers, particularly cyclic adenosine monophosphate (cAMP). When cAMP levels are elevated in the cell, it leads to the activation of a series of transcription factors, notably CREB (cAMP response element-binding protein). This has a direct impact on the expression levels of KRTAP10-3, as CREB binds to response elements in the DNA to enhance transcription. Certain activators increase cAMP by directly stimulating adenylate cyclase or by mimicking cAMP itself, which allows them to bypass the cell membrane and activate cAMP-dependent pathways from within. Others exert their effect by preventing the degradation of cAMP, thereby sustaining the activation of these pathways over a longer period.
The modulation of KRTAP10-3 is also influenced by the inhibition of phosphodiesterases, enzymes responsible for cAMP degradation. By inhibiting these enzymes, activators effectively raise the intracellular levels of cAMP, which indirectly leads to increased expression of KRTAP10-3 through prolonged CREB activation. Some activators even influence the activity of kinase enzymes, leading to a cascade of phosphorylation events that further ensure the activation of transcription factors involved in the expression of KRTAP10-3. Other activators impact G protein-coupled receptors, leading to increased intracellular cAMP and subsequent activation of the pathways that culminate in the upregulation of KRTAP10-3 expression.
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