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Journal articles on the topic 'In vivo assay'

Author: Grafiati

Published: 4 June 2021

Last updated: 10 February 2022

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1

Hayashi, Makoto, James T. MacGregor, David G. Gatehouse, David H. Blakey, Stephen D. Dertinger, Lilianne Abramsson-Zetterberg, Gopala Krishna, et al. "In vivo erythrocyte micronucleus assay." Mutation Research/Genetic Toxicology and Environmental Mutagenesis 627, no. 1 (February 2007): 10–30. http://dx.doi.org/10.1016/j.mrgentox.2006.08.010.

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2

Kim, So-Jung, Young-Jae Chung, and Taek-Kyun Lee. "In vivo Comet Assay on Flounder and Clam Exposed to BaP and TBT." Ocean and Polar Research 33, no. 2 (June 30, 2011): 127–33. http://dx.doi.org/10.4217/opr.2011.33.2.127.

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3

Matute, Alexis, Jessica Tabart, Jean-Paul Cheramy-Bien, Claire Kevers, Jacques Dommes, Jean-Olivier Defraigne, and Joël Pincemail. "Ex Vivo Antioxidant Capacities of Fruit and Vegetable Juices. Potential In Vivo Extrapolation." Antioxidants 10, no. 5 (May 12, 2021): 770. http://dx.doi.org/10.3390/antiox10050770.

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Background: In support of claims that their products have antioxidant properties, the food industry and dietary supplement manufacturers rely solely on the in vitro determination of the ORAC (oxygen radical antioxidant capacity) value, despite its acknowledged lack of any in vivo relevance. It thus appears necessary to use tests exploiting biological materials (blood, white blood cells) capable of producing physiological free radicals, in order to evaluate more adequately the antioxidant capacities of foods such as fruit and vegetable juices. Materials: Two approaches to assessing the antioxidant capacities of 21 commercial fruit and vegetable juices were compared: the ORAC assay and the “PMA–whole blood assay,” which uses whole blood stimulated by phorbol myristate acetate to produce the superoxide anion. We described in another paper the total polyphenol contents (TPCs) and individual phenolic compound contents of all the juices were investigated. Results: Ranking of the juices from highest to lowest antioxidant capacity differed considerably according to the test used, so there was no correlation (r = 0.33, p = 0.13) between the two assays when considering all juices. Although the results of the ORAC assay correlated positively with TPC (r = 0.50, p = 0.02), a much stronger correlation (r = 0.70, p = 0.004) emerged between TPC and % superoxide anion inhibition. In the PMA–whole blood assay, peonidin-3-O-glucoside, epigallocatechin gallate, catechin, and quercetin present in juices were found to inhibit superoxide anion production at concentrations below 1 µM, with a strong positive correlation. Conclusions: Associated with the determination of total and individual phenolic compounds contained in fruit and vegetable juices, the PMA–whole blood assay appears better than the ORAC assay for evaluating juice antioxidant capacity.

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4

Simpson, David M., Edward W. Stoller, and Loyd M. Wax. "An in vivo Acetolactate Synthase Assay." Weed Technology 9, no. 1 (March 1995): 17–22. http://dx.doi.org/10.1017/s0890037x00022879.

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A method was developed and tested for in vivo assay of acetolactate synthase (ALS). The method used foliar application of 1,1-cyclopropanedicarboxylic acid (CPCA) to inhibit ketol-acid reductoisomerase, the enzyme immediately following ALS in biosynthesis of branched-chain amino acids, thereby causing accumulation of acetolactate. Since the amount of acetolactate accumulation is a function of carbon flux through ALS, quantification of acetolactate accumulation determined ALS activity. Accumulation of acetolactate in soybean leaves resulted from CPCA rates as low as 15 g/ha and occurred within 1.5 h. Accumulation rates in soybean leaflets declined with leaf age from 84 μg/h/g tissue at 3 d to 17 μg/h/g tissue at 7 d. Foliar application of CPCA also caused acetolactate accumulation in corn, grain sorghum, velvetleaf, common cocklebur, and smooth pigweed. The ability of the in vivo assay to quantify the reduction in ALS activity following applications of ALS-inhibiting herbicides was validated by comparing ALS activity following thifensulfuron application to ‘Williams 82’ soybean, which has a sulfonylurea-sensitive ALS, and ‘Asgrow 3200’ soybean, which has a sulfonylurea-insensitive ALS. Thifensulfuron reduced ALS activity in Williams 82 soybean to 0, 0.8, 3.3, and 15.6% of the CPCA control at 6, 12, 24, and 48 HAT, but ALS activity in Asgrow 3200 soybean was reduced only to 34, 40, 57, and 88% of the CPCA control.

