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In enzymology, an IκB kinase (EC 2.7.11.10) is an enzyme that catalyzes the chemical reaction: . ATP + IκB protein ADP + IκB phosphoprotein. Thus, the two substrates of this enzyme are ATP and IκB protein, whereas its two products are ADP and IκB phosphoprotein.
This activity allows subsequent homodimerization and nuclear translocation of the IRF3 leading to transcriptional activation of pro-inflammatory and antiviral genes including IFNB. In order to establish such an antiviral state, IKBKE forms several different complexes whose composition depends on the type of cell and cellular stimuli.
IKK-β is an enzyme that serves as a protein subunit of IκB kinase, which is a component of the cytokine-activated intracellular signaling pathway involved in triggering immune responses. IKK's activity causes activation of a transcription factor known as Nuclear Transcription factor kappa-B or NF-κB.
NF-kappa-B essential modulator (NEMO) also known as inhibitor of nuclear factor kappa-B kinase subunit gamma (IKK-γ) is a protein that in humans is encoded by the IKBKG gene. NEMO is a subunit of the IκB kinase complex that activates NF-κB. [5] The human gene for IKBKG is located on the chromosome band Xq28. [6]
Inhibitor of nuclear factor kappa-B kinase subunit alpha (IKK-α) also known as IKK1 or conserved helix-loop-helix ubiquitous kinase (CHUK) is a protein kinase that in humans is encoded by the CHUK gene. [5] IKK-α is part of the IκB kinase complex that plays an important role in regulating the NF-κB transcription factor. [6]
This activity is actually inhibited by glutamate and other conditions that elevate intraneuronal calcium. In the final analysis, the role of NF-κB in neurons remains opaque due to the difficulty of measuring transcription in cells that are simultaneously identified for type.
Oxidative stress is the most powerfully specific stress activating p38 MAPK. [7] Abnormal activity (higher or lower than physiological) of p38 has been implicated in pathological stresses in several tissues, that include neuronal, [8] [9] [10] bone, [11] lung, [12] cardiac and skeletal muscle, [13] [14] red blood cells, [15] and fetal tissues. [16]
She found that kainate, a glutamate analog, elicited activation of NF-κB via the classical IkB kinase pathway and both ERK and PI3K were implicated in regulation of transcription via NF-κB in hippocampal area CA3. [6] In 2006, Lubin pursued further postdoctoral training in the lab of David Sweatt at Baylor College of Medicine. [1]