Background: Glyoxal (GO) and methylglyoxal (MGO) is among the majority of the toxic compounds emitted by electronic cigarettes (e-cigarettes) and cigarette smoke tobacco regularly. respiratory diseases presented mucus over production as their main pathophysiologic features. However, the effects of GO and MGO in pro-inflammatory cytokines and mucin expression in human nasal epithelial cells, as well as the underlying signaling pathway, has not been studied.
Objective: This study was to determine whether the GO and MGO induce pro-inflammatory cytokines, and expression of MUC5AC / 5B via MAPK (MAPK) and nuclear factor-kappa-light-chain-enhancer activated B cells (NF kB) signaling pathway.
Methods: The effect of GO and MGO in pro-inflammatory cytokines, mucins expression and signaling pathways of GO and MGO were investigated using enzyme immunoassay water-soluble tetrazolium salt-1, and immunoblot analysis with specific inhibitors and small interfering RNA.
Results: GO and MGO did not affect cell viability up to 2 mM in human nasal epithelial cells. GO and MGO increased production of pro-inflammatory such as interleukin (IL) -1β and IL-6) and MUC5AC / 5B. In addition, GO and MGO was significantly activated extracellular signal-regulated kinase 1/2 (ERK1 / 2), p38 MAPK and NF-kB. Do ERK1 / 2, p38 MAPK and NF-kB signaling pathway involved in the GO and MGO-induced production of pro-inflammatory cytokines (IL-1β and IL-6) and MUC5AC / 5B, we used specific inhibitors and siRNA transfection. This is significantly suppressed Go and MGO-induced expression of pro-inflammatory cytokines (IL-1β and IL-6) and MUC5AC / 5B.
Conclusions: GO and MGO-induced pro-inflammatory cytokines and expression of MUC5AC / 5B through ERK1 / 2, p38 MAPK and NF-kB in human nasal epithelial cells. These results indicate that GO and MGO may be involved in airway diseases related to hypersecretion of mucus.
Glyoxal and Methylglyoxal as E-cigarette Vapor Ingredients-Induced Pro-Inflammatory Cytokine and Mucins Expression in Human Nasal Epithelial Cells
Acyclic Triterpenoid Isolated from Alpinia katsumadai Relieves Chronic Formalin-Induced Rat Paw Inflammation by Inhibiting the phosphorylation of ERK and NF-kB
Chronic and excessive inflammation can damage organs and cause a host of inflammatory diseases such as inflammatory bowel disease, asthma, and rheumatoid arthritis. In this study, we investigated the anti-inflammatory effects of Alpinia katsumadai derived seed-pentahydroxy 2,3,5,22,23-2,6,10,15,19,23-hexamethyl-tetracosa-6,10,14, 18-tetraene (IPM) using lipopolysaccharide (LPS) -stimulated J774 cells and chronic foot rat model of formalin-induced inflammation. In vitro results showed that PHT showed no cytotoxicity and decreased LPS-induced NO secretion.
In addition, PHT inhibit LPS-induced inducible NO synthase (iNOS) and cyclooxygenase 2 expression (COX2) protein. Quantitative real-time PCR results showed that PHT downregulated gene expression of proinflammatory cytokine interleukin-1β (IL-1β) and interleukin-6 (IL-6) but not tumor necrosis factor α (TNF-α). IPM inhibit LPS-induced phosphorylation of extracellular signal-regulated kinase (ERK) and nuclear factor of kappa light chain enhancer activated B cells (NF-kB). In the mouse model, oral administration of 50 mg / kg PHT significantly reduced both the thickness and volume of mouse feet.
These results indicate that IPM has potential anti-inflammatory effects and should be considered as a possible functional material.Human podocytes (HPC) plays an important role in the pathogenesis of kidney disease. In this context, angiotensin II (Ang II) and nuclear factor kappa-light-chain-enhancer activated B cells (NF) plays an important role in Podosit injury.