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5

Hayashi, Makoto, Raymond R. Tice, James T. MacGregor, Diana Anderson, David H. Blakey, M. Kirsh-Volders, Frederick B. Oleson, et al. "In vivo rodent erythrocyte micronucleus assay." Mutation Research/Environmental Mutagenesis and Related Subjects 312, no. 3 (June 1994): 293–304. http://dx.doi.org/10.1016/0165-1161(94)90039-6.

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6

Spach, Colette, and Roland Motta. "In vivo eight-day ‘MLR’ assay." Journal of Immunological Methods 97, no. 2 (March 1987): 259–62. http://dx.doi.org/10.1016/0022-1759(87)90468-6.

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7

Uccellini, Melissa B., Sadaf Aslam, Sean T. H. Liu, Fahmida Alam, and Adolfo García-Sastre. "Development of a Macrophage-Based ADCC Assay." Vaccines 9, no. 6 (June 17, 2021): 660. http://dx.doi.org/10.3390/vaccines9060660.

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Fc-dependent effector functions are an important determinant of the in vivo potency of therapeutic antibodies. Effector function is determined by the combination of FcRs bound by the antibody and the cell expressing the relevant FcRs, leading to antibody-dependent cellular cytotoxicity (ADCC). A number of ADCC assays have been developed; however, they suffer from limitations in terms of throughput, reproducibility, and in vivo relevance. Existing assays measure NK cell-mediated ADCC activity; however, studies suggest that macrophages mediate the effector function of many antibodies in vivo. Here, we report the development of a macrophage-based ADCC assay that relies on luciferase expression in target cells as a measure of live cell number. In the presence of primary mouse macrophages and specific antibodies, loss of luciferase signal serves as a surrogate for ADCC-dependent killing. We show that the assay functions for a variety of mouse and human isotypes with a model antigen/antibody complex in agreement with the known effector function of the isotypes. We also use this assay to measure the activity of a number of influenza-specific antibodies and show that the assay correlates well with the known in vivo effector functions of these antibodies.

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8

Hosking, Laine, Christine Czakjo, and Sharon Choo. "Implementation of an ex vivo TH17 assay." Pathology 49 (February 2017): S43. http://dx.doi.org/10.1016/j.pathol.2016.12.102.

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9

Bertaccini, Alessandro, Catia Giovannini, Domenico Viola, Francesco Comerci, Luca Ronci, Michela Lacchini, Roberto Rusconi, Pasquale Chieco, and Giuseppe Martorana. "Telomerase assay from ex vivo prostate biopsies." European Urology Supplements 1, no. 1 (January 2002): 119. http://dx.doi.org/10.1016/s1569-9056(02)80461-4.

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10

Tang, De-chu, Adi F. Gazdar, and David P. Carbone. "In vivo cytotoxicity assay for assessing immunity." Journal of Immunological Methods 189, no. 2 (January 1996): 173–82. http://dx.doi.org/10.1016/0022-1759(95)00234-0.

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11

Simon, P., H. Ottenwälder, and H. M. Bolt. "Vinyl acetate: DNA-binding assay in vivo." Toxicology Letters 27, no. 1-3 (September 1985): 115–20. http://dx.doi.org/10.1016/0378-4274(85)90128-6.

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12

Russell, Bruce, Rossarin Suwanarusk, Céline Borlon, Fabio T. M. Costa, Cindy S. Chu, Marcus J. Rijken, Kanlaya Sriprawat, et al. "A reliable ex vivo invasion assay of human reticulocytes by Plasmodium vivax." Blood 118, no. 13 (September 29, 2011): e74-e81. http://dx.doi.org/10.1182/blood-2011-04-348748.

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AbstractCurrently, there are no reliable RBC invasion assays to guide the discovery of vaccines against Plasmodium vivax, the most prevalent malaria parasite in Asia and South America. Here we describe a protocol for an ex vivo P vivax invasion assay that can be easily deployed in laboratories located in endemic countries. The assay is based on mixing enriched cord blood reticulocytes with matured, trypsin-treated P vivax schizonts concentrated from clinical isolates. The reliability of this assay was demonstrated using a large panel of P vivax isolates freshly collected from patients in Thailand.

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13

Symonds, Jennifer M., Tomohiro Fujita, Shouhei Aoki, Kazuma Shiota, and Claire L. Kruger. "Toxicological assessment of β-galactosidase shows no adverse effects in vivo and in vitro." Toxicology Research and Application 4 (January 1, 2020): 239784732090877. http://dx.doi.org/10.1177/2397847320908776.

