Unbound glucocorticoids cross cell membranes and bind with high affinity to specific cytoplasmic receptors, modifying transcription and protein synthesis. By this mechanism, glucocorticoids can inhibit leukocyte infiltration at the site of inflammation, interfere with mediators of inflammatory response, and suppress humoral immune responses. The anti-inflammatory actions of corticosteroids are thought to involve phospholipase A2 inhibitory proteins, lipocortins, which control the biosynthesis of potent mediators of inflammation such as prostaglandins and leukotrienes.
AB - The chicken ovalbumin gene is subject to multihormonal regulation. Maximal expression of it requires not only the synergistic effects of estrogen and corticosterone, but also the permissive effects of insulin. In addition to effects on transcription, the stability of its message is greatly enhanced by estrogen. Furthermore, two signal transduction pathways involving protein kinases have been implicated in the regulation of the ovalbumin gene. To better define the role of second messengers on expression of the ovalbumin gene, the effects of the protein kinase-C (PKC) and the cAMP-dependent protein kinase (PKA) pathways on the endogenous levels of ovalbumin mRNA and the transcription of an ovalbumin fusion gene were investigated. Primary cultures of oviduct cells were treated with phorbol 12-myristilate 13-acetate (an activator of PKC) or with forskolin and 3-isobutyl-1-methylxanthine (an activator of PKA) alone, activators plus estrogen and corticosterone, or activators plus both steroids and insulin. The results indicate that phorbol 12-myristilate 13-acetate causes a dramatic destabilization of ovalbumin message, resulting in a reduction in ovalbumin mRNA levels. In contrast, the activators of the PKA system can substitute for insulin and, thereby, increase expression of the ovalbumin gene synergistically with the steroids. The effect of the activators of the PKA system is at the level of transcription. Thus, in chicken oviduct cell cultures, the PKA and PKC signal transduction pathways act in opposing ways to modulate the steroid-induced expression of the ovalbumin gene.
With respect to recognition and long term memories, corticosterone has variable effects. Studies show that the modification of certain chemical and brain processes that affect corticosterone levels can also impact stress effects on memory. In studies on rats, the fluctuations of corticosterone concentration are shown to prevent stress’ impairment of recognition memory in lower amounts. These lower levels seem to be linked to the rescue of stress-induced attenuation of CA1 long-term potentiation .  When researchers looked at stress effects on LTM, they found many outcomes. In multiple studies, the formation of LTM (tested 24 h later) was found to be enhanced by corticosterone in some studies, while the persistence of LTM (tested at least 1 wk later) was only assisted by corticosterone in the late phase of memory consolidation and reconsolidation .   Stress facilitates the consolidation but disrupts the reconsolidation of emotional memory. As mentioned previously, the persistence of LTM is selectively enhanced when stress and corticosterone are administered during the late phase after acquisition, but it is disrupted when stress and corticosterone are administered during the late phase after retrieval of memory.  With regards to the persistence of LTM, there is a restricted time window between acquisition or retrieval where persistence is affected. These studies found that while persistence of LTM is selectively affected based on stage of memory, the formation of LTM is left intact after a certain length of time. Up to this point, studies have not agreed as to whether or not these processes are dependent on corticosterone or what even happens based on corticosterone in these processes and how memory is ultimately affected.