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Nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor, alpha

This gene encodes a member of the NF-kappa-B inhibitor family, which contain multiple ankrin repeat domains. The encoded protein interacts with REL dimers to inhibit NF-kappa-B/REL complexes which are involved in inflammatory responses. The encoded protein moves between the cytoplasm and the nucleus via a nuclear localization signal and CRM1-mediated nuclear export. Mutations in this gene have been found in ectodermal dysplasia anhidrotic with T-cell immunodeficiency autosomal dominant disease. [provided by RefSeq, Aug 2011] (from NCBI)
Top mentioned proteins: NF-kappaB, p65, V1a, CAN, IL-1beta
Papers on IkappaBalpha
[Qinghuachang Decoction Inhibited NF-kappaB Activation in LPS-induced Human Enterocytes].
Speerra et al., In Zhongguo Zhong Xi Yi Jie He Za Zhi, Nov 2015
Expressions of inhibitory Kaba protein (IkappaB-alpha), phosphorylated inhibitory Kaba protein (p-lkappaB-alpha), nuclear transcription factor p50 (p50), and nuclear transcription factor ReIA (ReIA) protein were determined by Western blot.
Relationship between irradiation-induced neuro-inflammatory environments and impaired cognitive function in the developing brain of mice.
Cheng et al., Wuhan, China. In Int J Radiat Biol, Mar 2015
The cytoplasm to nuclei translocation of Nuclear factor kappa B (NF-κB), and the protein expressions of IkappaB-alpha (IκB-α), NF-κB essential modulator (NEMO), p53-induced protein with a death domain (PIDD), TNF-α and IL-1β were examined by Western blotting.
Seabuckthron (Hippophae rhamnoides L.) leaf extract ameliorates the gamma radiation mediated DNA damage and hepatic alterations.
Dey et al., In Indian J Exp Biol, 2014
The lipid peroxidation, liver function enzymes, expression of phosphorylated NFkappaB (p65) and IkappaBalpha increased whereas the endogenous antioxidants diminished upon radiation exposure compared to control.
[Serumimmunological study of moxibustion on helicobacter pylori gastritis in rats].
Lin et al., In Zhongguo Zhen Jiu, 2014
HE staining microscopic examination was used to observe inflammation severity in gastric mucosa, and enzyme-linked immunosorbent assay (ELISA) was adapted to measure content of heat shock protein (HSP) 72, TNF-alpha and IL-1beta, and real-time quantitative PCR was used to measure the expression of TLR2 mRNA, TLR4 mRNA, CD14 mRNA and MyD88 mRNA in peripheral blood mononuclear cells, and western blot method was used to measure content of NFkappaB and IkappaBalpha in peripheral blood mononuclear cells.
The response of porcine monocyte derived macrophages and dendritic cells to Salmonella Typhimurium and lipopolysaccharide.
Volf et al., Brno, Czech Republic. In Bmc Vet Res, 2013
Thirteen out of 22 up-regulated genes contained the NF-kappaB binding site in their promoters and could be considered as either part of the NF-kappaB feedback loop (IkappaBalpha and ISG15) or as NF-kappaB targets (IL1beta, IL1alpha, AMCF2, IL8, SOD2, CD14, CD48, OPN, OLDLR1, HMOX1 and VCAM1).
NEMO ensures signaling specificity of the pleiotropic IKKβ by directing its kinase activity toward IκBα.
Hoffmann et al., San Diego, United States. In Mol Cell, 2012
Data show that NEMO forms a complex with IKKbeta and IkappaBalpha.
Activation of IKK/NF-κB provokes renal inflammatory responses in guanylyl cyclase/natriuretic peptide receptor-A gene-knockout mice.
Pandey et al., New Orleans, United States. In Physiol Genomics, 2012
The consequences of the disruption of Npr1 gene on proinflammatory responses of nuclear factor kappa B, inhibitory kappa B kinase, and inhibitory kappa B alpha (NF-kappaB, IKK, IkappaBalpha) in the kidneys of mutant mice, was determined.
Blockade of the nuclear factor-κB pathway in the endothelium prevents insulin resistance and prolongs life spans.
Katagiri et al., Sendai, Japan. In Circulation, 2012
The endothelium plays important roles in obesity- and age-related disorders through intracellular NF-kappaB signaling, thereby ultimately affecting life span.
Blocking autophagy prevents bortezomib-induced NF-κB activation by reducing I-κBα degradation in lymphoma cells.