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A safety assessment for β-galactosidase derived from Aspergillus oryzae (GODO-FAL) was performed. The test article was a concentrated, purified β-galactosidase diluted in glycerin and water with an activity of 10,000 U/mL. A series of genotoxicology tests including micronucleus assay, chromosome aberration assay, and reverse mutagenesis (Ames) assay confirmed that GODO-FAL was not clastogenic or mutagenic at any of the concentrations used, up to 2000 µg/mL for the chromosome aberration assay and 5000 mg per plate in the Ames assay. GODO-FAL was not toxic in acute, repeated oral toxicity, and sub-chronic toxicity assays in Sprague–Dawley rats at any dose used, up to 2000 mg/kg/day. Based on results from the subchronic toxicology assay, the no observed adverse effects level for GODO-FAL was at least 2000 mg/kg/day.

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14

Unseld, Matthias, Johannes M. Breuss, Clemens Pausz, Eleonore Pablik, Gernot Schabbauer, Christoph C. Zielinski, Pavel Uhrin, and Gerald W. Prager. "In vivo Tube Assay: An Optimised Protocol of the Directed in vivo Angiogenesis Assay by Implementing Immunohistochemistry." Journal of Vascular Research 52, no. 2 (2015): 116–26. http://dx.doi.org/10.1159/000434751.

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15

Brattig, N. W., C. Timmann, R. S. Abraha, B. Lepping, B. Muller-Myhsok, and R. D. Horstmann. "Relevance of ex vivo blood lymphocyte assay for in vivo lymphocyte function." Clinical and Experimental Immunology 139, no. 1 (January 2005): 127–31. http://dx.doi.org/10.1111/j.1365-2249.2005.02667.x.

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16

Romli, Firdaus, Nadiah Abu, Faten A. Khorshid, Syed Umar Faruq Syed Najmuddin, Yeap Swee Keong, Nurul Elyani Mohamad, Muhajir Hamid, Noorjahan Banu Alitheen, and Nik Mohd Afizan Nik Abd Rahman. "The Growth Inhibitory Potential and Antimetastatic Effect of Camel Urine on Breast Cancer Cells In Vitro and In Vivo." Integrative Cancer Therapies 16, no. 4 (June 23, 2016): 540–55. http://dx.doi.org/10.1177/1534735416656051.

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Although it may sound unpleasant, camel urine has been consumed extensively for years in the Middle East as it is believed to be able to treat a wide range of diseases such as fever, cold, or even cancer. People usually take it by mixing small drops with camel milk or take it directly. The project aims to study the effects of camel urine in inhibiting the growth potential and metastatic ability of 4T1 cancer cell line in vitro and in vivo. Based on the MTT result, the cytotoxicity of camel urine against 4T1 cell was established, and it was dose-dependent. Additionally, the antimetastatic potential of camel urine was tested by running several assays such as scratch assay, migration and invasion assay, and mouse aortic ring assay with promising results in the ability of camel urine to inhibit metastatic process of the 4T1 cells. In order to fully establish camel urine’s potential, an in vivo study was carried out by treating mice inoculated with 4T1 cells with 2 different doses of camel urine. By the end of the treatment period, the tumor in both treated groups had reduced in size as compared to the control group. Additional assays such as the TUNEL assay, immunophenotyping, cytokine level detection assay, clonogenic assay, and proteome profiler demonstrated the capability of camel urine to reduce and inhibit the metastatic potential of 4T1 cells in vivo. To sum up, further study of anticancer properties of camel urine is justified, as evidenced through the in vitro and in vivo studies carried out. Better results were obtained at higher concentration of camel urine used in vivo. Apart from that, this project has laid out the mechanisms employed by the substance to inhibit the growth and the metastatic process of the 4T1 cell.

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17

Yesildal, F., FN Aydin, S. Deveci, S. Tekin, I. Aydin, R. Mammadov, O. Fermanli, F. Avcu, CH Acikel, and T. Ozgurtas. "Aspartame induces angiogenesis in vitro and in vivo models." Human & Experimental Toxicology 34, no. 3 (June 12, 2014): 260–65. http://dx.doi.org/10.1177/0960327114537535.

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Angiogenesis is the process of generating new blood vessels from preexisting vessels and is considered essential in many pathological conditions. The purpose of the present study is to evaluate the effect of aspartame on angiogenesis in vivo chick chorioallantoic membrane (CAM) and wound-healing models as well as in vitro 2,3-bis-2 H-tetrazolium-5-carboxanilide (XTT) and tube formation assays. In CAM assay, aspartame increased angiogenesis in a concentration-dependent manner. Compared with the control group, aspartame has significantly increased vessel proliferation ( p < 0.001). In addition, in vivo rat model of skin wound-healing study showed that aspartame group had better healing than control group, and this was statistically significant at p < 0.05. There was a slight proliferative effect of aspartame on human umbilical vein endothelial cells on XTT assay in vitro, but it was not statistically significant; and there was no antiangiogenic effect of aspartame on tube formation assay in vitro. These results provide evidence that aspartame induces angiogenesis in vitro and in vivo; so regular use may have undesirable effect on susceptible cases.

