Anti-inflammatory drugs degradation during LED-UV 365 photolysis of free chlorine: roles of reactive oxidative species and formation of disinfection by-products
ight-emitting diode (LED) which are environmentally friendly with longer life compared to traditional mercury lamp. This study investigated the anti-inflammatory drugs non-steroidal (NSAIDs) – phenacetin (PNT) and acetaminophen (ACT) – the deletion for LED-UV (365 nm) photolysis of free available chlorine (FAC). PNT degradation and ACT for LED-UV365 / FAC treatment at pH 5.5 to 8.5 followed pseudo-first-order kinetics. The presence of hydroxyl radicals (OH ·), reactive chlorine species (RCS), and ozone (O3, change of O (3P)) filtered by using a scavenger ethanol (EtOH), tert-butanol (TBA), and 3- Buten-2ol, and 4-hydroxy-2,2,6,6-tetramethylpiperidine (TEMP), and is measured by the kinetics of competition with probing compound nitrobenzene (NB), benzoic acid (BA), 1,4-dimethoxybenzene (Dmob). Higher pH will cause a decrease ·
OH contribution and increased contribution to the PNT and ACT FAC degradation. It has been determined that the contribution of PNT and ACT O3 degradation of less than 5% for all pH, and O3 (P) react to EtOH with second-order constant of 1.52 × 109 M-1s-1. LED-UV365 / FAC system reduces the formation of five typical CX3-R type of disinfection by-products (DBPs) as well as cytotoxicity and genotoxicity of water samples at pH 5.5 and 8.5, compared with FAC alone.
A decrease in the formation of DBPs resulting from the rapid decomposition of the irradiation LED FAC-UV365. A decent reaction path forming DBPs in LED-systems UV365 / FAC checked by density functional theory (DFT). To decay FAC for LED-UV365 / FAC effluents from waste water, in 15 minutes the rest of the FAC was 0.8 mg / L (lower than the limit of 0.2 mg / L) after the initial FAC was 2.0 mg / L. the results showed that more testing on the balance of the pollutant removal efficiency targets, FAC residual and fees should be explored in a system of LED-UV365 / FAC for the application.
Anti-Cancer Effect of 3-Hydroxy-β-Ionone Identified from Moringa oleifera Lam. Man leaves 15 squamous cell carcinoma cells
Squamous cell carcinoma is the most common type of cancer worldwide head and neck. Radiation and chemotherapy common treatment for patients; However, these drugs can have side effects and tumors develop drug resistance. effective treatments still require improvements for cancer patients. Here, we examined the effects of anti-cancer properties of Moringa oleifera (MO) Lam.
leaf extract and its fractions, 3-hydroxy-β-ionone in SCC15 cells. SCC15 treated with and without MO leaf extract and its fractions. MTT assay was used to determine cell viability in SCC15. cell cycle and apoptosis was evaluated by Muse ™ cell analyzer. colony formation and wound closure SCC15 analysis conducted in 6-well plates.
Description: Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Nucleosomes consist of approximately 146 bp of DNA wrapped around a histone octamer composed of pairs of each of the four core histones (H2A, H2B, H3, and H4). The chromatin fiber is further compacted through the interaction of a linker histone, H1, with the DNA between the nucleosomes to form higher order chromatin structures. This gene is intronless and encodes a replication-dependent histone that is a member of the histone H3 family. Transcripts from this gene lack polyA tails; instead, they contain a palindromic termination element. This gene is located separately from the other H3 genes that are in the histone gene cluster on chromosome 6p22-p21.3.
Description: Most cell types express three sizes of receptors for TGF-beta. These are designated Type I (53 kDa), Type II (70 - 85 kDa), and Type III (250 - 350 kDa). The Type I receptor is a membrane-bound serine/threonine kinase that apparently requires the presence of the Type II receptor to bind TGF-beta. The Type II receptor is also a membrane-bound serine/threonine kinase that binds TGF-beta1 and TGF-beta 3 with high affinity and TGF-beta 2 with much lower affinity. The Type I and Type II receptors together form a heterodimeric signaling complex that is essential for the transduction of the anti-proliferative signals of TGF-beta. The Type III receptor is a transmembrane proteoglycan with a large extracellular domain and a 43 amino acid residue cytoplasmic domain. The cytoplasmic domain of the Type III receptor lacks an obvious signaling motif and the receptor may not be involved directly in signal transduction.
Description: CD120b is a 75 kD type I transmembrane protein, also known as Tumor Necrosis Factor Receptor Type II (TNFRII) or p75. It is expressed on a variety of cells at low levels; the expression is upregulated upon activation. This receptor binds both TNF- α and β.
