Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.6.99.3 (diaphorase)
 5,903 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effects of 12-O-tetradecanoylphorbol-13-acetate (TPA), all trans-retinoic acid (RA), 5-azacytidine (5-AC), and phenobarbital (PB) on the activities of seven enzymes and/or isozymes of a diploid rat liver epithelial cell line have been studied. At 0.1 microgram/ml, TPA depressed the specific activities of lactate dehydrogenase and gamma-glutamyl transpeptidase, whereas 2 mM PB depressed gamma-glutamyl transpeptidase and alkaline phosphatase. At 0.01 microgram/ml, RA markedly depressed the activity of NADH-diaphorase and lactate dehydrogenase but enhanced the activity of alkaline phosphatase. Only 2 microM 5-AC caused the most significant shift of lactate dehydrogenase isozyme toward the "muscle"-type isozyme. Histochemical studies revealed that PB and 5-AC induced focal areas of cells with glycogen deposits, but no significant changes in either ultrastructure or alpha-fetoprotein and albumin immunohistochemical staining pattern were observed to suggest hepatocytic differentiation. Although none of the enzymatic changes could be consistently correlated with the effects of these biological modifiers on the cellular growth rate, the effect of RA on NADH-diaphorase, lactate dehydrogenase, and alkaline phosphatase activities was the opposite of the changes observed during carcinogenesis of these rat liver epithelial cells by multiple treatments with N-methyl-N'-nitro-N-nitrosoguanidine. The depression of gamma-glutamyl transpeptidase activity by PB is contradictory to that observed histochemically in hepatocytes in vivo, but such discrepancy may be related to the differences in cell type, growth conditions, or duration of exposure.
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PMID:Biochemical effects of 12-O-tetradecanoylphorbol-13-acetate, retinoic acid, phenobarbital, and 5-azacytidine on a normal rat liver epithelial cell line. 620 84

Surface-enhanced Raman spectroscopy (SERS) has exhibited great potential in protein identification and quantification. However, the poor spectral reproducibility, originating from random protein immobilization on SERS substrates, still makes it challenging for SERS to probe protein functions without any extrinsic Raman labels. Here, in our study, spacer molecules between proteins and SERS substrates are optimized for both biocompatible protein immobilization and Raman scattering enhancement. We have accordingly prepared iminodiacetic acid (IDA)-functionalized silver substrates, which are used for capturing His-tagged proteins via nickel-imidazole coordination. The controlled immobilization enables excellent SERS spectral reproducibility as evidenced by 6 polypeptides. Furthermore, the interactions between two model proteins, Erv1C (C-terminal domain of flavine adenine dinucleotide-dependent mitochondrial cytochrome c reductase Erv1) and AFP (alpha-fetoprotein), and their ligands Cyt c (cytochrome c) and ATRA (all-trans-retinoic acid) are examined, respectively. The results indicate that the IDA-functionalized silver substrates enable controlled protein immobilization and allow label-free protein function investigation by SERS. As a proof-of-concept study, the proposed functionalized SERS-active substrates combined with immobilized metal-affinity chromatography will be useful for mechanism studies on protein-ligand interactions, which is crucially important for understanding the structural basis of protein functional versatility and will contribute to the fields of drug design and biotechnology.
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PMID:Surface-Enhanced Raman Scattering for Direct Protein Function Investigation: Controlled Immobilization and Orientation. 3125 Oct 21

Vitamin B17 (VB17), also known as amygdalin and laetrile, is a type of carbohydrate occurring naturally in many plants, such as apricot kernels which have obtained a great interest in cancer therapy. This study aimed to investigate the hepatic protective potential of VB17 against Ehrlich ascites carcinoma (EAC)-bearing mice-induced liver injury, DNA damage, apoptotic P53, and PCNA alterations. A total of 100 female mice were divided into 5 groups (1st group, control group; 2nd group, VB17 group; 3rd group, EAC group; 4th group, pre-treated EAC with VB17; 5th group, co-treated EAC with VB17). Results showed that the presence of VB17 in pre-treated and co-treated groups lead to decreased DNA damage, microsomal protein, NADPH cytochrome c reductase, alpha-fetoprotein (AFP), AST, ALT, and ALP while showed increased cytochrome b5, cytochrome P450 amidopyrine N-demethylase, and aniline 4-hydroxylase compared with the EAC group. Many histopathological changes were observed in liver sections in EAC as moderate fibrosis and marked diffuse necrosis of hepatic tissue, marked inflammatory cells, and congested blood sinusoids. On the other hand, there was a moderate degree of improvement in hepatocytes in liver sections in pre-treated VB17+EAC, while a mild degree of improvement in hepatocytes, moderate cellular infiltrations, and moderate cytoplasmic vacuolization of hepatocytes in liver sections in co-treated EAC+VB17. In addition, there was a depletion in hepatic P53 and PCNA protein expression compared with the EAC group. It could be concluded that VB17 has a potential hepatoprotective effect against EAC cell-induced liver toxicity.
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PMID:Hepatic ameliorative role of vitamin B17 against Ehrlich ascites carcinoma-induced liver toxicity. 3191 66