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18

Hao, Nan, Adrienne E. Sullivan, Keith E. Shearwin, and Ian B. Dodd. "The loopometer: a quantitative in vivo assay for DNA-looping proteins." Nucleic Acids Research 49, no. 7 (January 28, 2021): e39-e39. http://dx.doi.org/10.1093/nar/gkaa1284.

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Abstract Proteins that can bring together separate DNA sites, either on the same or on different DNA molecules, are critical for a variety of DNA-based processes. However, there are no general and technically simple assays to detect proteins capable of DNA looping in vivo nor to quantitate their in vivo looping efficiency. Here, we develop a quantitative in vivo assay for DNA-looping proteins in Escherichia coli that requires only basic DNA cloning techniques and a LacZ assay. The assay is based on loop assistance, where two binding sites for the candidate looping protein are inserted internally to a pair of operators for the E. coli LacI repressor. DNA looping between the sites shortens the effective distance between the lac operators, increasing LacI looping and strengthening its repression of a lacZ reporter gene. Analysis based on a general model for loop assistance enables quantitation of the strength of looping conferred by the protein and its binding sites. We use this ‘loopometer’ assay to measure DNA looping for a variety of bacterial and phage proteins.

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19

Miura, Daishiro. "The In Vivo Pig-a Gene Mutation Assay." Genes and Environment 36, no. 4 (2014): 169–73. http://dx.doi.org/10.3123/jemsge.2014.027.

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20

Parng, Chuenlei, Christopher Ton, Ying-Xin Lin, Nicole Marie Roy, and Patricia McGrath. "A zebrafish assay for identifying neuroprotectants in vivo." Neurotoxicology and Teratology 28, no. 4 (July 2006): 509–16. http://dx.doi.org/10.1016/j.ntt.2006.04.003.

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21

Kim, Byung Soo, Myung-Haing Cho, and Hyun Jung Kim. "Statistical analysis of in vivo rodent micronucleus assay." Mutation Research/Genetic Toxicology and Environmental Mutagenesis 469, no. 2 (September 2000): 233–41. http://dx.doi.org/10.1016/s1383-5718(00)00085-1.

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22

Schuster, Sascha, Markus Enzelberger, Harald Trauthwein, Rolf D. Schmid, and Vlada B. Urlacher. "pHluorin-Based in Vivo Assay for Hydrolase Screening." Analytical Chemistry 77, no. 9 (May 2005): 2727–32. http://dx.doi.org/10.1021/ac0486692.

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23

Miraucourt, Lois, Michael Accardi, Hai Huang, and Simon Authier. "Proof of concept comprehensive ex vivo neurological assay." Journal of Pharmacological and Toxicological Methods 99 (September 2019): 106595. http://dx.doi.org/10.1016/j.vascn.2019.05.137.

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24

Lee, Wenjau, Chi-Wei Kan, Chung-Kai Su, Kataaki Okubo, and Yoshitaka Nagahama. "Detecting xenoestrogens with an in vivo assay system." Toxicology Letters 211 (June 2012): S49—S50. http://dx.doi.org/10.1016/j.toxlet.2012.03.199.

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25

Goldberg, M. T., and P. Chidiac. "An in vivo assay for small intestine genotoxicity." Mutation Research/Environmental Mutagenesis and Related Subjects 164, no. 4 (August 1986): 209–15. http://dx.doi.org/10.1016/0165-1161(86)90055-5.

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26

Hothorn, Ludwig A., and Daniel Gerhard. "Statistical evaluation of the in vivo micronucleus assay." Archives of Toxicology 83, no. 6 (December 9, 2008): 625–34. http://dx.doi.org/10.1007/s00204-008-0393-8.

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27

Dasgupta, Amitava, Edward Kang, Margaret Olsen, Jeffrey K. Actor, and Pradip Datta. "Interference of Asian, American, and Indian (Ashwagandha) Ginsengs in Serum Digoxin Measurements by a Fluorescence Polarization Immunoassay Can Be Minimized by Using a New Enzyme-Linked Chemiluminescent Immunosorbent or Turbidimetric Assay." Archives of Pathology & Laboratory Medicine 131, no. 4 (April 1, 2007): 619–21. http://dx.doi.org/10.5858/2007-131-619-ioaaai.