Description: cAMP-dependent protein kinase type II-alpha regulatory subunit is an enzyme that in humans is encoded by the PRKAR2A gene. cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the cAMP-dependent Protein Kinase, more commonly called Protein Kinase A (PKA), which transduces the signal through phosphorylation of different target proteins. The inactive holoenzyme of PKA is a tetramer composed of two regulatory and two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. Four different regulatory subunits and three catalytic subunits of PKA have been identified in humans. The protein encoded by this gene is one of the regulatory subunits. This subunit can be phosphorylated by the activated catalytic subunit. It may interact with various A-kinase anchoring proteins (AKAPs) and determine the subcellular localization of PKA. This subunit has been shown to regulate protein transport from endosomes to the Golgi apparatus and further to the endoplasmic reticulum (ER).
Description: Most cell types express three sizes of receptors for TGF-beta. These are designated Type I (53 kDa), Type II (70 - 85 kDa), and Type III (250 - 350 kDa). The Type I receptor is a membrane-bound serine/threonine kinase that apparently requires the presence of the Type II receptor to bind TGF-beta. The Type II receptor is also a membrane-bound serine/threonine kinase that binds TGF-beta1 and TGF-beta 3 with high affinity and TGF-beta 2 with much lower affinity. The Type I and Type II receptors together form a heterodimeric signaling complex that is essential for the transduction of the anti-proliferative signals of TGF-beta. The Type III receptor is a transmembrane proteoglycan with a large extracellular domain and a 43 amino acid residue cytoplasmic domain. The cytoplasmic domain of the Type III receptor lacks an obvious signaling motif and the receptor may not be involved directly in signal transduction.
Description: The Interleukin 1 receptor family comprises at least nine members. All family members possess three immunoglobulin (Ig)-like domains in their extracellular region. Most members also have an intracellular TIR (Toll-like receptor/IL-1 receptor) signaling domain that is also conserved in the Toll-like receptor family. A subtype of the IL-1 R family, SIGIRR (single Ig domain-containing IL-1 R-related molecule) differs from the other nine members by having only one Ig domain. IL-1 R1 is a type I transmembrane glycoprotein that functions as the ligand binding subunit in the IL-1 receptor complex. It associates with a signaling component, IL-1 R3 (IL-1 receptor accessory protein) to form a functional receptor complex for IL-1 alpha and IL-1 beta.
Description: The Interleukin 1 receptor family comprises at least nine members. All family members possess three immunoglobulin (Ig)-like domains in their extracellular region. Most members also have an intracellular TIR (Toll-like receptor/IL-1 receptor) signaling domain that is also conserved in the Toll-like receptor family. A subtype of the IL-1 R family, SIGIRR (single Ig domain-containing IL-1 R-related molecule) differs from the other nine members by having only one Ig domain. IL-1 Rrp2, also known as IL-1 R6, is a transmembrane protein belonging to the IL-1 receptor family. It is a ligand binding subunit that associates with IL-1 RAcP to form a functional receptor complex for IL-1F6, IL-1F8, and IL-1F9.
Description: The Interleukin 1 receptor family comprises at least nine members. All family members possess three immunoglobulin (Ig)-like domains in their extracellular region. Most members also have an intracellular TIR (Toll-like receptor/IL-1 receptor) signaling domain that is also conserved in the Toll-like receptor family. A subtype of the IL-1 R family, SIGIRR (single Ig domain-containing IL-1 R-related molecule) differs from the other nine members by having only one Ig domain. Interleukin 1 receptor accessory protein-like 1 (IL-1 RAPL1), also known as IL-1 R8, Oligophenin-4 (OPHN4) and three immunoglobulin domain containing IL-1 receptor-related 2 (TIGIRR-2), is a member of the IL-1 receptor superfamily.
Description: IL-1 is a name that designates two proteins, IL-1 alpha and IL-1 beta, that are the products of distinct genes, but recognize the same cell surface receptors. IL-1 alpha and IL-1 beta are structurally related polypeptides that show approximately 25% homology at the amino acid level. Both proteins are produced by a wide variety of cells in response to stimuli such as those produced by inflammatory agents, infections, or microbial endotoxins.
Description: IL-1 is a name that designates two proteins, IL-1 alpha and IL-1 beta, that are the products of distinct genes, but recognize the same cell surface receptors. IL-1 alpha and IL-1 beta are structurally related polypeptides that show approximately 25% homology at the amino acid level. Both proteins are produced by a wide variety of cells in response to stimuli such as those produced by inflammatory agents, infections, or microbial endotoxins.
Description: Interleukin-1 beta (IL-1beta) is produced by activated macrophages. IL-1beta stimulates thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, and fibroblast growth factor activity. IL-1beta proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells. IL-1 is a name that designates two pleiotropic cytokines, IL-1 alpha (IL1F1) and IL1 beta (IL1F2), which are the products of distinct genes. IL- 1alpha and IL-1 beta are structurally related polypeptides that share approximately 21% amino acid (aa) identity in human. Both proteins are produced by a wide variety of cells in response to inflammatory agents, infections, or microbial endotoxins. While IL-1 alpha and IL-1 beta are regulated independently, they bind to the same receptor and exert identical biological effects.The human IL-1 beta cDNA encodes a 269 aa precursor. A 116 aa propeptide is cleaved intracellularly by the cysteine protease IL-1 beta converting enzyme (Caspase1/ICE) to generate the active cytokine. The mature human IL-1 beta shares 96% aa sequence identity with rhesus and 67% 78% with canine, cotton rat, equine, feline, mouse, porcine, and rat IL-1 beta.
