Disease relevance of Firefly luciferin

• Both Cypridina luciferin analog-dependent chemiluminescence and luminol-dependent chemiluminescence were significantly decreased in neutrophils from patients with chronic liver disease (hepatocellular carcinoma < cirrhosis < chronic active hepatitis) when they were compared with normal healthy subjects [1].
• The activities of antioxidant enzymes and of luciferase in the prothorax (bright) and abdomen (dim) of luminous larval Pyrearinus termitilluminans (Coleoptera: Elateridae) were measured after previous challenge with either hyperoxia, hypoxia, or the firefly luciferase inhibitor luciferin 6'-methyl ether (LME) [2].
• An intensified charge coupled device video camera was used to noninvasively image luciferase-expressing human prostate tumors and metastases in nude mice, after ip inoculation of luciferin [3].
• The bioluminescent reaction of adenosine 5'-triphosphate (ATP) with luciferin and luciferase has been used in conjunction with a sensitive photometer (Lab-Line's ATP photometer) to detect significant bacteriuria in urine [4].
• Overexpression of the apoaequorin cDNA in E. coli now provides the means of obtaining gram quantities of a single isotype of the protein which can be converted to aequorin in the presence of coelenterate luciferin, oxygen and an appropriate thiol [5].

Psychiatry related information on Firefly luciferin

• Luciferin treatment and anesthesia during imaging did not adversely affect circadian rhythms in locomotor activity [6].

High impact information on Firefly luciferin

• The rates of ATP synthesis and hydrolysis were measured with the luciferin/luciferase assay after an acid-base transition at different [ATP]/([ADP][P(i)]) ratios as a function of deltapH, analysing the range from the ATP synthesis to the ATP hydrolysis direction and the deltapH at equilibrium, deltapH (eq) (zero net rate), was determined [7].
• This evidence regarding the origins of luciferin in Cnidaria has implications for the evolution of bioluminescence and for the extensive use of coelenterazine among marine organisms [8].
• Synaptolucins were targeted to synaptic vesicles and, upon exocytosis, formed light-emitting complexes with their cognate luciferin, which was added to the extracellular medium [9].
• The marine ostracod Vargula hilgendorfii ejects luciferin and luciferase into seawater to produce a bright luminous cloud [10].
• Photoprotein luciferin is identical to Renilla luciferin with respect to reaction kinetics and bioluminescence spectral distribution [11].

Chemical compound and disease context of Firefly luciferin

• DEX pretreatment (25muM, 48h) significantly increased CYP3A7-catalyzed luciferin 6' benzylether O-debenzylation, but had no effect on alachlor toxicity [12].

Biological context of Firefly luciferin

• Cell viability was measured on the basis of lactate dehydrogenase release, and ATP was quantitated with a luciferin/luciferase assay [13].
• Furthermore, there were significant positive correlations between albumin/prothrombin time and Cypridina luciferin analog-dependent chemiluminescence/luminol-dependent chemiluminescence [1].
• Local and systemic induction of two defense-related subtilisin-like protease promoters in transgenic Arabidopsis plants. Luciferin induction of PR gene expression [14].
• Also, we report that luciferin, the substrate for the reporter luciferase (LUC) gene, is able to activate expression of PR genes, and this may pose a problem when using this gene reporter system in studies related to plant defense [14].
• These criteria included determination of the efficiency of infection/transfection of various viral and nonviral delivery systems, promoter specificity, and visualization of luciferase activity, and of the ability of luciferin to reach various organs [15].

Anatomical context of Firefly luciferin

• We measured ATP flow (using the luciferin/luciferase method) through these channels after reconstitution into planar phospholipid membranes [16].
• At a substrate concentration of 0.01 mM, the peak luminescence from the cos cells expressing luciferase was up to 6-fold greater with the esters than with unmodified luciferin [17].
• Several measures of energy conservation, namely ADP/O ratio, P/O ratio, ATP/O ratio and phosphorylation detected by continuous assay with purified firefly luciferase and luciferin, all show phosphorylation can occur with mung-bean mitochondria at cyanide concentrations sufficient to inhibit the cytochrome oxidase system [18].
• Single isolated rat hepatocytes were injected with the ATP-dependent luminescent protein firefly luciferase, and then superfused with 45 microM luciferin in air-equilibrated medium [19].
• The atractyloside-insensitive accumulation of adenine nucleotides by rat liver mitochondria (as opposed to the exchange-diffusion catalysed by the adenine nucleotide translocase) has been measured by using the luciferin/luciferase assay as well as by measuring [14C]ATP uptake [20].

Associations of Firefly luciferin with other chemical compounds

• Although there were not significant correlations between glutamic pyruvic transaminase and Cypridina luciferin analog-dependent chemiluminescence/luminol-dependent chemiluminescence, there were significant negative correlations between total bilirubin and Cypridina luciferin analog-dependent chemiluminescence/luminol-dependent chemiluminescence [1].
• Oxyluciferin, a luminescence product of firefly luciferase, is enzymatically regenerated into luciferin [21].
• Oxygen radicals were measured as chemiluminescence amplified by a luciferin analog [Cypridina luciferin analog-dependent chemiluminescence (CLA-DCL), which is dependent on O2- generation] and luminol (L)-DCL, which is highly dependent on OCl- generation) in response to formyl-methonyl-leucyl-phenylalanine [22].
• Here we show that COS-7 cells transfected with a luciferase expression vector accumulate up to 0.5 mM adenine-containing dinucleoside tetraphosphates (Ap4N) during the 24 h following luciferin addition [23].
• When angiotensin II was added on aortic segments in the presence of Cypridina luciferin analog, immediate elevations of chemiluminescence were observed which were inhibited by SOD [24].

Gene context of Firefly luciferin

• Induction of CYP3A4 protein was examined by measuring catalytic activity with the CYP3A4 substrate, luciferin 6' benzyl ether (luciferin BE) [25].
• Myeloperoxidase activity was assayed by a chemiluminescence method, using a cypridina luciferin analog as a chemiluminescence probe, after extraction from peripheral human polymorphonuclear leukocytes [26].
• A Ca2+-triggered luciferin-binding protein (BP-LH2) from the bioluminescent marine coelenterate, Renilla reniformis, has been purified by conventional methods [27].
• The luciferin is protected from autoxidation by binding to LBP, and one luciferin is bound per dimer at alkaline pH (Ka approximately 5 x 10(7) M-1) [28].
• Injection of luciferin in these mice causes full-body bioluminescence, which can be detected using a low-light CCD camera [29].

Analytical, diagnostic and therapeutic context of Firefly luciferin

• The concentrations of RBC-derived ADP measured in the medium after shear, as determined by both high pressure liquid chromatography and the luciferin/luciferase system, were within the range of concentrations of ADP which may trigger PAG or potentiate PAG induced by low concentrations of other platelet agonists in the aggregometer [30].
• Bioluminescence of lesions was noninvasively imaged after intravenous or intraperitoneal injection of luciferin [29].
• Molecular cloning and genomic organization of a gene for luciferin-binding protein from the dinoflagellate Gonyaulax polyedra [31].
• As a new application of this reaction in confocal microscopy, we monitored luciferin fluorescence as a sign of ATP release by single acini [32].
• Autoxidation leads to concomitant decreases in the 390-nm absorbance, 474-nm fluorescence, and biological activity; similar changes occurred with oxidation by K3Fe(CN)6, thus allowing a quantitation of luciferin by titration [33].

References