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Abstract Context.—Ginsengs are widely used by the general population. These herbs interfere with serum digoxin measurement using the fluorescence polarization immunoassay. Objective.—To assess potential interference of different ginsengs (Asian, American, and Indian, also known as Ashwagandha) in vitro and in vivo in a mouse model by using a new enzyme-linked chemiluminescent immunosorbent digoxin assay and an existing turbidimetric assay. Comparisons were made with the fluorescence polarization immunoassay. Design.—Aliquots of drug-free serum pools were supplemented with ginseng and apparent digoxin concentrations were measured using enzyme-linked chemiluminescent immunosorbent digoxin assay, turbidimetric assay, and fluorescence polarization immunoassay digoxin assays. Mice were fed with different ginseng preparations and apparent digoxin concentrations were measured 1 and 3 hours later. In a separate experiment, aliquots of serum digoxin pools were further supplemented with ginsengs and the serum digoxin concentrations were measured again. Results.—A significant apparent digoxin concentration was observed both in vitro and in vivo using the fluorescence polarization immunoassay, but no apparent digoxin concentration was observed using enzyme-linked chemiluminescent immunosorbent digoxin assay and turbidimetric assay. No interference was observed with enzyme-linked chemiluminescent immunosorbent digoxin assay and turbidimetric assay when digoxin serum pools were further supplemented with various ginsengs. Conclusions.—It was concluded that both enzyme-linked chemiluminescent immunosorbent and turbidimetric digoxin assays are free from ginseng interferences.

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28

Meneses, J. O., M. V. S. do Couto, N. C. Sousa, F. dos S. Cunha, H. A. Abe, F. M. Ramos, E. C. Chagas, et al. "Efficacy of Ocimum gratissimum essential oil against the monogenean Cichlidogyrus tilapiae gill parasite of Nile tilapia." Arquivo Brasileiro de Medicina Veterinária e Zootecnia 70, no. 2 (March 2018): 497–504. http://dx.doi.org/10.1590/1678-4162-9667.

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ABSTRACT The phythotherapy is an alternative to use of chemotherapeutical agents against monogenean infection. This study evaluated the anthelmintic activity of essential oil Ocimum gratissimum against monogenean Cichlidogyrus tilapiae as well as its acute toxicity in tilapia juveniles. The mean lethal concentration (LC50) and different concentrations of the essential oil, both in vitro and in vivo assays (short and long-term baths) were assessed. The LC50 was 40.70mg.L-1 and in the in vitro assay this concentration showed 80% efficacy at the last two hours and in the in vivo assay 65.87% efficacy in long-term bath. However, it provoked morphological alterations on the gills such as hyperplasia and edema. The parasites exposure at the highest concentration (320mg.L-1) showed 100% mortality after 2h exposure in the in vitro assay, whereas in the in vivo assay, short-term baths of 5min for 3 consecutive days showed an efficacy of 87.71% without gills damage. These results demonstrate the anthelminthic activity of essential oil O. gratissimum and the safety concentration to use in Nile tilapia.

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29

Wegulo, Stephen N., and Miguel Vilchez. "Evaluation of Lisianthus Cultivars for Resistance to Botrytis cinerea." Plant Disease 91, no. 8 (August 2007): 997–1001. http://dx.doi.org/10.1094/pdis-91-8-0997.

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Lisianthus (Eustoma grandiflorum) is a high-value cut flower. However, major yield losses often result from gray mold caused by Botrytis cinerea. Various techniques were used to evaluate 12 lisianthus cultivars for resistance B. cinerea. Disease evaluations from detached leaf, leaf disc, cut stem, and in vivo growth chamber stem (GC) assays were correlated with those from an in vivo greenhouse stem (GH) assay, in which commercial greenhouse production of lisianthus was simulated. In all assays, stems or leaves were wounded before inoculation with spores or mycelia of B. cinerea. There was a significant (P ≤ 0.03) positive correlation between stem lesion length in the GH assay and disease incidence in the same assay (R = 0.74), stem lesion length from spore spray inoculation in the GC assay (R = 0.62), and percent necrosis from spore spray inoculation of detached leaves (R = 0.71). Correlations between stem lesion length in the GH assay and disease evaluations from spore drop and mycelial inoculation of detached leaves, leaf discs, and cut stems were not significant at P = 0.05. Considering only screening methods with significant correlations, ‘Magic Champagne’ was the most resistant cultivar (mean rank [mr] = 2 of 12). ‘Echo White’ and ‘Echo Lavender’ were the least resistant cultivars (mr = 11). The other cultivars were ‘Magic White’ (mr = 4); ‘Avila Ivory’, ‘Balboa Yellow’, ‘Echo Pink’, and ‘Magic Rose’ (mr = 5); ‘Balboa Blue’ (mr = 6); ‘Avila Blue Rim’ (mr = 8); and ‘Avila Purple’ and ‘Catalina Purple’ (mr = 9). The results from this study indicate that in vivo disease incidence, in vivo stem assays, and detached leaf assays, all initiated with wounding followed by spore spray inoculation, may be more reliable in evaluating lisianthus cultivars for resistance to B. cinerea than spore drop and mycelial inoculation of detached leaves, leaf discs, and cut stems. The results also indicate that lisianthus cultivars with moderate resistance to B. cinerea are commercially available. These cultivars have potential for use as germplasm in breeding lisianthus for resistance to the pathogen.