Description: A polyclonal antibody against Phospho-RELA (Ser281). Recognizes Phospho-RELA (Ser281) from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, WB;WB:1:500-1:1000
Description: NF-kappa-B is a ubiquitous transcription factor involved in several biological processes. It is held in the cytoplasm in an inactive state by specific inhibitors. Upon degradation of the inhibitor| NF-kappa-B moves to the nucleus and activates transcription of specific genes. NF-kappa-B is composed of NFKB1 or NFKB2 bound to either REL| RELA| or RELB. The most abundant form of NF-kappa-B is NFKB1 complexed with the product of this gene| RELA. Four transcript variants encoding different isoforms have been found for this gene.
Description: NF-kappa-B is a ubiquitous transcription factor involved in several biological processes. It is held in the cytoplasm in an inactive state by specific inhibitors. Upon degradation of the inhibitor| NF-kappa-B moves to the nucleus and activates transcription of specific genes. NF-kappa-B is composed of NFKB1 or NFKB2 bound to either REL| RELA| or RELB. The most abundant form of NF-kappa-B is NFKB1 complexed with the product of this gene| RELA. Four transcript variants encoding different isoforms have been found for this gene.
Description: NF-kappa-B is a ubiquitous transcription factor involved in several biological processes. It is held in the cytoplasm in an inactive state by specific inhibitors. Upon degradation of the inhibitor| NF-kappa-B moves to the nucleus and activates transcription of specific genes. NF-kappa-B is composed of NFKB1 or NFKB2 bound to either REL| RELA| or RELB. The most abundant form of NF-kappa-B is NFKB1 complexed with the product of this gene| RELA. Four transcript variants encoding different isoforms have been found for this gene.
Description: A polyclonal antibody for detection of NF?B-p65 phospho Ser281) from Human, Mouse, Rat. This NF?B-p65 phospho Ser281) antibody is for IHC-P, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from human NF?B-p65 around the phosphorylation site of S281
Description: A polyclonal antibody for detection of NF?B-p65 phospho Ser281) from Human, Mouse, Rat. This NF?B-p65 phospho Ser281) antibody is for IHC-P, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from human NF?B-p65 around the phosphorylation site of S281
Description: A polyclonal antibody for detection of NF?B-p65 phospho Ser281) from Human, Mouse, Rat. This NF?B-p65 phospho Ser281) antibody is for IHC-P, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from human NF?B-p65 around the phosphorylation site of S281
Description: The protein encoded by this gene is a member of the serine/threonine kinase family. This kinase contains a SH3 domain and a leucine zipper-basic motif. This kinase preferentially activates MAPK8/JNK kinase| and functions as a positive regulator of JNK signaling pathway. This kinase can directly phosphorylate| and activates IkappaB kinase alpha and beta| and is found to be involved in the transcription activity of NF-kappaB mediated by Rho family GTPases and CDC42.
Description: The protein encoded by this gene is a member of the serine/threonine kinase family. This kinase contains a SH3 domain and a leucine zipper-basic motif. This kinase preferentially activates MAPK8/JNK kinase| and functions as a positive regulator of JNK signaling pathway. This kinase can directly phosphorylate| and activates IkappaB kinase alpha and beta| and is found to be involved in the transcription activity of NF-kappaB mediated by Rho family GTPases and CDC42.
Description: The protein encoded by this gene is a member of the serine/threonine kinase family. This kinase contains a SH3 domain and a leucine zipper-basic motif. This kinase preferentially activates MAPK8/JNK kinase| and functions as a positive regulator of JNK signaling pathway. This kinase can directly phosphorylate| and activates IkappaB kinase alpha and beta| and is found to be involved in the transcription activity of NF-kappaB mediated by Rho family GTPases and CDC42.
More recently, transmembrane proteins (Tmem) 63C, a member of Tmem-family found to be expressed in the kidney and associated with Podosit function. In this study, we analyzed the expression and regulation of functional Tmem63c impact on cell viability and apoptosis in HPC in the context of activation of Ang II.
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