Gribben et al., London, United Kingdom. In Plos One, 2011
bortezomib-induced autophagy confers relative DLBCL cell drug resistance by eliminating I-kappaBalpha.
Effects of NFKB1 and NFKBIA gene polymorphisms on susceptibility to environmental factors and the clinicopathologic development of oral cancer.
Chien et al., T'ai-chung-shih, Taiwan. In Plos One, 2011
Our results suggest that NFKB1 -94 ATTG2, NFKBIA -826 T, and -881 G alleles are associated with oral carcinogenesis
Interleukin-6 signaling in liver-parenchymal cells suppresses hepatic inflammation and improves systemic insulin action.
Brüning et al., Köln, Germany. In Cell Metab, 2010
Surprisingly, hepatic IL-6Ralpha-disruption caused an exaggerated inflammatory response during euglycemic hyperinsulinemic clamp analysis, as revealed by increased expression of IL-6, TNF-alpha, and IL-10, as well as enhanced activation of inflammatory signaling such as phosphorylation of IkappaBalpha.
IkappaBbeta acts to inhibit and activate gene expression during the inflammatory response.
Ghosh et al., New Haven, United States. In Nature, 2010
Although cells lacking IkappaBbeta have been reported, in vivo studies have been limited and suggested redundancy between IkappaBalpha and IkappaBbeta.
Polyphenols from red wine are potent modulators of innate and adaptive immune responsiveness.
Jirillo et al., Bari, Italy. In Proc Nutr Soc, 2010
We have also provided evidence that Negromaro polyphenols are able to activate extracellular regulated kinase and p38 kinase and switch off the NF-kappaB pathway via an increased expression with time of the IkappaBalpha phosphorylated form.
Sphingosine-1-phosphate is a missing cofactor for the E3 ubiquitin ligase TRAF2.
Spiegel et al., Richmond, United States. In Nature, 2010
Here we show that SphK1 and the production of S1P is necessary for lysine-63-linked polyubiquitination of RIP1, phosphorylation of IkappaB kinase and IkappaBalpha, and IkappaBalpha degradation, leading to NF-kappaB activation.
Molecular targets of [6]-gingerol: Its potential roles in cancer chemoprevention.
Azeez et al., Ibadan, Nigeria. In Biofactors, 2010
It could decrease inducible nitric oxide synthase (iNOS) and tumor necrosis factor alpha (TNF-alpha) expression through suppression of I-kappaB alpha (IkappaBalpha) phosphorylation, nuclear factor kappa B (NF-kappaB) nuclear translocation.
Ubiquitination and degradation of the inhibitors of NF-kappaB.
Ben-Neriah et al., Jerusalem, Israel. In Cold Spring Harb Perspect Biol, 2010
The signal is eventually terminated through nuclear expulsion of NF-kappaB, the outcome of a negative feedback loop based on IkappaBalpha transcription, synthesis, and IkappaBalpha-dependent nuclear export of NF-kappaB (Karin and Ben-Neriah 2000).
Regulation of NF-kappaB inhibitor IkappaBalpha and viral replication by a KSHV microRNA.
Gao et al., San Antonio, United States. In Nat Cell Biol, 2010
The miRNA cluster regulates the NF-kappaB pathway by reducing expression of IkappaBalpha protein, an inhibitor of NF-kappaB complexes.
A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKgamma to dampen the host NF-kappaB-mediated inflammatory response.
Sasakawa et al., Tokyo, Japan. In Nat Cell Biol, 2010
NF-kappaB (nuclear factor kappaB) has a pivotal role in many cellular processes, including the inflammatory and immune responses and, therefore, its activation is tightly regulated by the IKK (IkappaB kinase) complex and by IkappaBalpha degradation.
Regulation of IkappaBalpha function and NF-kappaB signaling: AEBP1 is a novel proinflammatory mediator in macrophages.
Ro et al., Ukraine. In Mediators Inflamm, 2009
The structure, function, and regulation of the NF-kappaB inhibitors, IkappaBalpha and IkappaBbeta, are reviewed.
Interleukin-1 (IL-1) pathway.
Kracht et al., Gießen, Germany. In Sci Signal, 2009
In response to ligand binding of the receptor, a complex sequence of combinatorial phosphorylation and ubiquitination events results in activation of nuclear factor kappaB signaling and the JNK and p38 mitogen-activated protein kinase pathways, which, cooperatively, induce the expression of canonical IL-1 target genes (such as IL-6, IL-8, MCP-1, COX-2, IkappaBalpha, IL-1alpha, IL-1beta, MKP-1) by transcriptional and posttranscriptional mechanisms.
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