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30

Lee, Sun Young, Hee Jung Lee, Heejin Lee, Shukho Kim, Eun Hee Cho, and Heon Man Lim. "In Vivo Assay of Protein-Protein Interactions in Hin-Mediated DNA Inversion." Journal of Bacteriology 180, no. 22 (November 15, 1998): 5954–60. http://dx.doi.org/10.1128/jb.180.22.5954-5960.1998.

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ABSTRACT In order to form the catalytic nucleoprotein complex called the invertasome in the Hin-mediated DNA inversion reaction, interactions of the DNA-binding proteins Hin and Fis are required. Assays for these protein-protein interactions have been exploited with protein cross-linkers in vitro. In this study, an in vivo assay system that probes protein-protein interactions was developed. The formation of a DNA loop generated by protein interactions resulted in transcriptional repression of an artificially designed operon, which in turn increased the chance of survival of Escherichia colihost cells in a streptomycin-containing medium. Using this system, we were able to assay the Hin-Hin interaction that results in the pairing of the two recombination sites and protein interactions that result in the formation of the invertasome. This assay system also led us to find that an individual Hin dimer bound on a recombination site can form a stable complex with Fis bound on the recombinational enhancer; this finding has never been observed in in vitro studies. Possible pathways toward the formation of the invertasome are discussed based on the assay results for a previously reported Hin mutant.

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31

Lee, Eun-Gyung, and Maxine L. Linial. "Yeast Three-Hybrid Screening of Rous Sarcoma Virus Mutants with Randomly Mutagenized Minimal Packaging Signals Reveals Regions Important for Gag Interactions." Journal of Virology 74, no. 19 (October 1, 2000): 9167–74. http://dx.doi.org/10.1128/jvi.74.19.9167-9174.2000.

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ABSTRACT We previously showed that the yeast three-hybrid system provides a genetic assay of both RNA and protein components for avian retroviral RNA encapsidation. In the current study, we used this assay to precisely define cis-acting determinants involved in avian leukosis sarcoma virus packaging RNA binding to Gag protein. In vivo screening of Rous sarcoma virus mutants was performed with randomly mutated minimal packaging sequences (MΨ) made using PCR amplification after cotransformation with GagΔPR protein into yeast cells. Colonies with low β-galactosidase activity were analyzed to locate mutations in MΨ sequences affecting binding to Gag proteins. This genetic assay delineated secondary structural elements that are important for efficient RNA binding, including a single-stranded small bulge containing the initiation codon for uORF3, as well as adjacent stem structures. This implies a possible tertiary structure favoring the high-affinity binding sites for Gag. In most cases, results from the three-hybrid assay were well correlated with those from the viral RNA packaging assays. The results from random mutagenesis using the rapid three-hybrid binding assay are consistent with those from site-directed mutagenesis using in vivo packaging assays.

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32

Lee, Keyong Ho, and Ki Hyeong Rhee. "Correlative Effect between in vivo Hollow Fiber Assay and Xenografts Assay in Drug Screening." Cancer Research and Treatment 37, no. 3 (2005): 196. http://dx.doi.org/10.4143/crt.2005.37.3.196.

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33

Rainbolt, Curtis R., Donald C. Thill, Robert S. Zemetra, and Dale L. Shaner. "Imidazolinone-Resistant Wheat Acetolactate Synthase In Vivo Response to Imazamox." Weed Technology 19, no. 3 (September 2005): 539–48. http://dx.doi.org/10.1614/wt-03-215r1.1.

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Several experiments were conducted to evaluate the utility of an in vivo acetolactate synthase (ALS) assay for comparing sensitivity to imazamox among imidazolinone-resistant wheat cultivars/lines. Ten single-gene imidazolinone-resistant winter wheat cultivars/lines, one two-gene and four single-gene imidazolinone-resistant spring wheat cultivars/lines, and three pairs of heterozygous and homozygous imidazolinone-resistant winter wheat lines were evaluated in the assay experiments. Additionally, a dose-response assay was conducted to evaluate the tolerance of several imidazolinone-resistant wheat cultivars to imazamox on a whole plant level. The I50value (i.e., the imazamox dose that inhibited ALS activity by 50%) of the winter wheat cultivar ‘Above’ was 54 to 84% higher than the I50values of 99-420, 99-433, and CV-9804. However, based on the results of this study, it is unclear whether genetic background or market class (hard red winter vs. soft white winter) influences the level of ALS inhibition by imazamox. Teal 15A, the two-gene imidazolinone-resistant spring wheat cultivar, had an I50value that was two to three times greater than the I50value of the single-gene imidazolinone-resistant spring wheat cultivars/lines. The heterozygous imidazolinone-resistant wheat lines had I50values that were 69 to 81% less than the I50values of the homozygous lines. In the whole plant dose response, theR50values (i.e., the imazamox dose that reduced biomass by 50%) of the susceptible cultivars Brundage 96 and Conan were 15 to 17 times less than the homozygous single-gene imidazolinone-resistant winter and spring cultivars/lines, whoseR50values were about 1.7 times less than theR50value of the two-gene imidazolinone-resistant spring wheat line, Teal 15A. The results of the in vivo ALS imazamox assays and the whole plant imazamox dose-response assay were similar, indicating that the in vivo assay can be used to accurately and quickly compare resistance between imidazolinone-resistant wheat cultivars/lines.