Description: IL-1α is a non-secreted proinflammatory cytokine produced in a variety of cells including monocytes, tissue macrophages, keratinocytes and other epithelial cells. Both IL-1α and IL-1β binds to the same receptor and has similar if not identical biological properties. These cytokines have a broad range of activities including, stimulation of thymocyte proliferation, by inducing IL-2 release, B-cell maturation and proliferation, mitogenic FGF-like activity and the ability to stimulate the release of prostaglandin and collagenase from synovial cells. However, whereas IL-1β is a secreted cytokine, IL-1α is predominantly a cell-associated cytokine. Recombinant human IL-1α is an 18.0 kDa protein containing 159 amino acid residues.
Description: IL-1α is a non-secreted proinflammatory cytokine produced in a variety of cells including monocytes, tissue macrophages, keratinocytes and other epithelial cells. Both IL-1α and IL-1β binds to the same receptor and has similar if not identical biological properties. These cytokines have a broad range of activities including, stimulation of thymocyte proliferation, by inducing IL-2 release, B-cell maturation and proliferation, mitogenic FGF-like activity and the ability to stimulate the release of prostaglandin and collagenase from synovial cells. However, whereas IL-1β is a secreted cytokine, IL-1α is predominantly a cell-associated cytokine. Recombinant human IL-1α is an 18.0 kDa protein containing 159 amino acid residues.
Description: IL1α and IL1β are both synthesized as 31 kDa precursors that are subsequently cleaved into proteins with molecular weights of approximately 17,000 Da. Neither precursor contains a typical hydrophobic signal peptide sequence and most of the precursor form of IL1α remains in the cytosol of cells, although there is evidence for a membranebound form of the precursor form of IL1α. The IL1α precursor reportedly shows full biological activity in the EL4 assay. Among various species, the amino acid sequence of mature IL 1α is conserved 60% to 70% and human IL1 has been found to be biologically active on murine cell lines. Both forms of IL1 bind to the same receptors, designated type I and type II. Evidence suggests that only the type I receptor is capable of signal transduction and that the type II receptor may function as a decoy, binding IL1 and thus preventing binding of IL1 to the type I receptor.
Description: IFN-alpha/beta R2, also known as IFNAR2, is a 100 kDa component of the class II cytokine receptor that binds the type I interferons IFN-alpha, IFN-beta, and IFN-omega. IFN-alpha/beta R2 associates with the 125 kDa IFN-alpha/beta R1 component to form a receptor complex that transmits antiviral and antiproliferative signals. Down-regulation of the receptor is accomplished by ubiquitination and degradation. A soluble form of the protein, corresponding to the extracellular ligand-binding domain, is generated by alternative splicing.
Description: Interleukin-18 (IL-18) is a proinflammatory cytokine in the IL-1 family that exerts distinct immune effects depending on the local cytokine environment. It is expressed as a 24 kDa precursor by endothelial and epithelial cells, keratinocytes, gamma δT cells, and phagocytes. The precursor is activated intracellularly by Caspase-1 mediated proteolysis to release the 17 kDa mature cytokine. The precursor can also be released by necrotic cells for extracellular cleavage by multiple proteases. IL-18 activation is induced by infection or tissue damage and contributes to disease pathology in chronic inflammation. IL-18 binds to the widely expressed IL-18 R alpha which recruits IL-18 R beta to form the signaling receptor complex. Its bioactivity is negatively regulated by interactions with IL-18 binding proteins and virally encoded IL-18BP homologs.
Description: IL-1 receptor antagonist (IL-1ra) was originally isolated from the urine of patients with monocytic leukemia and has also been purified from adherent monocytes. The protein shows 26% amino acid homology to IL-1 beta and 19% homology to IL-1 alpha. It will compete with either factor for receptor binding, but does not interact with either one. Human IL-1ra will bind to both types of IL-1 receptor (I and II) on human cells. In mouse, IL-1RII does not bind IL-1ra.
Apoptotic markers were evaluated by immunoblotting. We found that an extract of moringa and 3-HBI significantly inhibit proliferation of SCC15. In addition, they induced apoptosis and cell cycle arrest in G2 / M phase in SCC15 compared with untreated controls. MO extract and 3-HBI also inhibit the colony formation and cell migration SCC15. In addition, we observed upregulation of cleaved caspase-3 and Bax with downregulation of anti-apoptotic Bcl-2, which shows the induction of apoptosis of cancer cells. Our results show that extracts of MO and 3-HBI supplied anti-cancer properties by inhibiting the progression and induce apoptosis of SCC15.