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Liu, Lili, Zhiying Xu, Binbin Yu, Li Tao, and Ying Cao. "Berbamine Inhibits Cell Proliferation and Migration and Induces Cell Death of Lung Cancer Cells via Regulating c-Maf, PI3K/Akt, and MDM2-P53 Pathways." Evidence-Based Complementary and Alternative Medicine 2021 (July 8, 2021): 1–20. http://dx.doi.org/10.1155/2021/5517143.

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Berbamine (BBM) is a natural product isolated from Berberis amurensis Rupr. We investigated the influence of BBM on the cell viability, proliferation, and migration of lung cancer cells and explored the possible mechanisms. The cell viability and proliferation of lung cancer cells were evaluated by MTT assay, EdU assay, and colony formation assay. Migration and invasion abilities of cancer cells were determined through wound scratch assay and Transwell assay. Cell death was evaluated by cell death staining assay and ELISA. The expressions of proteins were evaluated using western blot assay. A xenograft mouse model derived from non-small-cell lung cancer cells was used to detect the effect of BBM on tumor growth and metastasis in vivo. Both colony formation and EdU assays results revealed that BBM (10 μM) significantly inhibited the proliferation of A549 cells ( P < 0.001 ). BBM (10 μM) also significantly inhibited the migration and invasion ability of cancer cells in wound scratch and Transwell assays. Trypan blue assay and ELISA revealed that BBM (20 μM) significantly induced cell death of A549 cells. In xenograft mouse models, the tumor volume was significantly smaller in mice treated with BBM (20 mg/kg). The western blotting assay showed that BBM inhibited the PI3K/Akt and MDM2-p53 signaling pathways, and BBM downregulated the expression of c-Maf. Our results show that BBM inhibits proliferation and metastasis and induces cell death of lung cancer cells in vitro and in vivo. These effects may be achieved by BBM reducing the expression of c-Maf and regulating the PI3K/Akt and MDM2-p53 pathways.

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35

Amano, Yuto, Hiroshi Honda, Yuko Nukada, Naohiro Ikeda, Masayuki Yamane, Koji Nakano, Akiyo Kameyama, and Osamu Morita. "Safety Pharmacological Evaluation of the Coffee Component, Caffeoylquinic Acid, and Its Metabolites, Using Ex Vivo and In Vitro Profiling Assays." Pharmaceuticals 12, no. 3 (July 17, 2019): 110. http://dx.doi.org/10.3390/ph12030110.

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Although coffee components have gained interest for use as pharmaceuticals, little is known about their safety pharmacological effects. Hence, we aimed to evaluate the safety pharmacological effects of a chlorogenic acid (CGA)-related compound contained in coffee, 5-O-caffeoylquinic acid (5-CQA), and its metabolites, 5-O-feruloylquinic acid (5-FQA), caffeic acid (CA), and ferulic acid (FA). Langendorff perfused heart assay, electrophysiological assay of acute rat hippocampal slices, and in vitro Magnus assay of gastrointestinal tracts were conducted at 1–100 µM. Moreover, in vitro profiling assays against 38 major targets were conducted. In the Langendorff assay, no significant adverse effects were observed. In the electrophysiological assay, although epileptiform discharge rates were increased at 10 µM CA with 4-aminopyridine, and area under the curve (AUC) and number of population spike were increased at 10 µM FA with bicuculline, dose dependency was not confirmed, and no significant changes were observed at 1 µM and by CGAs alone. In the Magnus assay, a slight increase in contraction activity was observed at >1 µM FA in the stomach fundi and 100 µM 5-CQA in the ileum, suggesting enterokinesis promotion. No significant interactions were observed in the in vitro profiling assays. Therefore, CGAs could have a fundamental function as safe pharmaceuticals.

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Toyoizumi, Tomoyasu, Ryo Ohta, Kumiko Kawakami, Yuzuki Nakagawa, Yoshiyuki Tazura, Makiko Kuwagata, Satoshi Noguchi, Hajime Sui, and Kohji Yamakage. "Usefulness of combined in vivo skin comet assay and in vivo skin micronucleus test." Mutation Research/Genetic Toxicology and Environmental Mutagenesis 743, no. 1-2 (March 2012): 42–51. http://dx.doi.org/10.1016/j.mrgentox.2011.12.020.

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GOMEZ‐TREVINO, M., H. BOUREAU, T. KARJALAINEN, and P. BOURLIOUX. "Clostridium difficile Adherence to Mucus: Results of an in vivo and ex vivo Assay." Microbial Ecology in Health and Disease 9, no. 6 (November 1996): 329–34. http://dx.doi.org/10.1002/(sici)1234-987x(199611)9:6<329::aid-meh329>3.3.co;2-c.

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38

Rashid, S. Z., and M. Kyo. "IN VIVO FUNCTIONAL ASSAY OF WUS ORTHOLOG IN TOBACCO." Acta Horticulturae, no. 829 (June 2009): 161–66. http://dx.doi.org/10.17660/actahortic.2009.829.23.

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39

Hayashi, Makoto. "The in vivo rodent erythrocyte micronucleus assay (automated scoring)." Toxicology 226, no. 1 (September 2006): 34–35. http://dx.doi.org/10.1016/j.tox.2006.05.053.

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40

Ly, Suw Young, Kyung Lee, Jung Ki Baek, Ung June Kang, and Seungjun Lee. "Electro Diagnostic Nerve Feeling Assay in In-Vivo Muscles." KOREA SCIENCE & ART FORUM 36 (December 31, 2018): 247–54. http://dx.doi.org/10.17548/ksaf.2018.12.30.247.

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41

Api, A. M., and R. Gudi. "An in vivo mouse micronucleus assay on musk ketone." Mutation Research/Genetic Toxicology and Environmental Mutagenesis 464, no. 2 (January 2000): 263–67. http://dx.doi.org/10.1016/s1383-5718(99)00202-8.

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42

Sarnaizul, Erdenebaatar, Gereltu Borjihan, and Sun Zhaorigetu. "The preparation and antihyperlipidaemic assay of piperlonguminine in vivo." Phytochemistry Letters 6, no. 1 (February 2013): 101–5. http://dx.doi.org/10.1016/j.phytol.2012.12.002.

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Kim, Duk Yoon, and Je Chul Lee. "Adherence Assay of UropathogenicEscherichia coliIn Vivo and In Vitro." Urogenital Tract Infection 12, no. 3 (2017): 122. http://dx.doi.org/10.14777/uti.2017.12.3.122.

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44

Hartmann, A. "Recommendations for conducting the in vivo alkaline Comet assay." Mutagenesis 18, no. 1 (January 1, 2003): 45–51. http://dx.doi.org/10.1093/mutage/18.1.45.

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45

Corkery, Dale P., Graham Dellaire, and Jason N. Berman. "Leukaemia xenotransplantation in zebrafish - chemotherapy response assay in vivo." British Journal of Haematology 153, no. 6 (April 22, 2011): 786–89. http://dx.doi.org/10.1111/j.1365-2141.2011.08661.x.

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Richardson-Harman, Nicola, Robert Parody, Peter Anton, Ian McGowan, Gustavo Doncel, Andrea Ries Thurman, Carolina Herrera, et al. "Analytical Advances in the Ex Vivo Challenge Efficacy Assay." AIDS Research and Human Retroviruses 33, no. 4 (April 2017): 395–403. http://dx.doi.org/10.1089/aid.2016.0073.

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Maxwell, Karen L., Anthony K. Mittermaier, Julie D. Forman-Kay, and Alan R. Davidson. "A simple in vivo assay for increased protein solubility." Protein Science 8, no. 9 (1999): 1908–11. http://dx.doi.org/10.1110/ps.8.9.1908.

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Rizzo, Larissa Y., Susanne K. Golombek, Marianne E. Mertens, Yu Pan, Dominic Laaf, Janine Broda, Jabadurai Jayapaul, et al. "In vivo nanotoxicity testing using the zebrafish embryo assay." Journal of Materials Chemistry B 1, no. 32 (2013): 3918. http://dx.doi.org/10.1039/c3tb20528b.

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Butler, Scott L., Mark S. T. Hansen, and Frederic D. Bushman. "A quantitative assay for HIV DNA integration in vivo." Nature Medicine 7, no. 5 (May 2001): 631–34. http://dx.doi.org/10.1038/87979.

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Rezzola, Sara, Mirella Belleri, Domenico Ribatti, Ciro Costagliola, Marco Presta, and Francesco Semeraro. "A novel ex vivo murine retina angiogenesis (EMRA) assay." Experimental Eye Research 112 (July 2013): 51–56. http://dx.doi.org/10.1016/j.exer.2013.04.014.

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